|
Name |
Accession |
Description |
Interval |
E-value |
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
7-1379 |
0e+00 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 2713.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 7 WIEKLDNPTLSVLPHDFLRPQQEPYTkQATYSLQLPQLDVPHDSFSNKYAVALSVWAALIYRVTGDDDIVLYIANNK--- 83
Cdd:TIGR03443 2 WSERLDNPTLSVLPHDYLRPANNRLV-EATYSLQLPSAEVTAGGGSTPFIILLAAFAALVYRLTGDEDIVLGTSSNKsgr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 84 --ILRFNIQPTWSFNELYSTINNELNKLNSIEaNFSFDELAEKIQSCQDLERTPQLFRLAFLENQDFKLDEF-KHHLVDF 160
Cdd:TIGR03443 81 pfVLRLNITPELSFLQLYAKVSEEEKEGASDI-GVPFDELSEHIQAAKKLERTPPLFRLAFQDAPDNQQTTYsTGSTTDL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 161 ALNLDTSNNAHVLNLIYNSLLYSNERVTIVADQFTQYLTAALSDPSNCITKISLITASSKDSLPDPTKNLGWCDFVGCIH 240
Cdd:TIGR03443 160 TVFLTPSSPELELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPDEPIGKVSLITPSQKSLLPDPTKDLDWSGFRGAIH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 241 DIFQDNAEAFPERTCVVETPTL--NSDKSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAG 318
Cdd:TIGR03443 240 DIFADNAEKHPDRTCVVETPSFldPSSKTRSFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 319 ATFSVIDPAYPPARQTIYLGVAKPRGLIVIRAAGQLDQLVEDYINDELEIVSRINSIAIQENGTIEGGKLDNGE-DVLAP 397
Cdd:TIGR03443 320 ATFSVIDPAYPPARQTIYLSVAKPRALIVIEKAGTLDQLVRDYIDKELELRTEIPALALQDDGSLVGGSLEGGEtDVLAP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 398 YDHYKDTRTGVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFNWMSKRFNLTENDKFTMLSGIAHDPIQRDMFTPLF 477
Cdd:TIGR03443 400 YQALKDTPTGVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFGLSENDKFTMLSGIAHDPIQRDMFTPLF 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 478 LGAQLYVPTQDDIGTPGRLAEWMSKYGCTVTHLTPAMGQLLTAQATTPFPKLHHAFFVGDILTKRDCLRLQTLAENCRIV 557
Cdd:TIGR03443 480 LGAQLLVPTADDIGTPGRLAEWMAKYGATVTHLTPAMGQLLSAQATTPIPSLHHAFFVGDILTKRDCLRLQTLAENVCIV 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 558 NMYGTTETQRAVSYFEVKSKNDDPNFLKKLKDVMPAGKGMLNVQLLVVNRNDRTQICGIGEIGEIYVRAGGLAEGYRGLP 637
Cdd:TIGR03443 560 NMYGTTETQRAVSYFEIPSRSSDSTFLKNLKDVMPAGKGMKNVQLLVVNRNDRTQTCGVGEVGEIYVRAGGLAEGYLGLP 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 638 ELNKEKFVNNWFVEKDHWNYLDKDNGEPWRQFWLGPRDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTH 717
Cdd:TIGR03443 640 ELNAEKFVNNWFVDPSHWIDLDKENNKPEREFWLGPRDRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTH 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 718 ISQHPLVRENITLVRKNADNEPTLITFMVPRfDKPDDLSKFQSDVPKEVETDPIVKGLIGYHLLSKDIRTFLKKRLASYA 797
Cdd:TIGR03443 720 LSQHPLVRENVTLVRRDKDEEPTLVSYIVPQ-DKSDELEEFKSEVDDEESSDPVVKGLIKYRKLIKDIREYLKKKLPSYA 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 798 MPSLIVVMDKLPLNPNGKVDKPKLQFPTPKQLNLVAENTVSETDDSQFTNVEREVRDLWLSILPTKPASVSPDDSFFDLG 877
Cdd:TIGR03443 799 IPTVIVPLKKLPLNPNGKVDKPALPFPDTAQLAAVAKNRSASAADEEFTETEREIRDLWLELLPNRPATISPDDSFFDLG 878
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 878 GHSILATKMIFTLKKKLQVDLPLGTIFKYPTIKAFAAEIDRIKSSG-----GSSQGEVVENV-TANYAEDAKKLVETLPS 951
Cdd:TIGR03443 879 GHSILATRMIFELRKKLNVELPLGLIFKSPTIKGFAKEVDRLKKGEeladeGDSEIEEEETVlELDYAKDAKTLVDSLPK 958
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 952 SYPSREyfvepnSAEGKTTINVFVTGVTGFLGSYILADLLGRSpKNYSFKVFAHVRAKDEEAAFARLQKAGITYGTWNEK 1031
Cdd:TIGR03443 959 SYPSRK------ELDASTPITVFLTGATGFLGSFILRDLLTRR-SNSNFKVFAHVRAKSEEAGLERLRKTGTTYGIWDEE 1031
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 1032 FASNIKVVLGDLSKSQFGLSDEKWMDLANTVDIIIHNGALVHWVYPYAKLRDPNVISTINVMSLAAVGKPKFFDFVSSTS 1111
Cdd:TIGR03443 1032 WASRIEVVLGDLSKEKFGLSDEKWSDLTNEVDVIIHNGALVHWVYPYSKLRDANVIGTINVLNLCAEGKAKQFSFVSSTS 1111
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 1112 TLDTEYYFNLSDKLVSEGKPGILESDDLMNSASGLTGGYGQSKWAAEYIIRRAGERGLRGCIVRPGYVTGASANGSSNTD 1191
Cdd:TIGR03443 1112 ALDTEYYVNLSDELVQAGGAGIPESDDLMGSSKGLGTGYGQSKWVAEYIIREAGKRGLRGCIVRPGYVTGDSKTGATNTD 1191
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 1192 DFLLRFLKGSVQLGKIPDIENSVNMVPVDHVARVVVATSLNPPKENELAVAQVTGHPRILFKDYLYTLHDYGYDVEIESY 1271
Cdd:TIGR03443 1192 DFLLRMLKGCIQLGLIPNINNTVNMVPVDHVARVVVAAALNPPKESELAVAHVTGHPRIRFNDFLGTLKTYGYDVEIVDY 1271
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 1272 SKWKKSLEASVIDRNEENALYPLLHMVLDNLPESTKAPELDDRNAVASLKKDTAWTGVDWSNGIGVTPEEVGIYIAFLNK 1351
Cdd:TIGR03443 1272 VHWRKSLERFVIERSEDNALFPLLHFVLDDLPQSTKAPELDDTNAATSLKADAAWTGVDVSSGAGVTEEQIGIYIAYLVK 1351
|
1370 1380
....*....|....*....|....*...
gi 6319591 1352 VGFLPPPTHNDKLPLPSIELTQAQISLV 1379
Cdd:TIGR03443 1352 VGFLPAPTKTGALPLPKIEISEAQLKLI 1379
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
250-824 |
0e+00 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 1121.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 250 FPERTCVVETPTLNSDKSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFSVIDPAYP 329
Cdd:cd17647 1 FPERTCVVETPSLNSSKTRSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 330 PARQTIYLGVAKPRGLIVIRAAGqldqlvedyindeleivsrinsiaiqengtieggkldngedvlapydhykdtrtgVV 409
Cdd:cd17647 81 PARQNIYLGVAKPRGLIVIRAAG-------------------------------------------------------VV 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 410 VGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFNWMSKRFNLTENDKFTMLSGIAHDPIQRDMFTPLFLGAQLYVPTQDD 489
Cdd:cd17647 106 VGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTQDD 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 490 IGTPGRLAEWMSKYGCTVTHLTPAMGQLLTAQATTPFPKLHHAFFVGDILTKRDCLRLQTLAENCRIVNMYGTTETQRAV 569
Cdd:cd17647 186 IGTPGRLAEWMAKYGATVTHLTPAMGQLLTAQATTPFPKLHHAFFVGDILTKRDCLRLQTLAENVRIVNMYGTTETQRAV 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 570 SYFEVKSKNDDPNFLKKLKDVMPAGKGMLNVQLLVVNRNDRTQICGIGEIGEIYVRAGGLAEGYRGLPELNKEKFVNNWF 649
Cdd:cd17647 266 SYFEVPSRSSDPTFLKNLKDVMPAGRGMLNVQLLVVNRNDRTQICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNWF 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 650 VEKDHWNYLDKDNGEPWRQFWLGPRDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENIT 729
Cdd:cd17647 346 VEPDHWNYLDKDNNEPWRQFWLGPRDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENIT 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 730 LVRKNADNEPTLITFMVPRFDKPDDLSKFQSDVPKEVETDPIVKGLIGYHLLSKDIRTFLKKRLASYAMPSLIVVMDKLP 809
Cdd:cd17647 426 LVRRDKDEEPTLVSYIVPRFDKPDDESFAQEDVPKEVSTDPIVKGLIGYRKLIKDIREFLKKRLASYAIPSLIVVLDKLP 505
|
570
....*....|....*
gi 6319591 810 LNPNGKVDKPKLQFP 824
Cdd:cd17647 506 LNPNGKVDKPKLQFP 520
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
251-821 |
1.56e-146 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 452.75 E-value: 1.56e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 251 PERTCVVetptlnsDKSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFSVIDPAYPP 330
Cdd:cd05930 1 PDAVAVV-------DGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 331 ARQTIYLGVAKPrgliviraagqldqlvedyindeleivsrinsiaiqengtieggKLdngedvlapydhykdtrtgVVV 410
Cdd:cd05930 74 ERLAYILEDSGA--------------------------------------------KL-------------------VLT 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 411 GPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFNWMSKRFNLTENDKFTMLSGIAHDPIQRDMFTPLFLGAQLYVPTQDDI 490
Cdd:cd05930 91 DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVR 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 491 GTPGRLAEWMSKYGCTVTHLTPAMGQLLTAQAT-TPFPKLHHAFFVGDILTKRDCLRLQTLAENCRIVNMYGTTETQRAV 569
Cdd:cd05930 171 KDPEALADLLAEEGITVLHLTPSLLRLLLQELElAALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDA 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 570 SYFEVKSKNDDPnflkklkDVMPAGKGMLNVQLLVVNRNDrtQICGIGEIGEIYVRAGGLAEGYRGLPELNKEKFVNNWF 649
Cdd:cd05930 251 TYYRVPPDDEED-------GRVPIGRPIPNTRVYVLDENL--RPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPF 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 650 vekdhwnyldkdngepwrqfwlGPRDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENIT 729
Cdd:cd05930 322 ----------------------GPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAV 379
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 730 LVRKNADNEPTLITFMVPRFDKPDDLSkfqsdvpkevetdpivkgligyhllskDIRTFLKKRLASYAMPSLIVVMDKLP 809
Cdd:cd05930 380 VAREDGDGEKRLVAYVVPDEGGELDEE---------------------------ELRAHLAERLPDYMVPSAFVVLDALP 432
|
570
....*....|..
gi 6319591 810 LNPNGKVDKPKL 821
Cdd:cd05930 433 LTPNGKVDRKAL 444
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
7-932 |
1.60e-134 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 447.77 E-value: 1.60e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 7 WIEKLDN-PTLSVLPHDFLRPQQEPYTkQATYSLQLP-----QLDvphdSFSNK-----YAVALSVWAALIYRVTGDDDI 75
Cdd:COG1020 211 WRQQLAGlPPLLELPTDRPRPAVQSYR-GARVSFRLPaeltaALR----ALARRhgvtlFMVLLAAFALLLARYSGQDDV 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 76 VL-----------------YIANNKILRFNIQPTWSFNELYSTINNELnkLNSIE-ANFSFDELAEKIQSCQDLERTPqL 137
Cdd:COG1020 286 VVgtpvagrprpeleglvgFFVNTLPLRVDLSGDPSFAELLARVRETL--LAAYAhQDLPFERLVEELQPERDLSRNP-L 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 138 FRLAF-LENQDFKLDEFKHHLV------------DFALNLDTSNNAHVLNLIYNSLLYSNERVTIVADQFTQYLTAALSD 204
Cdd:COG1020 363 FQVMFvLQNAPADELELPGLTLepleldsgtakfDLTLTVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAAD 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 205 PSNCITKISLITASSKDSL-----------PDPTknlgwcdfvgCIHDIFQDNAEAFPERTCVVetptlnsDKSRSFTYR 273
Cdd:COG1020 443 PDQPLGDLPLLTAAERQQLlaewnataapyPADA----------TLHELFEAQAARTPDAVAVV-------FGDQSLTYA 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 274 DINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFSVIDPAYPPARQTIYLGVAKPRglIVIRAAGQ 353
Cdd:COG1020 506 ELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGAR--LVLTQSAL 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 354 LDQLVEDyindELEIVSrinsiaiqengtieggkLDNGEDVLAPydhykDTRTGVVVGPDSnptLS---FTSGSEGIPKG 430
Cdd:COG1020 584 AARLPEL----GVPVLA-----------------LDALALAAEP-----ATNPPVPVTPDD---LAyviYTSGSTGRPKG 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 431 VLGRHFSLAYYFNWMSKRFNLTENDKFTMLSGIAHDPIQRDMFTPLFLGAQLYVPTQDDIGTPGRLAEWMSKYGCTVTHL 510
Cdd:COG1020 635 VMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNL 714
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 511 TPAMGQLLTAQATTPFPKLHHAFFVGDILTKRDCLRLQTLAENCRIVNMYGTTETQRAVSYFEVKSKNDDPnflkklkDV 590
Cdd:COG1020 715 TPSLLRALLDAAPEALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYYEVTPPDADG-------GS 787
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 591 MPAGKGMLNVQLLVVNRNDrtQICGIGEIGEIYVrAG-GLAEGYRGLPELNKEKFVNNWFVEkdhwnyldkdngepwrqf 669
Cdd:COG1020 788 VPIGRPIANTRVYVLDAHL--QPVPVGVPGELYI-GGaGLARGYLNRPELTAERFVADPFGF------------------ 846
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 670 wlgPRDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRKNADNEPTLITFMVPRF 749
Cdd:COG1020 847 ---PGARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEA 923
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 750 DKPDDLSkfqsdvpkevetdpivkgligyhllskDIRTFLKKRLASYAMPSLIVVMDKLPLNPNGKVDKPKLQFPTPkql 829
Cdd:COG1020 924 GAAAAAA---------------------------LLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAA--- 973
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 830 nlvaenTVSETDDSQFTNVEREVRDLWLSILPtkPASVSPDDSFFDLGGHSILATKMIFTLKKKLQVDLPLGTIFKYPTI 909
Cdd:COG1020 974 ------AAAAAAAAPPAEEEEEEAALALLLLL--VVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAA 1045
|
970 980
....*....|....*....|...
gi 6319591 910 KAFAAEIDRIKSSGGSSQGEVVE 932
Cdd:COG1020 1046 AAAAAAAAAAAAAAAAPLAAAAA 1068
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
271-728 |
5.05e-123 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 388.93 E-value: 5.05e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 271 TYRDINRTSNIVAHYLIKT-GIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFSVIDPAYPPARQTIYLGVAKPRGLIVIR 349
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 350 --AAGQLDQLVEDYINDELEIVSrinsiaiqengtieggkLDNGEDVLAPydhykdtrtGVVVGPDSNPTLSFTSGSEGI 427
Cdd:TIGR01733 81 alASRLAGLVLPVILLDPLELAA-----------------LDDAPAPPPP---------DAPSGPDDLAYVIYTSGSTGR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 428 PKGVLGRHFSLAYYFNWMSKRFNLTENDKFTMLSGIAHDPIQRDMFTPLFLGAQLYVPTQDDIGTPGRL-AEWMSKYGCT 506
Cdd:TIGR01733 135 PKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALlAALIAEHPVT 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 507 VTHLTPAMGQLLTAQATTPFPKLHHAFFVGDILTKRDCLRLQTLAENCRIVNMYGTTETQRAVSYFEVKSKNDDPNFLkk 586
Cdd:TIGR01733 215 VLNLTPSLLALLAAALPPALASLRLVILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVDPDDAPRESP-- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 587 lkdvMPAGKGMLNVQLLVVNRNDRtqICGIGEIGEIYVRAGGLAEGYRGLPELNKEKFVNNWFvekdhwnyldkdngepw 666
Cdd:TIGR01733 293 ----VPIGRPLANTRLYVLDDDLR--PVPVGVVGELYIGGPGVARGYLNRPELTAERFVPDPF----------------- 349
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6319591 667 rqfWLGPRDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENI 728
Cdd:TIGR01733 350 ---AGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAV 408
|
|
| SDR_e1 |
cd05235 |
extended (e) SDRs, subgroup 1; This family consists of an SDR module of multidomain proteins ... |
972-1274 |
6.65e-120 |
|
extended (e) SDRs, subgroup 1; This family consists of an SDR module of multidomain proteins identified as putative polyketide sythases fatty acid synthases (FAS), and nonribosomal peptide synthases, among others. However, unlike the usual ketoreductase modules of FAS and polyketide synthase, these domains are related to the extended SDRs, and have canonical NAD(P)-binding motifs and an active site tetrad. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187546 [Multi-domain] Cd Length: 290 Bit Score: 375.45 E-value: 6.65e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 972 NVFVTGVTGFLGSYILADLLGRSPknySFKVFAHVRAKDEEAAFARLQKAGITYG--TWNEKFASNIKVVLGDLSKSQFG 1049
Cdd:cd05235 1 TVLLTGATGFLGAYLLRELLKRKN---VSKIYCLVRAKDEEAALERLIDNLKEYGlnLWDELELSRIKVVVGDLSKPNLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 1050 LSDEKWMDLANTVDIIIHNGALVHWVYPYAKLRDPNVISTINVMSLAAVGKPKFFDFVSSTSTLDTEYYFNLSDKlvseg 1129
Cdd:cd05235 78 LSDDDYQELAEEVDVIIHNGANVNWVYPYEELKPANVLGTKELLKLAATGKLKPLHFVSTLSVFSAEEYNALDDE----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 1130 kpgilESDDLMNSASGLTGGYGQSKWAAEYIIRRAGERGLRGCIVRPGYVTGASANGSSNTDDFLLRFLKGSVQLGKIPD 1209
Cdd:cd05235 153 -----ESDDMLESQNGLPNGYIQSKWVAEKLLREAANRGLPVAIIRPGNIFGDSETGIGNTDDFFWRLLKGCLQLGIYPI 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6319591 1210 IENSVNMVPVDHVARVVVATSLNPpkENELAVAQVTGHPRILFKDYLYTLHDYGYDVEIESYSKW 1274
Cdd:cd05235 228 SGAPLDLSPVDWVARAIVKLALNE--SNEFSIYHLLNPPLISLNDLLDALEEKGYSIKEVSYEEW 290
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
7-965 |
5.15e-104 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 367.56 E-value: 5.15e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 7 WIEKL--DNPTLSvLPHDFLRPQQEPYtKQATYSLQLPQL------DVPHDSFSNKYAVALSVWAALIYRVTGDDDI--- 75
Cdd:PRK12467 243 WQEQLggEHTVLE-LPTDRPRPAVPSY-RGARLRVDLPQAlsaglkALAQREGVTLFMVLLASFQTLLHRYSGQSDIrig 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 76 --------------VLYIANNKILRFNIQPTWSFNELYSTInnelnKLNSIEA----NFSFDELAEKIQSCQDLERTPqL 137
Cdd:PRK12467 321 vpnanrnrveterlIGFFVNTQVLKAEVDPQASFLELLQQV-----KRTALGAqahqDLPFEQLVEALQPERSLSHSP-L 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 138 FRLAFLENQD--------------FKLDEFK--HHLVDFALNLDTSNNAHVL--NLIYNSLLYSNERVTIVADQFTQYLT 199
Cdd:PRK12467 395 FQVMFNHQNTatggrdregaqlpgLTVEELSwaRHTAQFDLALDTYESAQGLwaAFTYATDLFEATTIERLATHWRNLLE 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 200 AALSDPSNCITKISLITASS-----KDSLPDPTKNLGwcdfvGCIHDIFQDNAEAFPERtcvvetPTLNSDKSRsFTYRD 274
Cdd:PRK12467 475 AIVAEPRRRLGELPLLDAEErarelVRWNAPATEYAP-----DCVHQLIEAQARQHPER------PALVFGEQV-LSYAE 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 275 INRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFSVIDPAYPPARQTIYL---GVAkprglIVIRAA 351
Cdd:PRK12467 543 LNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLddsGVR-----LLLTQS 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 352 GQLDQLvedyindelEIVSRINSIAIQENGtieggkldngedvlAPYDHYKDTRTGVVVGPDSNPTLSFTSGSEGIPKGV 431
Cdd:PRK12467 618 HLLAQL---------PVPAGLRSLCLDEPA--------------DLLCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGV 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 432 LGRHFSLAYYFNWMSKRFNLTENDKFTMLSGIAHDPIQRDMFTPLFLGAQLYVPTQDDIGTPGRLAEWMSKYGCTVTHLT 511
Cdd:PRK12467 675 AISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIV 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 512 PAMGQ-LLTAQATTPFPKLHHAFFVGDILTKRDCLRLQTLAENCRIVNMYGTTETQRAVSYFEVKSKNDDPNflkklkdV 590
Cdd:PRK12467 755 PSHLQaLLQASRVALPRPQRALVCGGEALQVDLLARVRALGPGARLINHYGPTETTVGVSTYELSDEERDFG-------N 827
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 591 MPAGKGMLNVQLLVVNRNdrTQICGIGEIGEIYVRAGGLAEGYRGLPELNKEKFVNNWFvekdhwnyldKDNGEpwrqfw 670
Cdd:PRK12467 828 VPIGQPLANLGLYILDHY--LNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPF----------GADGG------ 889
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 671 lgprdRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVrKNADNEPTLITFMVPrfD 750
Cdd:PRK12467 890 -----RLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLA-QPGDAGLQLVAYLVP--A 961
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 751 KPDDLSKFQSdvpkevetdpivkgligyhlLSKDIRTFLKKRLASYAMPSLIVVMDKLPLNPNGKVDKPKLqfPTPKqln 830
Cdd:PRK12467 962 AVADGAEHQA--------------------TRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKAL--PKPD--- 1016
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 831 lvaENTVSETDDSQFTNVEREVRDLWLSILPTKPasVSPDDSFFDLGGHSILATKMIFTLKKKLQVDLPLGTIFKYPTIK 910
Cdd:PRK12467 1017 ---ASAVQATFVAPQTELEKRLAAIWADVLKVER--VGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFEHQTLA 1091
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|....*....
gi 6319591 911 AFAAEIDriksSGGSSQGEVVENVtanyAEDAkklveTLPSSYP-SREYFV---EPNSA 965
Cdd:PRK12467 1092 GFAQAVA----AQQQGAQPALPDV----DRDQ-----PLPLSYAqERQWFLwqlEPGSA 1137
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
241-821 |
4.48e-99 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 326.08 E-value: 4.48e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 241 DIFQDNAEAFPERTCVVetptlnsDKSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGAT 320
Cdd:cd12117 1 ELFEEQAARTPDAVAVV-------YGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 321 FSVIDPAYPPARQTIYLGVAKPRGLIVIRA-AGQLDQLVEDYINDEleivsrinsiaiqengtieggKLDNGEDVLAPyd 399
Cdd:cd12117 74 YVPLDPELPAERLAFMLADAGAKVLLTDRSlAGRAGGLEVAVVIDE---------------------ALDAGPAGNPA-- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 400 hykdtrtgVVVGPDSNPTLSFTSGSEGIPKGVLGRHFS---LAYYFNWMSkrfnLTENDKFTMLSGIAHDPIQRDMFTPL 476
Cdd:cd12117 131 --------VPVSPDDLAYVMYTSGSTGRPKGVAVTHRGvvrLVKNTNYVT----LGPDDRVLQTSPLAFDASTFEIWGAL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 477 FLGAQLYVPTQDDIGTPGRLAEWMSKYGCTVTHLTPAMGQLLTAQATTPFPKLHHAFFVGDILTKRDCLRLqtLAENC-- 554
Cdd:cd12117 199 LNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLTAALFNQLADEDPECFAGLRELLTGGEVVSPPHVRRV--LAACPgl 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 555 RIVNMYGTTETQRAVSYFEVKSKNDDPnflkklkDVMPAGKGMLNVQLLVVNRNdrTQICGIGEIGEIYVRAGGLAEGYR 634
Cdd:cd12117 277 RLVNGYGPTENTTFTTSHVVTELDEVA-------GSIPIGRPIANTRVYVLDED--GRPVPPGVPGELYVGGDGLALGYL 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 635 GLPELNKEKFVNNWFvekdhwnyldkdngepwrqfwlGPRDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEI 714
Cdd:cd12117 348 NRPALTAERFVADPF----------------------GPGERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEI 405
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 715 DTHISQHPLVRENITLVRKNADNEPTLITFMVPRFDKPDDlskfqsdvpkevetdpivkgligyhllskDIRTFLKKRLA 794
Cdd:cd12117 406 EAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGALDAA-----------------------------ELRAFLRERLP 456
|
570 580
....*....|....*....|....*..
gi 6319591 795 SYAMPSLIVVMDKLPLNPNGKVDKPKL 821
Cdd:cd12117 457 AYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| Thioester-redct |
TIGR01746 |
thioester reductase domain; This model includes the terminal domain from the fungal alpha ... |
972-1354 |
7.80e-99 |
|
thioester reductase domain; This model includes the terminal domain from the fungal alpha aminoadipate reductase enzyme (also known as aminoadipate semialdehyde dehydrogenase) which is involved in the biosynthesis of lysine, as well as the reductase-containing component of the myxochelin biosynthetic gene cluster, MxcG. The mechanism of reduction involves activation of the substrate by adenylation and transfer to a covalently-linked pantetheine cofactor as a thioester. This thioester is then reduced to give an aldehyde (thus releasing the product) and a regenerated pantetheine thiol. (In myxochelin biosynthesis this aldehyde is further reduced to an alcohol or converted to an amine by an aminotransferase.) This is a fundamentally different reaction than beta-ketoreductase domains of polyketide synthases which act at a carbonyl two carbons removed from the thioester and forms an alcohol as a product. This domain is invariably found at the C-terminus of the proteins which contain it (presumably because it results in the release of the product). The majority of hits to this model are non-ribosomal peptide synthetases in which this domain is similarly located proximal to a thiolation domain (pfam00550). In some cases this domain is found at the end of a polyketide synthetase enzyme, but is unlike ketoreductase domains which are found before the thiolase domains. Exceptions to this observed relationship with the thiolase domain include three proteins which consist of stand-alone reductase domains (GP|466833 from M. leprae, GP|435954 from Anabaena and OMNI|NTL02SC1199 from Strep. coelicolor) and one protein (OMNI|NTL01NS2636 from Nostoc) which contains N-terminal homology with a small group of hypothetical proteins but no evidence of a thiolation domain next to the putative reductase domain. Below the noise cutoff to this model are proteins containing more distantly related ketoreductase and dehydratase/epimerase domains. It has been suggested that a NADP-binding motif can be found in the N-terminal portion of this domain that may form a Rossman-type fold.
Pssm-ID: 273787 [Multi-domain] Cd Length: 367 Bit Score: 321.29 E-value: 7.80e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 972 NVFVTGVTGFLGSYILADLLGRSPknySFKVFAHVRAKDEEAAFARLQKAGITYGTWNEKFA-SNIKVVLGDLSKSQFGL 1050
Cdd:TIGR01746 1 TVLLTGATGFLGAYLLEELLRRST---RAKVICLVRADSEEHAMERLREALRSYRLWHENLAmERIEVVAGDLSKPRLGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 1051 SDEKWMDLANTVDIIIHNGALVHWVYPYAKLRDPNVISTINVMSLAAVGKPKFFDFVSSTSTLDTEYYfnlsdklvsegK 1130
Cdd:TIGR01746 78 SDAEWERLAENVDTIVHNGALVNHVYPYSELRGANVLGTVEVLRLAASGRAKPLHYVSTISVGAAIDL-----------S 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 1131 PGILESDDLMNSASGLTGGYGQSKWAAEYIIRRAGERGLRGCIVRPGYVTGASANGSSNTDDFLLRFLKGSVQLGKIPD- 1209
Cdd:TIGR01746 147 TGVTEDDATVTPYPGLAGGYTQSKWVAELLVREASDRGLPVTIVRPGRILGDSYTGAWNSSDILWRMVKGCLALGAYPQs 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 1210 IENSVNMVPVDHVARVVVATSLNPPKENELAVAQVTGHPRILFKDYLYTLHDYGYDVEIESYSKWKKSLEASV-IDRNEE 1288
Cdd:TIGR01746 227 PELTEDLTPVDFVARAIVALSSRPAASAGGIVFHVVNPNPVPLDEFLEWLERAGYNLRLVSFDEWLQRLEDSDtAKRDSR 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6319591 1289 N-ALYPLLHMVLDNLPESTK-APELDDRNAVaslkkdtAWTGVDWSNGIGVTPEEVGIYIAFLNKVGF 1354
Cdd:TIGR01746 307 RyPLLPLLHFTGDAFESDETdTRNLDSRSTA-------EALEGDGIREPSITAPLLHLYLQYLKEIGF 367
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
240-821 |
1.20e-94 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 313.83 E-value: 1.20e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 240 HDIFQDNAEAFPERTCVVETPtlnsdksRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGA 319
Cdd:cd17646 1 HALVAEQAARTPDAPAVVDEG-------RTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 320 TFSVIDPAYPPARQTIYLGVAKPRglIVIRAAGQLDQLVEDyindeleivsrinsiaiqengtieggkLDNGEDVLAPYD 399
Cdd:cd17646 74 AYLPLDPGYPADRLAYMLADAGPA--VVLTTADLAARLPAG---------------------------GDVALLGDEALA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 400 HYKDTRTGVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFNWMSKRFNLTENDKFTMLSGIAHDPIQRDMFTPLFLG 479
Cdd:cd17646 125 APPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAG 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 480 AQLYVPTQDDIGTPGRLAEWMSKYGCTVTHLTPAM-GQLLTAQATTPFPKLHHAFFVGDILTKRDCLRLQTLAeNCRIVN 558
Cdd:cd17646 205 ARLVVARPGGHRDPAYLAALIREHGVTTCHFVPSMlRVFLAEPAAGSCASLRRVFCSGEALPPELAARFLALP-GAELHN 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 559 MYGTTETQRAVSYFEVKSKNDDPNflkklkdvMPAGKGMLNVQLLVVNrnDRTQICGIGEIGEIYVRAGGLAEGYRGLPE 638
Cdd:cd17646 284 LYGPTEAAIDVTHWPVRGPAETPS--------VPIGRPVPNTRLYVLD--DALRPVPVGVPGELYLGGVQLARGYLGRPA 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 639 LNKEKFVNNWFvekdhwnyldkdngepwrqfwlGPRDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHI 718
Cdd:cd17646 354 LTAERFVPDPF----------------------GPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAAL 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 719 SQHPLVRENITLVRKNADNEPTLITFMVPRFDKPDdlskfqsdvpkevetdpivkgligyhLLSKDIRTFLKKRLASYAM 798
Cdd:cd17646 412 AAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAG--------------------------PDTAALRAHLAERLPEYMV 465
|
570 580
....*....|....*....|...
gi 6319591 799 PSLIVVMDKLPLNPNGKVDKPKL 821
Cdd:cd17646 466 PAAFVVLDALPLTANGKLDRAAL 488
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
243-826 |
1.22e-94 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 314.27 E-value: 1.22e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 243 FQDNAEAFPERTCVV-ETPTLnsdksrsfTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATF 321
Cdd:cd17655 3 FEEQAEKTPDHTAVVfEDQTL--------TYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 322 SVIDPAYPPAR-QTIylgvAKPRGLIVIRAAGQLDQLvEDYIndeleivsrinsiaiqenGTIEggkLDNGEDVlapyDH 400
Cdd:cd17655 75 LPIDPDYPEERiQYI----LEDSGADILLTQSHLQPP-IAFI------------------GLID---LLDEDTI----YH 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 401 YKDTRTGVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFNWMSKRFNLTENDKFTMLSGIAHDPIQRDMFTPLFLGA 480
Cdd:cd17655 125 EESENLEPVSKSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGN 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 481 QLYVPTQDDIGTPGRLAEWMSKYGCTVTHLTPAMGQLLTAQATTPFPKLHHAFFVGDILTKRDCLRL-QTLAENCRIVNM 559
Cdd:cd17655 205 TLYIVRKETVLDGQALTQYIRQNRITIIDLTPAHLKLLDAADDSEGLSLKHLIVGGEALSTELAKKIiELFGTNPTITNA 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 560 YGTTETQRAVSYFEVKSKNDDpnflkklKDVMPAGKGMLNVQLLVVNRNDRTQicGIGEIGEIYVRAGGLAEGYRGLPEL 639
Cdd:cd17655 285 YGPTETTVDASIYQYEPETDQ-------QVSVPIGKPLGNTRIYILDQYGRPQ--PVGVAGELYIGGEGVARGYLNRPEL 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 640 NKEKFVNNWFVekdhwnyldkdngepwrqfwlgPRDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHIS 719
Cdd:cd17655 356 TAEKFVDDPFV----------------------PGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLL 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 720 QHPLVRENITLVRKNADNEPTLITFMVprFDKpddlskfqsdvpkevetdpivkgligyHLLSKDIRTFLKKRLASYAMP 799
Cdd:cd17655 414 QHPDIKEAVVIARKDEQGQNYLCAYIV--SEK---------------------------ELPVAQLREFLARELPDYMIP 464
|
570 580
....*....|....*....|....*..
gi 6319591 800 SLIVVMDKLPLNPNGKVDKPKLqfPTP 826
Cdd:cd17655 465 SYFIKLDEIPLTPNGKVDRKAL--PEP 489
|
|
| NAD_binding_4 |
pfam07993 |
Male sterility protein; This family represents the C-terminal region of the male sterility ... |
975-1226 |
2.09e-93 |
|
Male sterility protein; This family represents the C-terminal region of the male sterility protein in a number of arabidopsis and drosophila. A sequence-related jojoba acyl CoA reductase is also included.
Pssm-ID: 462334 [Multi-domain] Cd Length: 257 Bit Score: 301.84 E-value: 2.09e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 975 VTGVTGFLGSYILADLLgRSPKNYsFKVFAHVRAKDEEAAFARLQKAGITYGTWN---EKFASNIKVVLGDLSKSQFGLS 1051
Cdd:pfam07993 1 LTGATGFLGKVLLEKLL-RSTPDV-KKIYLLVRAKDGESALERLRQELEKYPLFDallKEALERIVPVAGDLSEPNLGLS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 1052 DEKWMDLANTVDIIIHNGALVHWVYPYAKLRDPNVISTINVMSLAAVGKPKF-FDFVSsTSTLDTEYYFNLSDKLVSEGK 1130
Cdd:pfam07993 79 EEDFQELAEEVDVIIHSAATVNFVEPYDDARAVNVLGTREVLRLAKQGKQLKpFHHVS-TAYVNGERGGLVEEKPYPEGE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 1131 PGILESDDLMNSASGLTGGYGQSKWAAEYIIRRAGERGLRGCIVRPGYVTGASANGSSNTDDFLLRFLKGSVQLGKIPDI 1210
Cdd:pfam07993 158 DDMLLDEDEPALLGGLPNGYTQTKWLAEQLVREAARRGLPVVIYRPSIITGEPKTGWINNFDFGPRGLLGGIGKGVLPSI 237
|
250 260
....*....|....*....|
gi 6319591 1211 ENS----VNMVPVDHVARVV 1226
Cdd:pfam07993 238 LGDpdavLDLVPVDYVANAI 257
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
243-817 |
1.01e-92 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 308.89 E-value: 1.01e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 243 FQDNAEAFPERTCVVetptlnsDKSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFS 322
Cdd:cd17651 1 FERQAARTPDAPALV-------AEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 323 VIDPAYPPARQTIYLGVAKPRgLIVIRAAGQLDQLVEDyindeleivsrinsiaiqengtIEGGKLDNGEDVLAPydhyk 402
Cdd:cd17651 74 PLDPAYPAERLAFMLADAGPV-LVLTHPALAGELAVEL----------------------VAVTLLDQPGAAAGA----- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 403 DTRTGVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFNWMSKRFNLTENDKFTMLSGIAHDPIQRDMFTPLFLGAQL 482
Cdd:cd17651 126 DAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHRSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATL 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 483 YVPTqDDIGT-PGRLAEWMSKYGCTVTHLTPAMGQLLTAQAT---TPFPKLHHAFFVGDILTKRDCLRLQTLAE-NCRIV 557
Cdd:cd17651 206 VLPP-EEVRTdPPALAAWLDEQRISRVFLPTVALRALAEHGRplgVRLAALRYLLTGGEQLVLTEDLREFCAGLpGLRLH 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 558 NMYGTTETQrAVSYFEVKSKNDDPnflkklKDVMPAGKGMLNVQLLVVNRNDRTqiCGIGEIGEIYVRAGGLAEGYRGLP 637
Cdd:cd17651 285 NHYGPTETH-VVTALSLPGDPAAW------PAPPPIGRPIDNTRVYVLDAALRP--VPPGVPGELYIGGAGLARGYLNRP 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 638 ELNKEKFVNNWFVekdhwnyldkdngepwrqfwlgPRDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTH 717
Cdd:cd17651 356 ELTAERFVPDPFV----------------------PGARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAA 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 718 ISQHPLVRENITLVRKNADNEPTLITFMVPRFDKPDDLSkfqsdvpkevetdpivkgligyhllskDIRTFLKKRLASYA 797
Cdd:cd17651 414 LARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDAA---------------------------ELRAALATHLPEYM 466
|
570 580
....*....|....*....|
gi 6319591 798 MPSLIVVMDKLPLNPNGKVD 817
Cdd:cd17651 467 VPSAFVLLDALPLTPNGKLD 486
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
247-821 |
1.60e-86 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 289.92 E-value: 1.60e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 247 AEAFPERTCVVETPtlnsdksRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFSVIDP 326
Cdd:cd05945 1 AAANPDRPAVVEGG-------RTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 327 AYPPARQTIYLGVAKPRGLIVIraagqldqlvedyindeleivsrinsiaiqengtieggkldngedvlapydhykdtrt 406
Cdd:cd05945 74 SSPAERIREILDAAKPALLIAD---------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 407 gvvvgPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFNWMSKRFNLTENDKFTMLSGIAHDPIQRDMFTPLFLGAQLYVPT 486
Cdd:cd05945 96 -----GDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVP 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 487 QDDIGTPGRLAEWMSKYGCTVTHLTP-AMGQLLTAQATTP--FPKLHHAFFVGDILTKRDCLRLQTLAENCRIVNMYGTT 563
Cdd:cd05945 171 RDATADPKQLFRFLAEHGITVWVSTPsFAAMCLLSPTFTPesLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPT 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 564 ETQRAVSYFEVkskndDPNFLKKLKDVmPAGKGMLNVQLLVVNrnDRTQICGIGEIGEIYVRAGGLAEGYRGLPELNKEK 643
Cdd:cd05945 251 EATVAVTYIEV-----TPEVLDGYDRL-PIGYAKPGAKLVILD--EDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAA 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 644 FVnnwfvekdhwnyldKDNGEPWrqfwlgprdrlYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPL 723
Cdd:cd05945 323 FF--------------PDEGQRA-----------YRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPG 377
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 724 VRENITLVRKNADNEPTLITFMVPRfdkpddlskfqsdvpkevETDPIVkgligyhlLSKDIRTFLKKRLASYAMPSLIV 803
Cdd:cd05945 378 VKEAVVVPKYKGEKVTELIAFVVPK------------------PGAEAG--------LTKAIKAELAERLPPYMIPRRFV 431
|
570
....*....|....*...
gi 6319591 804 VMDKLPLNPNGKVDKPKL 821
Cdd:cd05945 432 YLDELPLNANGKIDRKAL 449
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
57-922 |
1.01e-85 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 310.74 E-value: 1.01e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 57 VALSVWAALIYRVTGDDDIVL--YIANNKILRFNIQptwsfnELYSTINNELNKLNSIEANFSFDELAEKIQSC----QD 130
Cdd:PRK12316 4342 LVQAAWLLLLQRYTGQDTVAFgaTVAGRPAELPGIE------GQIGLFINTLPVIATPRAQQSVVEWLQQVQRQnlalRE 4415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 131 LERTP--QLFRLAFL------------EN------------QDFKLDEFKHH-----LVDFALNLDTSNNAHvlnLIYNS 179
Cdd:PRK12316 4416 HEHTPlyEIQRWAGQggealfdsllvfENypvsealqqgapGGLRFGEVTNHeqtnyPLTLAVGLGETLSLQ---FSYDR 4492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 180 LLYSNERVTIVADQFTQYLTAALSDPSNCITKISLITasskdslPDPTKNLG--WCDFVG------CIHDIFQDNAEAFP 251
Cdd:PRK12316 4493 GHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLE-------KAEQQRIValWNRTDAgypatrCVHQLVAERARMTP 4565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 252 ERTCVVEtptlnsdKSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFSVIDPAYPpa 331
Cdd:PRK12316 4566 DAVAVVF-------DEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYP-- 4636
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 332 rqtiylgvaKPRGLIVIRAAGQLDQLVEDYINDELEIVSRINSIAIQENGTIEGgkldngedvlapydhYKDTRTGVVVG 411
Cdd:PRK12316 4637 ---------RERLAYMMEDSGAALLLTQSHLLQRLPIPDGLASLALDRDEDWEG---------------FPAHDPAVRLH 4692
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 412 PDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFNWMSKRFNLTENDKFTMLSGIAHDPIQRDMFTPLFLGAQLYVPtQDDIG 491
Cdd:PRK12316 4693 PDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIR-DDSLW 4771
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 492 TPGRLAEWMSKYGCTVTHLTPAMGQLLT--AQATTPFPKLHHAFFVGDILTKRDCLRLQTLAENCRIVNMYGTTETQRAV 569
Cdd:PRK12316 4772 DPERLYAEIHEHRVTVLVFPPVYLQQLAehAERDGEPPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTVTV 4851
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 570 SYFEVksknddPNFLKKLKDVMPAGKGMLNVQLLVVNrnDRTQICGIGEIGEIYVRAGGLAEGYRGLPELNKEKFVNNWF 649
Cdd:PRK12316 4852 LLWKA------RDGDACGAAYMPIGTPLGNRSGYVLD--GQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPF 4923
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 650 vekdhwnylDKDNGepwrqfwlgprdRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENIT 729
Cdd:PRK12316 4924 ---------GAPGG------------RLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVV 4982
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 730 LVRKNADNEpTLITFMVPrfdkpddlskfqsDVPKEVETDPIVKGLIGyhllskDIRTFLKKRLASYAMPSLIVVMDKLP 809
Cdd:PRK12316 4983 IAQEGAVGK-QLVGYVVP-------------QDPALADADEAQAELRD------ELKAALRERLPEYMVPAHLVFLARMP 5042
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 810 LNPNGKVDKPKLQFPTPKQLNLVAENTVSEtddsqftnVEREVRDLWLSILptKPASVSPDDSFFDLGGHSILATKMIFT 889
Cdd:PRK12316 5043 LTPNGKLDRKALPQPDASLLQQAYVAPRSE--------LEQQVAAIWAEVL--QLERVGLDDNFFELGGHSLLAIQVTSR 5112
|
890 900 910
....*....|....*....|....*....|...
gi 6319591 890 LKKKLQVDLPLGTIFKYPTIKAFAAEIDRIKSS 922
Cdd:PRK12316 5113 IQLELGLELPLRELFQTPTLAAFVELAAAAGSG 5145
|
|
| Lys2b |
COG3320 |
Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary ... |
972-1234 |
3.92e-85 |
|
Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary metabolites biosynthesis, transport and catabolism]; Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 442549 [Multi-domain] Cd Length: 265 Bit Score: 278.63 E-value: 3.92e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 972 NVFVTGVTGFLGSYILADLLGRSPknysFKVFAHVRAKDEEAAFARLQKAGITYGTWNEKFASNIKVVLGDLSKSQFGLS 1051
Cdd:COG3320 2 TVLLTGATGFLGAHLLRELLRRTD----ARVYCLVRASDEAAARERLEALLERYGLWLELDASRVVVVAGDLTQPRLGLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 1052 DEKWMDLANTVDIIIHNGALVHWVYPYAKLRDPNVISTINVMSLAAVGKPKFFDFVSSTSTLDTEYYfnlsdklvsegkP 1131
Cdd:COG3320 78 EAEFQELAEEVDAIVHLAALVNLVAPYSELRAVNVLGTREVLRLAATGRLKPFHYVSTIAVAGPADR------------S 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 1132 GILESDDLmNSASGLTGGYGQSKWAAEYIIRRAGERGLRGCIVRPGYVTGASANGSSNTDDFLLRFLKGSVQLGKIPDIE 1211
Cdd:COG3320 146 GVFEEDDL-DEGQGFANGYEQSKWVAEKLVREARERGLPVTIYRPGIVVGDSRTGETNKDDGFYRLLKGLLRLGAAPGLG 224
|
250 260
....*....|....*....|....
gi 6319591 1212 NS-VNMVPVDHVARVVVATSLNPP 1234
Cdd:COG3320 225 DArLNLVPVDYVARAIVHLSRQPE 248
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
239-822 |
3.93e-85 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 287.13 E-value: 3.93e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 239 IHDIFQDNAEAFPERTCVVETptlnsdkSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAG 318
Cdd:cd05918 1 VHDLIEERARSQPDAPAVCAW-------DGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 319 ATFSVIDPAYPPARqtiylgvakprgliviraagqLDQLVEDyINDELEIVSRINSIAiqengtieggkldngedvlapy 398
Cdd:cd05918 74 GAFVPLDPSHPLQR---------------------LQEILQD-TGAKVVLTSSPSDAA---------------------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 399 dhYkdtrtgvVVgpdsnptlsFTSGSEGIPKGVLGRHFSL---AYYFnwmSKRFNLTENDKFTMLSGIAHDPIQRDMFTP 475
Cdd:cd05918 110 --Y-------VI---------FTSGSTGKPKGVVIEHRALstsALAH---GRALGLTSESRVLQFASYTFDVSILEIFTT 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 476 LFLGAQLYVPTQDDIgtPGRLAEWMSKYGCTVTHLTPAMGQLLTAQAttpFPKLHHAFFVGDILTKRDclrLQTLAENCR 555
Cdd:cd05918 169 LAAGGCLCIPSEEDR--LNDLAGFINRLRVTWAFLTPSVARLLDPED---VPSLRTLVLGGEALTQSD---VDTWADRVR 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 556 IVNMYGTTETQRAVSYFEVKSKNDDPNFlkklkdvmpaGKGmLNVQLLVVNRNDRTQICGIGEIGEIYVRAGGLAEGYRG 635
Cdd:cd05918 241 LINAYGPAECTIAATVSPVVPSTDPRNI----------GRP-LGATCWVVDPDNHDRLVPIGAVGELLIEGPILARGYLN 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 636 LPELNKEKFVNNWFvekdhWnyldkdngepWRQFWLGPRDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEID 715
Cdd:cd05918 310 DPEKTAAAFIEDPA-----W----------LKQEGSGRGRRLYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIE 374
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 716 THISQHPLVRENIT---LVRKNADNEPTLITFMVPRFDKPDDLSKFQSDVPKEVETDPIVkgligyhllsKDIRTFLKKR 792
Cdd:cd05918 375 HHLRQSLPGAKEVVvevVKPKDGSSSPQLVAFVVLDGSSSGSGDGDSLFLEPSDEFRALV----------AELRSKLRQR 444
|
570 580 590
....*....|....*....|....*....|
gi 6319591 793 LASYAMPSLIVVMDKLPLNPNGKVDKPKLQ 822
Cdd:cd05918 445 LPSYMVPSVFLPLSHLPLTASGKIDRRALR 474
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
7-914 |
2.87e-83 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 302.85 E-value: 2.87e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 7 WIEKL--DNPTLSvLPHDFLRPQQEPYtKQATYSLQLP--------QLDVPHDSfsNKYAVALSVWAALIYRVTGDDDI- 75
Cdd:PRK12467 1308 WKAQLggEQPVLE-LPTDRPRPAVQSH-RGARLAFELPpalaeglrALARREGV--TLFMLLLASFQTLLHRYSGQDDIr 1383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 76 ----------------VLYIANNKILRFNIQPTWSFNELYSTInnelnKLNSIEA----NFSFDELAEKIQSCQDLERTP 135
Cdd:PRK12467 1384 vgvpianrnraeteglIGFFVNTQVLRAEVDGQASFQQLLQQV-----KQAALEAqahqDLPFEQLVEALQPERSLSHSP 1458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 136 qLFRLAF---------------LENQDFKLDefkHHLVDFALNLDTSNNAHVL--NLIYNSLLYSNERVTIVADQFTQYL 198
Cdd:PRK12467 1459 -LFQVMFnhqrddhqaqaqlpgLSVESLSWE---SQTAQFDLTLDTYESSEGLqaSLTYATDLFEASTIERLAGHWLNLL 1534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 199 TAALSDPSNCITKISLITASSKDSLPdptknLGW----CDFVG--CIHDIFQDNAEAFPERTCVVETptlnsdkSRSFTY 272
Cdd:PRK12467 1535 QGLVADPERRLGELDLLDEAERRQIL-----EGWnathTGYPLarLVHQLIEDQAAATPEAVALVFG-------EQELTY 1602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 273 RDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFSVIDPAYPPARqtiylgvakprgliviraag 352
Cdd:PRK12467 1603 GELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRER-------------------- 1662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 353 qLDQLVEDyindeleivSRI-----NSIAIQENGTIEGGK---LDNGEDVLAPYDhykDTRTGVVVGPDSNPTLSFTSGS 424
Cdd:PRK12467 1663 -LAYMIED---------SGIellltQSHLQARLPLPDGLRslvLDQEDDWLEGYS---DSNPAVNLAPQNLAYVIYTSGS 1729
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 425 EGIPKGVLGRHFSLAYYFNWMSKRFNLTENDKFTMLSGIAHDPIQRDMFTPLFLGAQLYVPTQDDIGTPGRLAEWMSKYG 504
Cdd:PRK12467 1730 TGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQ 1809
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 505 CTVTHLTPAMGQLL---TAQATTPfPKLHHAFFVGDILtKRDCLRlQTLAE--NCRIVNMYGTTETQRAVSYFEVKSKND 579
Cdd:PRK12467 1810 VTTLHFVPSMLQQLlqmDEQVEHP-LSLRRVVCGGEAL-EVEALR-PWLERlpDTGLFNLYGPTETAVDVTHWTCRRKDL 1886
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 580 DPnflkklKDVMPAGKGMLNVQLLVVnrNDRTQICGIGEIGEIYVRAGGLAEGYRGLPELNKEKFVNNWFvekdhwnyld 659
Cdd:PRK12467 1887 EG------RDSVPIGQPIANLSTYIL--DASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPF---------- 1948
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 660 KDNGEpwrqfwlgprdRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRKNAdNEP 739
Cdd:PRK12467 1949 GTVGS-----------RLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQDGA-NGK 2016
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 740 TLITFMVPrfdkpddlskfqsdvpkeveTDP-IVKGLIGYHLLSKDIRTFLKKRLASYAMPSLIVVMDKLPLNPNGKVDK 818
Cdd:PRK12467 2017 QLVAYVVP--------------------TDPgLVDDDEAQVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDR 2076
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 819 PKLQFPTPKQLNLVAENTVSEtddsqftnVEREVRDLWLSILptKPASVSPDDSFFDLGGHSILATKMIfTLKKKLQVDL 898
Cdd:PRK12467 2077 KALPAPDASELQQAYVAPQSE--------LEQRLAAIWQDVL--GLEQVGLHDNFFELGGDSIISIQVV-SRARQAGIRF 2145
|
970
....*....|....*.
gi 6319591 899 PLGTIFKYPTIKAFAA 914
Cdd:PRK12467 2146 TPKDLFQHQTVQSLAA 2161
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
251-821 |
2.18e-82 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 278.04 E-value: 2.18e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 251 PERTCVVetptlnsDKSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFSVIDPAYPP 330
Cdd:cd17643 1 PEAVAVV-------DEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 331 ARQTIYLGVAKPRGLIviraaGQLDQLVedYIndeleivsrinsiaiqengtIeggkldngedvlapydhykdtrtgvvv 410
Cdd:cd17643 74 ERIAFILADSGPSLLL-----TDPDDLA--YV--------------------I--------------------------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 411 gpdsnptlsFTSGSEGIPKGVLGRHFSLAYYFNWMSKRFNLTENDKFTMLSGIAHDPIQRDMFTPLFLGAQLYVPTQDDI 490
Cdd:cd17643 100 ---------YTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVA 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 491 GTPGRLAEWMSKYGCTVTHLTP-AMGQLLTA--QATTPFPKLHHAFFVGDILTKRdclRLQTLAENC-----RIVNMYGT 562
Cdd:cd17643 171 RSPEDFARLLRDEGVTVLNQTPsAFYQLVEAadRDGRDPLALRYVIFGGEALEAA---MLRPWAGRFgldrpQLVNMYGI 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 563 TETQRAVSYFEVkskndDPNFLKkLKDVMPAGKGMLNVQLLVVNRNDRTQicGIGEIGEIYVRAGGLAEGYRGLPELNKE 642
Cdd:cd17643 248 TETTVHVTFRPL-----DAADLP-AAAASPIGRPLPGLRVYVLDADGRPV--PPGVVGELYVSGAGVARGYLGRPELTAE 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 643 KFVNNWFVekdhwnyldkdngepwrqfwlGPRDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHP 722
Cdd:cd17643 320 RFVANPFG---------------------GPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHP 378
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 723 LVRENITLVRKNADNEPTLITFMVPRFDKPDDLSkfqsdvpkevetdpivkgligyhllskDIRTFLKKRLASYAMPSLI 802
Cdd:cd17643 379 SVRDAAVIVREDEPGDTRLVAYVVADDGAAADIA---------------------------ELRALLKELLPDYMVPARY 431
|
570
....*....|....*....
gi 6319591 803 VVMDKLPLNPNGKVDKPKL 821
Cdd:cd17643 432 VPLDALPLTVNGKLDRAAL 450
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
22-917 |
6.08e-82 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 295.41 E-value: 6.08e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 22 DFLRPQQEP----YTKQATYSLQLPQLDVphdsfsnkyAVALSvwAALIYRVTGDDDIVL---YIA-------------- 80
Cdd:PRK10252 226 DILRLKLEFtdgaFRQLAAQASGVQRPDL---------ALALV--ALWLGRLCGRMDYAAgfiFMRrlgsaaltatgpvl 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 81 NNKILRFNIQPTWSFNELYSTINNELNKLNSIEanfSFDelAEKIQscQDLERT--------PQLFRLAFLENQDFKLDE 152
Cdd:PRK10252 295 NVLPLRVHIAAQETLPELATRLAAQLKKMRRHQ---RYD--AEQIV--RDSGRAagdeplfgPVLNIKVFDYQLDFPGVQ 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 153 FKHHL-----VD---FALNLDTSNNAHvLNLIYNSLLYSNERVTIVADQFTQYLTAALSDPSNCITKISLITAS------ 218
Cdd:PRK10252 368 AQTHTlatgpVNdleLALFPDEHGGLS-IEILANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGeyaqla 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 219 ----SKDSLPDPTknlgwcdfvgcIHDIFQDNAEAFPErtcvveTPTLnSDKSRSFTYRDINRTSNIVAHYLIKTGIKRG 294
Cdd:PRK10252 447 qvnaTAVEIPETT-----------LSALVAQQAAKTPD------APAL-ADARYQFSYREMREQVVALANLLRERGVKPG 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 295 DVVMIYSSRGVDLMVCVMGVLKAGATFSVIDPAYPPARQTIYLGVAKPRglIVIRAAGQLDQLVEdyindeleivsrins 374
Cdd:PRK10252 509 DSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPS--LLITTADQLPRFAD--------------- 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 375 iaiqengtIEGGKLDNGEDVLAPydhyKDTRTGVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFNWMSKRFNLTEN 454
Cdd:PRK10252 572 --------VPDLTSLCYNAPLAP----QGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTAD 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 455 DKFTMLSGIAHDPIQRDMFTPLFLGAQLYVPTQDDIGTPGRLAEWMSKYGCTVTHLTPAM-----GQLLTAQATTPFPKL 529
Cdd:PRK10252 640 DVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSMlaafvASLTPEGARQSCASL 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 530 HHAFFVGDILTKRDCLRLQTLAeNCRIVNMYGTTETQRAVSYFevksknddPNFLKKLKDV----MPAGKGMLNVQLLVV 605
Cdd:PRK10252 720 RQVFCSGEALPADLCREWQQLT-GAPLHNLYGPTEAAVDVSWY--------PAFGEELAAVrgssVPIGYPVWNTGLRIL 790
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 606 NrnDRTQICGIGEIGEIYVRAGGLAEGYRGLPELNKEKFVNNWFvekdhwnyldkdngepwrqfwlGPRDRLYRTGDLGR 685
Cdd:PRK10252 791 D--ARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPF----------------------APGERMYRTGDVAR 846
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 686 YLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVR------KNADNEPTLITFMVPRFDKPDDLSkfq 759
Cdd:PRK10252 847 WLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHACvinqaaATGGDARQLVGYLVSQSGLPLDTS--- 923
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 760 sdvpkevetdpivkgligyhllskDIRTFLKKRLASYAMPSLIVVMDKLPLNPNGKVDKPKLqfPTPkqlnlvaENTVSE 839
Cdd:PRK10252 924 ------------------------ALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL--PLP-------ELKAQV 970
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6319591 840 TDDSQFTNVEREVRDLWLSILPTKPASVspDDSFFDLGGHSILATKMIFTLKKKLQVDLPLGTIFKYPTIKAFAAEID 917
Cdd:PRK10252 971 PGRAPKTGTETIIAAAFSSLLGCDVVDA--DADFFALGGHSLLAMKLAAQLSRQFARQVTPGQVMVASTVAKLATLLD 1046
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
7-934 |
6.69e-80 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 292.63 E-value: 6.69e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 7 WIEKLDN--PTLSvLPHDFLRPQQEPYtKQATYSLQL-PQLDVPHDSFSNKYAVAL-----SVWAALIYRVTGDDDI--- 75
Cdd:PRK12316 243 WRAQLGEehPVLE-LPTDHPRPAVPSY-RGSRYEFSIdPALAEALRGTARRQGLTLfmlllGAFNVLLHRYSGQTDIrvg 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 76 --------------VLYIANNKILRFNIQPTWSFNELYSTInnelnKLNSIEA----NFSFDELAEKIQSCQDLERTPqL 137
Cdd:PRK12316 321 vpianrnraeveglIGFFVNTQVLRSVFDGRTRVATLLAGV-----KDTVLGAqahqDLPFERLVEALKVERSLSHSP-L 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 138 FRLAF--------------LENQDFKLDEFKHHLVDFALNLDTSNNAHVLN--LIYNSLLYSNERVTIVADQFTQYLTAA 201
Cdd:PRK12316 395 FQVMYnhqplvadiealdtVAGLEFGQLEWKSRTTQFDLTLDTYEKGGRLHaaLTYATDLFEARTVERMARHWQNLLRGM 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 202 LSDPSNCITKISLITASSKDSLPDptknlGW----CDF--VGCIHDIFQDNAEAFPERTCVVETPTlnsdksrSFTYRDI 275
Cdd:PRK12316 475 VENPQARVDELPMLDAEERGQLVE-----GWnataAEYplQRGVHRLFEEQVERTPEAPALAFGEE-------TLDYAEL 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 276 NRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFSVIDPAYPPARQTiYLgvakprglivIRAAGQLD 355
Cdd:PRK12316 543 NRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLA-YM----------LEDSGVQL 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 356 QLVEDYINDELEIVSRINSIAiqengtieggkLDNGEdvlAPYDHYKDTRTGVVVGPDSNPTLSFTSGSEGIPKGVLGRH 435
Cdd:PRK12316 612 LLSQSHLGRKLPLAAGVQVLD-----------LDRPA---AWLEGYSEENPGTELNPENLAYVIYTSGSTGKPKGAGNRH 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 436 FSLAYYFNWMSKRFNLTENDKFTMLSGIAHDPIQRDMFTPLFLGAQLYVPTQDDIGTPGRLAEWMSKYGCTVTHLTPAMG 515
Cdd:PRK12316 678 RALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSML 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 516 Q-LLTAQATTPFPKLHHAFFVGDILTKRDCLRLQTLAENCRIVNMYGTTETQRAVSYFEVKSKNddpnflkklKDVMPAG 594
Cdd:PRK12316 758 QaFLQDEDVASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEG---------GDSVPIG 828
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 595 KGMLNVQLLVVNRNdrTQICGIGEIGEIYVRAGGLAEGYRGLPELNKEKFVNNWFVekdhwnyldkdNGEpwrqfwlgpr 674
Cdd:PRK12316 829 RPIANLACYILDAN--LEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFV-----------AGE---------- 885
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 675 dRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLvrknADNEPTLITFMVPRFDKPDd 754
Cdd:PRK12316 886 -RMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL----AVDGKQLVGYVVLESEGGD- 959
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 755 lskfqsdvpkevetdpivkgligyhlLSKDIRTFLKKRLASYAMPSLIVVMDKLPLNPNGKVDKPKLqfPTPKQLNLVAE 834
Cdd:PRK12316 960 --------------------------WREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKAL--PAPEASVAQQG 1011
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 835 NTVSETDdsqftnVEREVRDLWLSILPTKPasVSPDDSFFDLGGHSILATKMIfTLKKKLQVDLPLGTIFKYPTIKAFaA 914
Cdd:PRK12316 1012 YVAPRNA------LERTLAAIWQDVLGVER--VGLDDNFFELGGDSIVSIQVV-SRARQAGIQLSPRDLFQHQTIRSL-A 1081
|
970 980
....*....|....*....|
gi 6319591 915 EIDRIKSSGGSSQGEVVENV 934
Cdd:PRK12316 1082 LVAKAGQATAADQGPASGEV 1101
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
238-821 |
2.55e-79 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 270.08 E-value: 2.55e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 238 CIHDIFQDNAEAFPERTCVVetptlnsDKSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKA 317
Cdd:cd17644 1 CIHQLFEEQVERTPDAVAVV-------FEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 318 GATFSVIDPAYPPARQTiylgvakprgliviraagqldqlvedYIndeLEivsrinsiaiqengtieggklDNGEDVLap 397
Cdd:cd17644 74 GGAYVPLDPNYPQERLT--------------------------YI---LE---------------------DAQISVL-- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 398 ydhykdtrtgvVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFNWMSKRFNLTENDKFTMLSGIAHDPIQRDMFTPLF 477
Cdd:cd17644 102 -----------LTQPENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLL 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 478 LGAQLYVPTQDDIGTPGRLAEWMSKYGCTVTHLTPAMGQLLT---AQATTPFPKLHHAFFVG--DILTKRDCLRLQTLAE 552
Cdd:cd17644 171 SGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPPAYWHLLVlelLLSTIDLPSSLRLVIVGgeAVQPELVRQWQKNVGN 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 553 NCRIVNMYGTTETQRAVSYFEVKSknddpNFLKKLKDVmPAGKGMLNVQLLVVNRNdrTQICGIGEIGEIYVRAGGLAEG 632
Cdd:cd17644 251 FIQLINVYGPTEATIAATVCRLTQ-----LTERNITSV-PIGRPIANTQVYILDEN--LQPVPVGVPGELHIGGVGLARG 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 633 YRGLPELNKEKFVNNWFVEKdhwnyldkdngepwrqfwlgPRDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELG 712
Cdd:cd17644 323 YLNRPELTAEKFISHPFNSS--------------------ESERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELG 382
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 713 EIDTHISQHPLVRENITLVRKNADNEPTLITFMVPrfdkpddlskfqsdvPKEVETDPivkgligyhllsKDIRTFLKKR 792
Cdd:cd17644 383 EIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVP---------------HYEESPST------------VELRQFLKAK 435
|
570 580
....*....|....*....|....*....
gi 6319591 793 LASYAMPSLIVVMDKLPLNPNGKVDKPKL 821
Cdd:cd17644 436 LPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
132-950 |
1.33e-77 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 285.13 E-value: 1.33e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 132 ERTPQLFRLAFLENQdfkldEFKHHLVDFALNLDTSNNAHvlnLIYNSLLYSNERVTIVADQFTQYLTAALSDPSNCITK 211
Cdd:PRK12467 2997 QGAPSGLRFGAVSSR-----EQTNYPLTLAVGLGDTLELE---FSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARLGE 3068
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 212 ISLITASSKDSLP---DPTKNLGWCDFvgCIHDIFQDNAEAFPERTCVVEtptlnsdKSRSFTYRDINRTSNIVAHYLIK 288
Cdd:PRK12467 3069 LPTLAAHERRQVLhawNATAAAYPSER--LVHQLIEAQVARTPEAPALVF-------GDQQLSYAELNRRANRLAHRLIA 3139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 289 TGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFSVIDPAYPPARQTIYLGVAKPRGLiviraagqldqLVEDYINDELEI 368
Cdd:PRK12467 3140 IGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLL-----------LTQAHLLEQLPA 3208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 369 VSRINSIaiqengTIEGGKLDNgedvlapydhYKDTRTGVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFNWMSKR 448
Cdd:PRK12467 3209 PAGDTAL------TLDRLDLNG----------YSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEA 3272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 449 FNLTENDKFTMLSGIAHDPIQRDMFTPLFLGAQLYVpTQDDIGTPGRLAEWMSKYGCTVTHLTPAMGQLLTAQA-TTPFP 527
Cdd:PRK12467 3273 YELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVV-RDNDLWDPEELWQAIHAHRISIACFPPAYLQQFAEDAgGADCA 3351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 528 KLHHAFFVGDILTKRDCLRLQTLAENCRIVNMYGTTETQravsyfevksknDDPNFLKKLKD------VMPAGKGMLNVQ 601
Cdd:PRK12467 3352 SLDIYVFGGEAVPPAAFEQVKRKLKPRGLTNGYGPTEAV------------VTVTLWKCGGDavceapYAPIGRPVAGRS 3419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 602 LLVVNRNdrTQICGIGEIGEIYVRAGGLAEGYRGLPELNKEKFVNNWFvekdhwnyldKDNGEpwrqfwlgprdRLYRTG 681
Cdd:PRK12467 3420 IYVLDGQ--LNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPF----------SGSGG-----------RLYRTG 3476
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 682 DLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRKNADNEpTLITFMVPRFDKPDdlskfqsd 761
Cdd:PRK12467 3477 DLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAGGK-QLVAYVVPADPQGD-------- 3547
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 762 vpkevetdpivkgligyhlLSKDIRTFLKKRLASYAMPSLIVVMDKLPLNPNGKVDKPKLqfPTPkqlnlvaENTVSETD 841
Cdd:PRK12467 3548 -------------------WRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKAL--PDP-------DAKGSREY 3599
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 842 DSQFTNVEREVRDLWLSILPTKPASVSpdDSFFDLGGHSILATKMIFTLKKKLQVDLPLGTIFKYPTIKAFAaeidriks 921
Cdd:PRK12467 3600 VAPRSEVEQQLAAIWADVLGVEQVGVT--DNFFELGGDSLLALQVLSRIRQSLGLKLSLRDLMSAPTIAELA-------- 3669
|
810 820
....*....|....*....|....*....
gi 6319591 922 sgGSSQGevvENVTANYAEDAKKLVETLP 950
Cdd:PRK12467 3670 --GYSPL---GDVPVNLLLDLNRLETGFP 3693
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
239-822 |
1.14e-75 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 258.97 E-value: 1.14e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 239 IHDIFQDNAEAFPERTCVVetptlnsDKSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAG 318
Cdd:COG0318 1 LADLLRRAAARHPDRPALV-------FGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 319 ATFSVIDPAYPPARQTIYLGVAKPRGLIVIraagqldqlvedyindeleivsrinsiAIQengtieggkldngedvlapy 398
Cdd:COG0318 74 AVVVPLNPRLTAEELAYILEDSGARALVTA---------------------------LIL-------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 399 dhykdtrtgvvvgpdsnptlsFTSGSEGIPKGVLGRHFSLAYYFNWMSKRFNLTENDKFTMLSGIAHD-PIQRDMFTPLF 477
Cdd:COG0318 107 ---------------------YTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVfGLTVGLLAPLL 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 478 LGAQLYVPTQDDigtPGRLAEWMSKYGCTVTHLTPAMGQLLTAQ---ATTPFPKLHHAFFVGDILTKRDCLRLQTLAeNC 554
Cdd:COG0318 166 AGATLVLLPRFD---PERVLELIERERVTVLFGVPTMLARLLRHpefARYDLSSLRLVVSGGAPLPPELLERFEERF-GV 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 555 RIVNMYGTTETQRAVSYfevkskNDDPNFLKKLkdvMPAGKGMLNVQLLVVNrnDRTQICGIGEIGEIYVRAGGLAEGYR 634
Cdd:COG0318 242 RIVEGYGLTETSPVVTV------NPEDPGERRP---GSVGRPLPGVEVRIVD--EDGRELPPGEVGEIVVRGPNVMKGYW 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 635 GLPELNKEKFVNNWFvekdhwnyldkdngepwrqfwlgprdrlyRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEI 714
Cdd:COG0318 311 NDPEATAEAFRDGWL-----------------------------RTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEV 361
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 715 DTHISQHPLVRENITLVRKNADNEPTLITFMVPRFDKPDDLskfqsdvpkevetdpivkgligyhllsKDIRTFLKKRLA 794
Cdd:COG0318 362 EEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDA---------------------------EELRAFLRERLA 414
|
570 580
....*....|....*....|....*...
gi 6319591 795 SYAMPSLIVVMDKLPLNPNGKVDKPKLQ 822
Cdd:COG0318 415 RYKVPRRVEFVDELPRTASGKIDRRALR 442
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
264-821 |
1.90e-74 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 255.47 E-value: 1.90e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 264 SDKSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFSVIDPAYPPARQTIYLGvakpr 343
Cdd:cd17650 7 SDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLE----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 344 gliviraagqldqlvedyindeleivsrinsiaiqengtieggklDNGEDVLapydhykdtrtgvVVGPDSNPTLSFTSG 423
Cdd:cd17650 82 ---------------------------------------------DSGAKLL-------------LTQPEDLAYVIYTSG 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 424 SEGIPKGVLGRHFSLAY-YFNWmSKRFNLtenDKFTM----LSGIAHDPIQRDMFTPLFLGAQLYVPTQDDIGTPGRLAE 498
Cdd:cd17650 104 TTGKPKGVMVEHRNVAHaAHAW-RREYEL---DSFPVrllqMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYD 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 499 WMSKYGCTVTHLTPA-----MGQLLTAQATTPFPKLhhaFFVG-DILTKRDCLRL-QTLAENCRIVNMYGTTETQRAVSY 571
Cdd:cd17650 180 LILKSRITLMESTPAlirpvMAYVYRNGLDLSAMRL---LIVGsDGCKAQDFKTLaARFGQGMRIINSYGVTEATIDSTY 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 572 FEvksKNDDPnflKKLKDVMPAGKGMLNVQLLVVNRNDRTQICGIgeIGEIYVRAGGLAEGYRGLPELNKEKFVNNWFve 651
Cdd:cd17650 257 YE---EGRDP---LGDSANVPIGRPLPNTAMYVLDERLQPQPVGV--AGELYIGGAGVARGYLNRPELTAERFVENPF-- 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 652 kdhwnyldkdngepwrqfwlGPRDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLV 731
Cdd:cd17650 327 --------------------APGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAV 386
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 732 RKNADNEPTLITFMVPRfDKPDdlskfqsdvpkevetdpivkgligyhllSKDIRTFLKKRLASYAMPSLIVVMDKLPLN 811
Cdd:cd17650 387 REDKGGEARLCAYVVAA-ATLN----------------------------TAELRAFLAKELPSYMIPSYYVQLDALPLT 437
|
570
....*....|
gi 6319591 812 PNGKVDKPKL 821
Cdd:cd17650 438 PNGKVDRRAL 447
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
173-930 |
1.06e-73 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 272.60 E-value: 1.06e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 173 LNLIYNSLLYSNERVTIVADQFTQYLTAALSDPSNCITKISLITASSK-DSLPDPTKNLGWCDFVGCIHDIFQDNAEAFP 251
Cdd:PRK12316 1938 LQYSYDRGHFDAAAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERqRILADWDRTPEAYPRGPGVHQRIAEQAARAP 2017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 252 ERTCVVEtptlnsdKSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFSVIDPAYPPA 331
Cdd:PRK12316 2018 EAIAVVF-------GDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAE 2090
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 332 RQTIYLGVAKPRGLiviraagqldqLVEDYINDELEIVSRINSIAIQENGTIEGgkldngedvlapydhYKDTRTGVVVG 411
Cdd:PRK12316 2091 RLAYMLEDSGAALL-----------LTQRHLLERLPLPAGVARLPLDRDAEWAD---------------YPDTAPAVQLA 2144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 412 PDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFNWMSKRFNLTENDKFTMLSGIAHDPIQRDMFTPLFLGAQLYVpTQDDIG 491
Cdd:PRK12316 2145 GENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLI-RDDELW 2223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 492 TPGRLAEWMSKYGCTVTHLTPAMGQLLTAQATTP--FPKLHHAFFVGDILTKRDCLRLQTLAENCRIVNMYGTTETqrAV 569
Cdd:PRK12316 2224 DPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDgrPPAVRVYCFGGEAVPAASLRLAWEALRPVYLFNGYGPTEA--VV 2301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 570 SYFEVKSKNDDPNFlkklKDVMPAGKGMLNVQLLVVNRNdrTQICGIGEIGEIYVRAGGLAEGYRGLPELNKEKFVNNWF 649
Cdd:PRK12316 2302 TPLLWKCRPQDPCG----AAYVPIGRALGNRRAYILDAD--LNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPF 2375
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 650 VekdhwnyldkdngepwrqfwlGPRDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENIT 729
Cdd:PRK12316 2376 S---------------------ASGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVV 2434
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 730 LVRKNADNePTLITFMVprfdkPDDLSKfqsdvpkevetdpivkgligyhLLSKDIRTFLKKRLASYAMPSLIVVMDKLP 809
Cdd:PRK12316 2435 VAQDGASG-KQLVAYVV-----PDDAAE----------------------DLLAELRAWLAARLPAYMVPAHWVVLERLP 2486
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 810 LNPNGKVDKPKLQFPTPKQLNLVAENTVSEtddsqftnVEREVRDLWLSILptKPASVSPDDSFFDLGGHSILATKMIFT 889
Cdd:PRK12316 2487 LNPNGKLDRKALPKPDVSQLRQAYVAPQEG--------LEQRLAAIWQAVL--KVEQVGLDDHFFELGGHSLLATQVVSR 2556
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 6319591 890 LKKKLQVDLPLGTIFKYPTIKAFAAEIDRIKSSGGSSQGEV 930
Cdd:PRK12316 2557 VRQDLGLEVPLRILFERPTLAAFAASLESGQTSRAPVLQKV 2597
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
7-913 |
2.18e-73 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 271.83 E-value: 2.18e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 7 WIEKL--DNPTLSvLPHDFLRPQQEPYtKQATYSLQLPQ------LDVPHDSFSNKYAVALSVWAALIYRVTGDDDI--- 75
Cdd:PRK12316 2792 WRERLggEQPVLE-LPLDRPRPALQSH-RGARLDVALDValsrelLALARREGVTLFMLLLASFQVLLHRYSGQSDIrvg 2869
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 76 --------------VLYIANNKILRFNIQPTWSFNELYSTINNELNKLNSIEaNFSFDELAEKIQSCQDLERTPqLFRLA 141
Cdd:PRK12316 2870 vpianrnraeterlIGFFVNTQVLRAQVDAQLAFRDLLGQVKEQALGAQAHQ-DLPFEQLVEALQPERSLSHSP-LFQVM 2947
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 142 F-----------LENQDFKLDEFKHHLVDFALNLDTSNNAHVL--NLIYNSLLYSNERVTIVADQFTQYLTAALSDPSNC 208
Cdd:PRK12316 2948 YnhqsgeraaaqLPGLHIESFAWDGAATQFDLALDTWESAEGLgaSLTYATDLFDARTVERLARHWQNLLRGMVENPQRS 3027
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 209 ITKISLITASSKDSLPDptknlGWCDFVG------CIHDIFQDNAEAFPERTCVVETptlnsdkSRSFTYRDINRTSNIV 282
Cdd:PRK12316 3028 VDELAMLDAEERGQLLE-----AWNATAAeyplerGVHRLFEEQVERTPDAVALAFG-------EQRLSYAELNRRANRL 3095
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 283 AHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFSVIDPAYPPARQTIylgvakprgliviraagqldqLVEDyi 362
Cdd:PRK12316 3096 AHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAY---------------------MLED-- 3152
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 363 ndeleivSRINSIAIQENGTIEGGKLDNGEDVLAPYDHYKDTRTGVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYF 442
Cdd:PRK12316 3153 -------SGAQLLLSQSHLRLPLAQGVQVLDLDRGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHL 3225
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 443 NWMSKRFNLTENDKFTMLSGIAHDPIQRDMFTPLFLGAQLYVPTQDDIGTPGRLAEWMSKYGCTVTHLTPAMGQLLTAQA 522
Cdd:PRK12316 3226 CWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLEEE 3305
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 523 TTPFPKLHHAFFVGDILTKRDCLrlQTLAENCRIVNMYGTTETQRAVSYFEVKSKNddpnflkklKDVMPAGKGMLNVQL 602
Cdd:PRK12316 3306 DAHRCTSLKRIVCGGEALPADLQ--QQVFAGLPLYNLYGPTEATITVTHWQCVEEG---------KDAVPIGRPIANRAC 3374
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 603 LVVNrnDRTQICGIGEIGEIYVRAGGLAEGYRGLPELNKEKFVNNWFVekdhwnyldkdngepwrqfwlgPRDRLYRTGD 682
Cdd:PRK12316 3375 YILD--GSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFV----------------------PGERLYRTGD 3430
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 683 LGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLvrknADNEPTLITFMVPRFDKPDdlskfqsdv 762
Cdd:PRK12316 3431 LARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVL----AVDGRQLVAYVVPEDEAGD--------- 3497
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 763 pkevetdpivkgligyhlLSKDIRTFLKKRLASYAMPSLIVVMDKLPLNPNGKVDKPKLQFPTPKQLNLVAENTVSEtdd 842
Cdd:PRK12316 3498 ------------------LREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQQDYVAPVNE--- 3556
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6319591 843 sqftnVEREVRDLWLSILptKPASVSPDDSFFDLGGHSILATKMIfTLKKKLQVDLPLGTIFKYPTIKAFA 913
Cdd:PRK12316 3557 -----LERRLAAIWADVL--KLEQVGLTDNFFELGGDSIISLQVV-SRARQAGIRFTPKDLFQHQTIQGLA 3619
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
7-964 |
2.96e-73 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 271.27 E-value: 2.96e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 7 WIEKL--DNPTLSvLPHDFLRPQQEPYTKqATYSLQLP--------QLDVPHDSFSnkYAVALSVWAALIYRVTGDDDI- 75
Cdd:PRK05691 869 WKAQLgdEQPVLE-LATDHPRSARQAHSA-ARYSLRVDaslsealrGLAQAHQATL--FMVLLAAFQALLHRYSGQGDIr 944
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 76 ----------------VLYIANNKILRFNIQPTWSFNELYSTInnelnKLNSIEA----NFSFDELAEKIQScqdlERTP 135
Cdd:PRK05691 945 igvpnanrprletqglVGFFINTQVLRAQLDGRLPFTALLAQV-----RQATLGAqahqDLPFEQLVEALPQ----AREQ 1015
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 136 QLFRLAFLENQ-DFK---------LDEFKHHL----VDFALNLDTSNNAHV-LNLIYNSLLYSNERVTIVADQFTQYLTA 200
Cdd:PRK05691 1016 GLFQVMFNHQQrDLSalrrlpgllAEELPWHSreakFDLQLHSEEDRNGRLtLSFDYAAELFDAATIERLAEHFLALLEQ 1095
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 201 ALSDPSNCITKISLITASSKDSLpdptknLGWCDfVGC------IHDIFQDNAEAFPERTCVVEtptlnsdKSRSFTYRD 274
Cdd:PRK05691 1096 VCEDPQRALGDVQLLDAAERAQL------AQWGQ-APCapaqawLPELLNEQARQTPERIALVW-------DGGSLDYAE 1161
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 275 INRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFSVIDPAYPPARQTIYLGVAKPRGLiviraagql 354
Cdd:PRK05691 1162 LHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELL--------- 1232
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 355 dqLVEDYINDELEIVSRINSIAIQENgtieggKLDNGEdVLAPYDHYKDTRTGVVVgpdsnptlsFTSGSEGIPKGVLGR 434
Cdd:PRK05691 1233 --LTQSHLLERLPQAEGVSAIALDSL------HLDSWP-SQAPGLHLHGDNLAYVI---------YTSGSTGQPKGVGNT 1294
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 435 HFSLAYYFNWMSKRFNLTENDKFTMLSGIAHDPIQRDMFTPLFLGAQLYVPTQDDIGTPGRLAEWMSKYGCTVTHLTPAM 514
Cdd:PRK05691 1295 HAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYGVTTLHFVPPL 1374
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 515 GQL-----LTAQATTpfpkLHHAFFVGDILTKRDCLRLQTLAENCRIVNMYGTTETQRAVSYFEVKSknDDPNFlkklkd 589
Cdd:PRK05691 1375 LQLfidepLAAACTS----LRRLFSGGEALPAELRNRVLQRLPQVQLHNRYGPTETAINVTHWQCQA--EDGER------ 1442
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 590 vMPAGKGMLNVQLLVvnRNDRTQICGIGEIGEIYVRAGGLAEGYRGLPELNKEKFVNNwfvekdhwnyLDKDNGEpwrqf 669
Cdd:PRK05691 1443 -SPIGRPLGNVLCRV--LDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPD----------PLGEDGA----- 1504
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 670 wlgprdRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRKNAdNEPTLITFmvprf 749
Cdd:PRK05691 1505 ------RLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGA-AGAQLVGY----- 1572
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 750 dkpddlskFQSDVPKEVETDpivkgligyhllskDIRTFLKKRLASYAMPSLIVVMDKLPLNPNGKVDKPKLQFPTPKQL 829
Cdd:PRK05691 1573 --------YTGEAGQEAEAE--------------RLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPVWQQR 1630
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 830 NLVAENtvsetddsqfTNVEREVRDLWLSILPTKpaSVSPDDSFFDLGGHSILATKMIFTLKKKLQVDLPLGTIFKYPTI 909
Cdd:PRK05691 1631 EHVEPR----------TELQQQIAAIWREVLGLP--RVGLRDDFFALGGHSLLATQIVSRTRQACDVELPLRALFEASEL 1698
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|....*....
gi 6319591 910 KAFAAEIDRIKSSGGSSQGEVVENVtanyaeDAKKLVetlPSSYP-SREYFV---EPNS 964
Cdd:PRK05691 1699 GAFAEQVARIQAAGERNSQGAIARV------DRSQPV---PLSYSqQRMWFLwqmEPDS 1748
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
251-818 |
2.46e-72 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 250.27 E-value: 2.46e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 251 PERTCVVetptlnsDKSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFSVIDPAYPP 330
Cdd:cd12114 1 PDATAVI-------CGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 331 ARQTIYLGVAKPRGLIVIRAAGQLDQLVEDYIndeleivsrinsiaiqengtIEGGKLDNGEDVLAPydhykdtrtgVVV 410
Cdd:cd12114 74 ARREAILADAGARLVLTDGPDAQLDVAVFDVL--------------------ILDLDALAAPAPPPP----------VDV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 411 GPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFNWMSKRFNLTENDKFTMLSGIAHDPIQRDMFTPLFLGAQLYVPTQDDI 490
Cdd:cd12114 124 APDDLAYVIFTSGSTGTPKGVMISHRAALNTILDINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARR 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 491 GTPGRLAEWMSKYGCTVTHLTPAMGQLLT---AQATTPFPKLHHAFFVGD-I-LTKRDclRLQTLAENCRIVNMYGTTET 565
Cdd:cd12114 204 RDPAHWAELIERHGVTLWNSVPALLEMLLdvlEAAQALLPSLRLVLLSGDwIpLDLPA--RLRALAPDARLISLGGATEA 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 566 QRAVSYFEVKSKNDDPNflkklkdVMPAGKGMLNVQLLVVNRNDRTqiCGIGEIGEIYVRAGGLAEGYRGLPELNKEKFV 645
Cdd:cd12114 282 SIWSIYHPIDEVPPDWR-------SIPYGRPLANQRYRVLDPRGRD--CPDWVPGELWIGGRGVALGYLGDPELTAARFV 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 646 NnwfvekdhwnyldkdngepwrqfwLGPRDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVR 725
Cdd:cd12114 353 T------------------------HPDGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVA 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 726 ENITLVRKNaDNEPTLITFMVPRFDKPDDlskfqsdvpkevetdpivkgligyhlLSKDIRTFLKKRLASYAMPSLIVVM 805
Cdd:cd12114 409 RAVVVVLGD-PGGKRLAAFVVPDNDGTPI--------------------------APDALRAFLAQTLPAYMIPSRVIAL 461
|
570
....*....|...
gi 6319591 806 DKLPLNPNGKVDK 818
Cdd:cd12114 462 EALPLTANGKVDR 474
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
243-705 |
8.80e-72 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 246.46 E-value: 8.80e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 243 FQDNAEAFPERTCVVetptlnSDKSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFS 322
Cdd:pfam00501 1 LERQAARTPDKTALE------VGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 323 VIDPAYPPARQTIYLGVAKPRGLIViraagqLDQLVEDYINDELEIVSRINSIAIQENGTIEGGKLDNGEDVLApydhYK 402
Cdd:pfam00501 75 PLNPRLPAEELAYILEDSGAKVLIT------DDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPA----DV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 403 DTRTGVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAY----YFNWMSKRFNLTENDKFTMLSGIAHD-PIQRDMFTPLF 477
Cdd:pfam00501 145 PPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVAnvlsIKRVRPRGFGLGPDDRVLSTLPLFHDfGLSLGLLGPLL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 478 LGAQLYVPTQDDIGTPGRLAEWMSKYGCTVTHLTPAMGQLLTAQATTP---FPKLHHAFFVGDILTKRDCLRLQTLAeNC 554
Cdd:pfam00501 225 AGATVVLPPGFPALDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKralLSSLRLVLSGGAPLPPELARRFRELF-GG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 555 RIVNMYGTTETQRAVSYfevkskndDPNFLKKLKDVMPAGKGMLNVQLLVVNRNDRtQICGIGEIGEIYVRAGGLAEGYR 634
Cdd:pfam00501 304 ALVNGYGLTETTGVVTT--------PLPLDEDLRSLGSVGRPLPGTEVKIVDDETG-EPVPPGEPGELCVRGPGVMKGYL 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6319591 635 GLPELNKEKFVNnwfvekdhwnyldkdngepwrqfwlgprDRLYRTGDLGRYLPNGDCECCGRADDQVKIR 705
Cdd:pfam00501 375 NDPELTAEAFDE----------------------------DGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
268-821 |
4.50e-71 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 245.74 E-value: 4.50e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 268 RSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFSVIDPAYPPARqtiylgvakprgliv 347
Cdd:cd17649 11 QSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAER--------------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 348 iraagqLDQLVEDyindeleivSRINSIAIQEngtieggkldngedvlapydhykdtrtgvvvgPDSNPTLSFTSGSEGI 427
Cdd:cd17649 76 ------LRYMLED---------SGAGLLLTHH--------------------------------PRQLAYVIYTSGSTGT 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 428 PKGVLGRHFSLAYYFNWMSKRFNLTENDKFTMLSGIAHDPIQRDMFTPLFLGAQLYVPTQDDIGTPGRLAEWMSKYGCTV 507
Cdd:cd17649 109 PKGVAVSHGPLAAHCQATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTV 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 508 THLTPAMGQLLTAQA----TTPFPKLHHAFFVGDILTKrDCLRlQTLAENCRIVNMYGTTETQRAVSYFEVKSKNddpnf 583
Cdd:cd17649 189 LDLPPAYLQQLAEEAdrtgDGRPPSLRLYIFGGEALSP-ELLR-RWLKAPVRLFNAYGPTEATVTPLVWKCEAGA----- 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 584 lKKLKDVMPAGKGMLNVQLLVVNrnDRTQICGIGEIGEIYVRAGGLAEGYRGLPELNKEKFVNNWFvekdhwnyldkdng 663
Cdd:cd17649 262 -ARAGASMPIGRPLGGRSAYILD--ADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPF-------------- 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 664 epwrqfwLGPRDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRkNADNEPTLIT 743
Cdd:cd17649 325 -------GAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVAL-DGAGGKQLVA 396
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6319591 744 FMVPRfdkpddlskfqsdVPKEVETDPivkgligyhllsKDIRTFLKKRLASYAMPSLIVVMDKLPLNPNGKVDKPKL 821
Cdd:cd17649 397 YVVLR-------------AAAAQPELR------------AQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKAL 449
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
240-821 |
1.98e-70 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 243.62 E-value: 1.98e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 240 HDIFQDNAEAFPERTCVVetptlnsDKSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGA 319
Cdd:cd17645 1 HQLFEEQVERTPDHVAVV-------DRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 320 TFSVIDPAYPPARqtiylgvakprgliviraagqldqlvedyindeleivsrinsiaiqengtIEGGKLDNGEDVLapyd 399
Cdd:cd17645 74 AYVPIDPDYPGER--------------------------------------------------IAYMLADSSAKIL---- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 400 hykdtrtgvVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFNWMSKRFNLTENDKFTMLSGIAHDPIQRDMFTPLFLG 479
Cdd:cd17645 100 ---------LTNPDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAG 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 480 AQLYVPTQDDIGTPGRLAEWMSKYGCTVTHL-TPAMGQLLTAQattpfpklHHAFFVgdILTKRDclRLQTLAENC-RIV 557
Cdd:cd17645 171 AALHVVPSERRLDLDALNDYFNQEGITISFLpTGAAEQFMQLD--------NQSLRV--LLTGGD--KLKKIERKGyKLV 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 558 NMYGTTETQRAVSYFEVkskndDPNFLKklkdvMPAGKGMLNVQLLVVNRNdrTQICGIGEIGEIYVRAGGLAEGYRGLP 637
Cdd:cd17645 239 NNYGPTENTVVATSFEI-----DKPYAN-----IPIGKPIDNTRVYILDEA--LQLQPIGVAGELCIAGEGLARGYLNRP 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 638 ELNKEKFVNNWFVekdhwnyldkdngepwrqfwlgPRDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTH 717
Cdd:cd17645 307 ELTAEKFIVHPFV----------------------PGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPF 364
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 718 ISQHPLVRENITLVRKNADNEPTLITFMVPrfdkpddlskfqsdvPKEVETDpivkgligyhllskDIRTFLKKRLASYA 797
Cdd:cd17645 365 LMNHPLIELAAVLAKEDADGRKYLVAYVTA---------------PEEIPHE--------------ELREWLKNDLPDYM 415
|
570 580
....*....|....*....|....
gi 6319591 798 MPSLIVVMDKLPLNPNGKVDKPKL 821
Cdd:cd17645 416 IPTYFVHLKALPLTANGKVDRKAL 439
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
251-821 |
2.53e-70 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 244.12 E-value: 2.53e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 251 PERTCVvetptlnSDKSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFSVIDPAYPP 330
Cdd:cd12116 1 PDATAV-------RDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 331 ARQTIYLGVAKPrGLIVIRAAGqldqlvEDyindeleivsrinsiaiqengtieggKLDNGEDVLA---PYDHYKDTRTG 407
Cdd:cd12116 74 DRLRYILEDAEP-ALVLTDDAL------PD--------------------------RLPAGLPVLLlalAAAAAAPAAPR 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 408 VVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFNWMSKRFNLTENDKFTMLSGIAHDPIQRDMFTPLFLGAQLYVPTQ 487
Cdd:cd12116 121 TPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPR 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 488 DDIGTPGRLAEWMSKYGCTVTHLTPAMGQLLTAQATTPFPKLHhAFFVGDILTKRdcLRLQTLAENCRIVNMYGTTETQR 567
Cdd:cd12116 201 ETQRDPEALARLIEAHSITVMQATPATWRMLLDAGWQGRAGLT-ALCGGEALPPD--LAARLLSRVGSLWNLYGPTETTI 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 568 AVSYFEVKSKNDDPnflkklkdvmPAGKGMLNVQLLVVNrnDRTQICGIGEIGEIYVRAGGLAEGYRGLPELNKEKFVNN 647
Cdd:cd12116 278 WSTAARVTAAAGPI----------PIGRPLANTQVYVLD--AALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPD 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 648 WFvekdhwnyldkdngepwrqfwLGPRDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVREN 727
Cdd:cd12116 346 PF---------------------AGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQA 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 728 ITLVRKNaDNEPTLITFMVPRFDKPDDLSkfqsdvpkevetdpivkgligyhllskDIRTFLKKRLASYAMPSLIVVMDK 807
Cdd:cd12116 405 AVVVRED-GGDRRLVAYVVLKAGAAPDAA---------------------------ALRAHLRATLPAYMVPSAFVRLDA 456
|
570
....*....|....
gi 6319591 808 LPLNPNGKVDKPKL 821
Cdd:cd12116 457 LPLTANGKLDRKAL 470
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
266-821 |
2.92e-68 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 237.15 E-value: 2.92e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 266 KSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFSVIDPAYPPARQTIYLGVAKPRgl 345
Cdd:cd17652 9 GDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPA-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 346 IVIRAAGQLDqlvedYIndeleivsrinsiaiqengtieggkldngedvlapydhykdtrtgvvvgpdsnptlSFTSGSE 425
Cdd:cd17652 87 LLLTTPDNLA-----YV--------------------------------------------------------IYTSGST 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 426 GIPKGVLGRHFSLAYYFNWMSKRFNLTENDKFTMLSGIAHDPIQRDMFTPLFLGAQLYVPTQDDIGTPGRLAEWMSKYGC 505
Cdd:cd17652 106 GRPKGVVVTHRGLANLAAAQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRI 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 506 TVTHLTPAmgqLLTAQATTPFPKLHHAFFVGDILTKRdclRLQTLAENCRIVNMYGTTETQRAVSYFEVKSKNDDPnflk 585
Cdd:cd17652 186 THVTLPPA---ALAALPPDDLPDLRTLVVAGEACPAE---LVDRWAPGRRMINAYGPTETTVCATMAGPLPGGGVP---- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 586 klkdvmPAGKGMLNVQLLVVNrnDRTQICGIGEIGEIYVRAGGLAEGYRGLPELNKEKFVNNWFVekdhwnyldkdngep 665
Cdd:cd17652 256 ------PIGRPVPGTRVYVLD--ARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFG--------------- 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 666 wrqfwlGPRDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRKNADNEPTLITFM 745
Cdd:cd17652 313 ------APGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYV 386
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6319591 746 VPRFDKPDDlskfqsdvpkevetdpivkgligyhllSKDIRTFLKKRLASYAMPSLIVVMDKLPLNPNGKVDKPKL 821
Cdd:cd17652 387 VPAPGAAPT---------------------------AAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
239-821 |
1.68e-67 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 235.29 E-value: 1.68e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 239 IHDIFQDNAEAFPERTCVVetptlnsDKSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAG 318
Cdd:cd12115 1 LHDLVEAQAARTPDAIALV-------CGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 319 ATFSVIDPAYPPARQTIYLGVAKPRGLIViraagQLDQLVedYIndeleivsrinsiaiqengtieggkldngedvlapy 398
Cdd:cd12115 74 AAYVPLDPAYPPERLRFILEDAQARLVLT-----DPDDLA--YV------------------------------------ 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 399 dhykdtrtgvvvgpdsnptlSFTSGSEGIPKGVLGRHFSLAYYFNWMSKRFNLTEndkftmLSGI-AHDPIQRD-----M 472
Cdd:cd12115 111 --------------------IYTSGSTGRPKGVAIEHRNAAAFLQWAAAAFSAEE------LAGVlASTSICFDlsvfeL 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 473 FTPLFLGAQLyVPTQDDIGTP--GRLAEwmskygCTVTHLTP-AMGQLLTAQAttpFPK-LHHAFFVGDILTKRDCLRLQ 548
Cdd:cd12115 165 FGPLATGGKV-VLADNVLALPdlPAAAE------VTLINTVPsAAAELLRHDA---LPAsVRVVNLAGEPLPRDLVQRLY 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 549 TLAENCRIVNMYGTTETQRAVSYFEVKSKNDDPnflkklkdvMPAGKGMLNVQLLVVNRNdrTQICGIGEIGEIYVRAGG 628
Cdd:cd12115 235 ARLQVERVVNLYGPSEDTTYSTVAPVPPGASGE---------VSIGRPLANTQAYVLDRA--LQPVPLGVPGELYIGGAG 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 629 LAEGYRGLPELNKEKFVNNWFvekdhwnyldkdngepwrqfwlGPRDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFR 708
Cdd:cd12115 304 VARGYLGRPGLTAERFLPDPF----------------------GPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFR 361
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 709 IELGEIDTHISQHPLVRENITLVRKNADNEPTLITFMVPRFDKPddlskfqsdvpkevetdpivkgligyhLLSKDIRTF 788
Cdd:cd12115 362 IELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAA---------------------------GLVEDLRRH 414
|
570 580 590
....*....|....*....|....*....|...
gi 6319591 789 LKKRLASYAMPSLIVVMDKLPLNPNGKVDKPKL 821
Cdd:cd12115 415 LGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
241-822 |
2.67e-66 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 231.43 E-value: 2.67e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 241 DIFQDNAEAFPERTCVvetptlnSDKSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGAT 320
Cdd:cd17653 1 DAFERIAAAHPDAVAV-------ESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 321 FSVIDPAYPPARQTIYLGVAKPRGLIViraagqldqlvedyindeleivsrinsiaiqengtieggkLDNGEDVLApydh 400
Cdd:cd17653 74 YVPLDAKLPSARIQAILRTSGATLLLT----------------------------------------TDSPDDLAY---- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 401 ykdtrtgvvvgpdsnptLSFTSGSEGIPKGVLGRHFSLAYYFNWMSKRFNLTENDKFTMLSGIAHDPIQRDMFTPLFLGA 480
Cdd:cd17653 110 -----------------IIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGG 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 481 QLYVPT-QDDIGTPGRlaewmskyGCTVTHLTPAMGQLLTAQattPFPKLHHAFFVGDILTKRdclRLQTLAENCRIVNM 559
Cdd:cd17653 173 TLVLADpSDPFAHVAR--------TVDALMSTPSILSTLSPQ---DFPNLKTIFLGGEAVPPS---LLDRWSPGRRLYNA 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 560 YGTTETQRAVSYFEVKSknDDPNFLkklkdvmpaGKGMLNVQLLVVNRNDRTQIcgIGEIGEIYVRAGGLAEGYRGLPEL 639
Cdd:cd17653 239 YGPTECTISSTMTELLP--GQPVTI---------GKPIPNSTCYILDADLQPVP--EGVVGEICISGVQVARGYLGNPAL 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 640 NKEKFVNNWFVekdhwnyldkdNGEpwrqfwlgprdRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEI-DTHI 718
Cdd:cd17653 306 TASKFVPDPFW-----------PGS-----------RMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIeEVVL 363
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 719 SQHPLVRENITLVRKNadnepTLITFMVPrfdkpddlskfqSDVPKEvetdpivkgligyhllskDIRTFLKKRLASYAM 798
Cdd:cd17653 364 QSQPEVTQAAAIVVNG-----RLVAFVTP------------ETVDVD------------------GLRSELAKHLPSYAV 408
|
570 580
....*....|....*....|....
gi 6319591 799 PSLIVVMDKLPLNPNGKVDKPKLQ 822
Cdd:cd17653 409 PDRIIALDSFPLTANGKVDRKALR 432
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
251-821 |
6.65e-65 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 228.90 E-value: 6.65e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 251 PERTCVVetptlnsDKSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFSVIDPAYPP 330
Cdd:cd17656 2 PDAVAVV-------FENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 331 ARQTIYLGVAKPRGLIVIRAagqldqlVEDYINDELEIVSRINSIAIQENGtiEGGKLDNGEDVLApydhykdtrtgvvv 410
Cdd:cd17656 75 ERRIYIMLDSGVRVVLTQRH-------LKSKLSFNKSTILLEDPSISQEDT--SNIDYINNSDDLL-------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 411 gpdsnpTLSFTSGSEGIPKGVLGRHFSLAYYFNWMSKRFNLTENDKFTMLSGIAHDPIQRDMFTPLFLGAQLYVPTQDDI 490
Cdd:cd17656 132 ------YIIYTSGTTGKPKGVQLEHKNMVNLLHFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETK 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 491 GTPGRLAEWMSKYGCTVTHLTPAMGQLLTA--QATTPFPK-LHHAFFVGDILTKRDCLRLQTLAENCRIVNMYGTTETQr 567
Cdd:cd17656 206 RDVEQLFDLVKRHNIEVVFLPVAFLKFIFSerEFINRFPTcVKHIITAGEQLVITNEFKEMLHEHNVHLHNHYGPSETH- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 568 AVSYFEVKSKNDDPnflkklkDVMPAGKGMLNVQLLVVNRNDRTQICGIgeIGEIYVRAGGLAEGYRGLPELNKEKFVNN 647
Cdd:cd17656 285 VVTTYTINPEAEIP-------ELPPIGKPISNTWIYILDQEQQLQPQGI--VGELYISGASVARGYLNRQELTAEKFFPD 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 648 wfvekdhwnyldkdngePWRqfwlgPRDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVREN 727
Cdd:cd17656 356 -----------------PFD-----PNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEA 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 728 ITLVRKNADNEPTLITFMVPrfdkpddlskfqsdvpkeVETDPIVkgligyhllskDIRTFLKKRLASYAMPSLIVVMDK 807
Cdd:cd17656 414 VVLDKADDKGEKYLCAYFVM------------------EQELNIS-----------QLREYLAKQLPEYMIPSFFVPLDQ 464
|
570
....*....|....
gi 6319591 808 LPLNPNGKVDKPKL 821
Cdd:cd17656 465 LPLTPNGKVDRKAL 478
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
251-821 |
8.27e-61 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 216.11 E-value: 8.27e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 251 PERTCVVetptlnsDKSRSFTYRDINRTSNIVAHYLIKTGIKRGD-VVMIYSSRGVDLMVCVMGVLKAGATFSVIDPAYP 329
Cdd:cd17648 1 PDRVAVV-------YGDKRLTYRELNERANRLAHYLLSVAEIRPDdLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 330 PARQTIYLGVAKPRGLIviraagqldqlvedyindeleivsrinsiaiqengtieggkldngedvlapydhykdtrtgvv 409
Cdd:cd17648 74 DERIQFILEDTGARVVI--------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 410 vgpdSNPT----LSFTSGSEGIPKGVLGRHFSLAYYFNWMSKRFNLTENDKFTML--SGIAHDPIQRDMFTPLFLGAQLY 483
Cdd:cd17648 91 ----TNSTdlayAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGRDNGDEAVLffSNYVFDFFVEQMTLALLNGQKLV 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 484 VPTQDDIGTPGRLAEWMSKYGCTVTHLTPAMGQLLTAQAttpFPKLHHAFFVGDILTKR--DCLRlQTLAEncRIVNMYG 561
Cdd:cd17648 167 VPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQQYDLAR---LPHLKRVDAAGEEFTAPvfEKLR-SRFAG--LIINAYG 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 562 TTETqrAVsYFEVKSKNDDPNFLKKLkdvmpaGKGMLNVQLLVVNrnDRTQICGIGEIGEIYVRAGGLAEGYRGLPELNK 641
Cdd:cd17648 241 PTET--TV-TNHKRFFPGDQRFDKSL------GRPVRNTKCYVLN--DAMKRVPVGAVGELYLGGDGVARGYLNRPELTA 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 642 EKFVNNWFvekdhwnYLDKDngepwRQfwLGPRDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQH 721
Cdd:cd17648 310 ERFLPNPF-------QTEQE-----RA--RGRNARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASY 375
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 722 PLVRENITLVRKNADNEPTlitfmvprfdkpddlskfqsdvpkevetdPIVKGLIGYHLLSK------DIRTFLKKRLAS 795
Cdd:cd17648 376 PGVRECAVVAKEDASQAQS-----------------------------RIQKYLVGYYLPEPghvpesDLLSFLRAKLPR 426
|
570 580
....*....|....*....|....*.
gi 6319591 796 YAMPSLIVVMDKLPLNPNGKVDKPKL 821
Cdd:cd17648 427 YMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
63-929 |
1.59e-58 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 223.89 E-value: 1.59e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 63 AALIYRVTGDDDivLYIA-------------------NNKILRFNIQPTWSFNELYSTINNELNKLNSiEANFSFDELAE 123
Cdd:PRK05691 1984 AALLYRYSGQRD--LRIGapvanrirpesegligaflNTQVLRCQLDGQMSVSELLEQVRQTVIEGQS-HQDLPFDHLVE 2060
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 124 KIQSCQDLERTPqLF-------RLAFLENQDFKLDEFKHHLVD-----FALNLDTSNNAHVLN--LIYNSLLYSNERVTI 189
Cdd:PRK05691 2061 ALQPPRSAAYNP-LFqvmcnvqRWEFQQSRQLAGMTVEYLVNDaratkFDLNLEVTDLDGRLGccLTYSRDLFDEPRIAR 2139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 190 VADQFTQYLTAALSDPSNCITKISLITASSKDSLPDPTkNLGWCDFV--GCIHDIFQDNAEAFPErtcvveTPTLNSDkS 267
Cdd:PRK05691 2140 MAEHWQNLLEALLGDPQQRLAELPLLAAAEQQQLLDSL-AGEAGEARldQTLHGLFAAQAARTPQ------APALTFA-G 2211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 268 RSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFSVIDPAYPPARqtiylgvakprgliv 347
Cdd:PRK05691 2212 QTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLER--------------- 2276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 348 iraagqLDQLVEDyindeleivSRINSIAIQENGTIEGGKLDNG------EDVLAPYDHYKDTRTGVVVGPDSNPTLSFT 421
Cdd:PRK05691 2277 ------LHYMIED---------SGIGLLLSDRALFEALGELPAGvarwclEDDAAALAAYSDAPLPFLSLPQHQAYLIYT 2341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 422 SGSEGIPKGVLGRHFSLAYYFNWMSKRFNLTENDKFTMLSGIAHDPIQRDMFTPLFLGAQLYVPTQDDIGTPgRLAEWMS 501
Cdd:PRK05691 2342 SGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGARVVLRAQGQWGAE-EICQLIR 2420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 502 KYGCTVTHLTPAMGQ-----LLTAQATTPfpkLHHAFFVGDILTKRDCLRLQTLAENCRIVNMYGTTETQRAvsyfevks 576
Cdd:PRK05691 2421 EQQVSILGFTPSYGSqlaqwLAGQGEQLP---VRMCITGGEALTGEHLQRIRQAFAPQLFFNAYGPTETVVM-------- 2489
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 577 knddPnfLKKLK-DVMPAGKGMLNVQLLVVNR-----NDRTQICGIGEIGEIYVRAGGLAEGYRGLPELNKEKFVNNWFv 650
Cdd:PRK05691 2490 ----P--LACLApEQLEEGAASVPIGRVVGARvayilDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPF- 2562
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 651 ekdhwnylDKDNGepwrqfwlgprdRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITL 730
Cdd:PRK05691 2563 --------AADGG------------RLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVL 2622
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 731 VRKNADNEpTLITFMVPRFDKPDDLSKFQsdvpkevetdpivkgligyhlLSKDIRTFLKKRLASYAMPSLIVVMDKLPL 810
Cdd:PRK05691 2623 ALDTPSGK-QLAGYLVSAVAGQDDEAQAA---------------------LREALKAHLKQQLPDYMVPAHLILLDSLPL 2680
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 811 NPNGKVDKPKLQFPTPKQLNLVAENTVSEtddsqftnVEREVRDLWLSILPTkpASVSPDDSFFDLGGHSILATKMIfTL 890
Cdd:PRK05691 2681 TANGKLDRRALPAPDPELNRQAYQAPRSE--------LEQQLAQIWREVLNV--ERVGLGDNFFELGGDSILSIQVV-SR 2749
|
890 900 910 920
....*....|....*....|....*....|....*....|..
gi 6319591 891 KKKLQVDLPLGTIFKYPTIKAFAAEIDR---IKSSGGSSQGE 929
Cdd:PRK05691 2750 ARQLGIHFSPRDLFQHQTVQTLAAVATHseaAQAEQGPLQGA 2791
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
242-927 |
1.52e-57 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 220.42 E-value: 1.52e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 242 IFQDNAEAFPERTCVvetptlnSDKSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATF 321
Cdd:PRK05691 3725 LFEAQVAAHPQRIAA-------SCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGY 3797
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 322 SVIDPAYPPARQTIYLGVAkpRGLIVIRAAGQLDQLVEdyINDELEIVSRinsiaiqengtiegGKLDNGEDVLApyDHY 401
Cdd:PRK05691 3798 LPLDPGLPAQRLQRIIELS--RTPVLVCSAACREQARA--LLDELGCANR--------------PRLLVWEEVQA--GEV 3857
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 402 KDTRTGVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYyfNWMSK--RFNLTENDKFTMLSGIAHD-PIQRDMFTPLFl 478
Cdd:PRK05691 3858 ASHNPGIYSGPDNLAYVIYTSGSTGLPKGVMVEQRGMLN--NQLSKvpYLALSEADVIAQTASQSFDiSVWQFLAAPLF- 3934
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 479 GAQLYVPTQDDIGTPGRLAEWMSKYGCTVTHLTPAMGQLLTAQATTPFPKLHHAFFVGDILTKRdcLRLQTLAENCRI-- 556
Cdd:PRK05691 3935 GARVEIVPNAIAHDPQGLLAHVQAQGITVLESVPSLIQGMLAEDRQALDGLRWMLPTGEAMPPE--LARQWLQRYPQIgl 4012
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 557 VNMYGTTETQRAVSYFEVKSKNDDPNFLkklkdvmPAGKGMLNVQLLVVNrnDRTQICGIGEIGEIYVRAGGLAEGYRGL 636
Cdd:PRK05691 4013 VNAYGPAECSDDVAFFRVDLASTRGSYL-------PIGSPTDNNRLYLLD--EALELVPLGAVGELCVAGTGVGRGYVGD 4083
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 637 PELNKEKFVNNWFVekdhwnyldkdngepwrqfwlGPRDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDT 716
Cdd:PRK05691 4084 PLRTALAFVPHPFG---------------------APGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEA 4142
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 717 HISQHPLVRENITLVRKNAdNEPTLITFMVPRfdkpddlSKFQSDVPkevetdpivkgligyhlLSKDIRTFLKKRLASY 796
Cdd:PRK05691 4143 RLHEQAEVREAAVAVQEGV-NGKHLVGYLVPH-------QTVLAQGA-----------------LLERIKQRLRAELPDY 4197
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 797 AMPSLIVVMDKLPLNPNGKVDKPKLqfPTPKQLNLVAENTVSETDDsqftnVEREVRDLWLSILptKPASVSPDDSFFDL 876
Cdd:PRK05691 4198 MVPLHWLWLDRLPLNANGKLDRKAL--PALDIGQLQSQAYLAPRNE-----LEQTLATIWADVL--KVERVGVHDNFFEL 4268
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 6319591 877 GGHSILATKMIFTLKKKLQVDLPLGTIFKYPTIKAFAAEIDRIKSSGGSSQ 927
Cdd:PRK05691 4269 GGHSLLATQIASRVQKALQRNVPLRAMFECSTVEELAEYIEGLAGSAIDEQ 4319
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
420-817 |
9.89e-50 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 180.17 E-value: 9.89e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 420 FTSGSEGIPKGVLGRHFSLAYYFNWMSKRFNLTENDKFTMLSGIAHDPIQRDMFTPLFLGAQLYVPTQDDigtPGRLAEW 499
Cdd:cd04433 7 YTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFD---PEAALEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 500 MSKYGCTVTHLTPAMGQLLTAQ---ATTPFPKLHHAFFVGDILTKRDCLRLQTlAENCRIVNMYGTTETQRAVSYFEVks 576
Cdd:cd04433 84 IEREKVTILLGVPTLLARLLKApesAGYDLSSLRALVSGGAPLPPELLERFEE-APGIKLVNGYGLTETGGTVATGPP-- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 577 knddPNFLKKLKDVmpaGKGMLNVQLLVVNRNDRTqiCGIGEIGEIYVRAGGLAEGYRGLPELNKEKFVNNWfvekdhwn 656
Cdd:cd04433 161 ----DDDARKPGSV---GRPVPGVEVRIVDPDGGE--LPPGEIGELVVRGPSVMKGYWNNPEATAAVDEDGW-------- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 657 yldkdngepwrqfwlgprdrlYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRKNAD 736
Cdd:cd04433 224 ---------------------YRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPE 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 737 NEPTLITFMVPRFDKPddlskfqsdvpkevetdpivkgligyhLLSKDIRTFLKKRLASYAMPSLIVVMDKLPLNPNGKV 816
Cdd:cd04433 283 WGERVVAVVVLRPGAD---------------------------LDAEELRAHVRERLAPYKVPRRVVFVDALPRTASGKI 335
|
.
gi 6319591 817 D 817
Cdd:cd04433 336 D 336
|
|
| D-ala-DACP-lig |
TIGR01734 |
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ... |
239-821 |
8.55e-49 |
|
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also called D-alanine-D-alanyl carrier protein ligase) which activates D-alanine as an adenylate via the reaction D-ala + ATP -> D-ala-AMP + PPi, and further catalyzes the condensation of the amino acid adenylate with the D-alanyl carrier protein (D-ala-ACP). The D-alanine is then further transferred to teichoic acid in the biosynthesis of lipoteichoic acid (LTA) and wall teichoic acid (WTA) in gram positive bacteria, both polysacchatides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273780 [Multi-domain] Cd Length: 502 Bit Score: 182.27 E-value: 8.55e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 239 IHDIfQDNAEAFPERTCVVETPTlnsdksrSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAG 318
Cdd:TIGR01734 3 IEAI-QAFAETYPQTIAYRYQGQ-------ELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 319 ATFSVIDPAYPPARQTIYLGVAKPRGLIVIRAagqldqlvedyINDELEIVSRINsiaiqengtieggkLDNGEDVLApy 398
Cdd:TIGR01734 75 HAYIPVDTSIPSERIEMIIEAAGPELVIHTAE-----------LSIDAVGTQIIT--------------LSALEQAET-- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 399 DHYKDTRTGVVVGPDSNPTLsFTSGSEGIPKGVLGRHFSLAYYFNWMSKRFNLTENDKFTMLSGIAHDPIQRDMFTPLFL 478
Cdd:TIGR01734 128 SGGPVSFDHAVKGDDNYYII-YTSGSTGNPKGVQISHDNLVSFTNWMLADFPLSEGKQFLNQAPFSFDLSVMDLYPCLAS 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 479 GAQLYVPTQDDIGTPGRLAEWMSKYGCTVTHLTPA---MGQLLTAQATTPFPKLHHAFFVGDILTKRDCLRLQTLAENCR 555
Cdd:TIGR01734 207 GGTLHCLDKDITNNFKLLFEELPKTGLNVWVSTPSfvdMCLLDPNFNQENYPHLTHFLFCGEELPVKTAKALLERFPKAT 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 556 IVNMYGTTETQRAVSYFEVKSKNDDPNflkklkDVMPAGKGMLNVQLLVVnrNDRTQICGIGEIGEIYVRAGGLAEGYRG 635
Cdd:TIGR01734 287 IYNTYGPTEATVAVTSVKITQEILDQY------PRLPIGFAKPDMNLFIM--DEEGEPLPEGEKGEIVIVGPSVSKGYLN 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 636 LPELNKEKFvnnwFVEKDHWNyldkdngepwrqfwlgprdrlYRTGDLGrYLPNGDCECCGRADDQVKIRGFRIELGEID 715
Cdd:TIGR01734 359 NPEKTAEAF----FSHEGQPA---------------------YRTGDAG-TITDGQLFYQGRLDFQIKLHGYRIELEDIE 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 716 THISQHPLVRENITLVRKNADNEPT-LITFMVPrfdKPDDlskFQSDVpkevetdpivkgligyhLLSKDIRTFLKKRLA 794
Cdd:TIGR01734 413 FNLRQSSYIESAVVVPKYNKDHKVEyLIAAIVP---ETED---FEKEF-----------------QLTKAIKKELKKSLP 469
|
570 580
....*....|....*....|....*..
gi 6319591 795 SYAMPSLIVVMDKLPLNPNGKVDKPKL 821
Cdd:TIGR01734 470 AYMIPRKFIYRDQLPLTANGKIDRKAL 496
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
239-821 |
5.40e-48 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 180.09 E-value: 5.40e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 239 IHDI---FQDNAEAFPERTCVVETPTlnsdksrSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVL 315
Cdd:PRK04813 1 IMDIietIEEFAQTQPDFPAYDYLGE-------KLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 316 KAGATFSVIDPAYPPARQTIYLGVAKPRGLIvirAAGQLDQLVEDyindeleiVSRINSIAIQENGTieggkldngEDVL 395
Cdd:PRK04813 74 KAGHAYIPVDVSSPAERIEMIIEVAKPSLII---ATEELPLEILG--------IPVITLDELKDIFA---------TGNP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 396 APYDHYkdtrtgvvVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFNWMSKRFNLTENDKFtmlsgIAHDPIQRDM--- 472
Cdd:PRK04813 134 YDFDHA--------VKGDDNYYIIFTSGTTGKPKGVQISHDNLVSFTNWMLEDFALPEGPQF-----LNQAPYSFDLsvm 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 473 --FTPLFLGAQLYVPTQDDIGTPGRLAEWMSKYGCTVTHLTPA---MGQLLTAQATTPFPKLHHAFFVGDILTKRDCLRL 547
Cdd:PRK04813 201 dlYPTLASGGTLVALPKDMTANFKQLFETLPQLPINVWVSTPSfadMCLLDPSFNEEHLPNLTHFLFCGEELPHKTAKKL 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 548 QTLAENCRIVNMYGTTETQRAVSYFEVkskndDPNFLKKlKDVMPAGKGMLNVQLLVVNRNDrtQICGIGEIGEIYVRAG 627
Cdd:PRK04813 281 LERFPSATIYNTYGPTEATVAVTSIEI-----TDEMLDQ-YKRLPIGYAKPDSPLLIIDEEG--TKLPDGEQGEIVISGP 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 628 GLAEGYRGLPELNKEKFVnnwfvekdhwnyldKDNGEPwrqfwlgprdrLYRTGDLGrYLPNGDCECCGRADDQVKIRGF 707
Cdd:PRK04813 353 SVSKGYLNNPEKTAEAFF--------------TFDGQP-----------AYHTGDAG-YLEDGLLFYQGRIDFQIKLNGY 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 708 RIELGEIDTHISQHPLVRENITlVRKNADNEPT-LITFMVPRfdkpddlskfQSDVPKEVEtdpivkgligyhlLSKDIR 786
Cdd:PRK04813 407 RIELEEIEQNLRQSSYVESAVV-VPYNKDHKVQyLIAYVVPK----------EEDFEREFE-------------LTKAIK 462
|
570 580 590
....*....|....*....|....*....|....*
gi 6319591 787 TFLKKRLASYAMPSLIVVMDKLPLNPNGKVDKPKL 821
Cdd:PRK04813 463 KELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
265-816 |
5.90e-41 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 158.53 E-value: 5.90e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 265 DKSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFSVIDPAYPPARQTIYLGVAKPRG 344
Cdd:cd05911 6 DTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 345 LIVirAAGQLDQLVEdyINDELEIVSRINSIAIQENGTIEGGKLDNGEDvLAPYDHYKDTRtgvVVGPDSNPTLSFTSGS 424
Cdd:cd05911 86 IFT--DPDGLEKVKE--AAKELGPKDKIIVLDDKPDGVLSIEDLLSPTL-GEEDEDLPPPL---KDGKDDTAAILYSSGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 425 EGIPKGVL--GRHFSLAYYFNWMSKRFNLTENDKFTMLSGIAH---DPIqrdMFTPLFLGAQLYVPTQDDIGTPGRLAEw 499
Cdd:cd05911 158 TGLPKGVClsHRNLIANLSQVQTFLYGNDGSNDVILGFLPLYHiygLFT---TLASLLNGATVIIMPKFDSELFLDLIE- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 500 msKYGCTVTHLTPAMGQLLtaqATTP------FPKLHHAFFVGDILTKRDCLRLQTLAENCRIVNMYGTTETQRAVSYfe 573
Cdd:cd05911 234 --KYKITFLYLVPPIAAAL---AKSPlldkydLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGILTV-- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 574 vkskndDPNFLKKLKDVmpaGKGMLNVQLLVVNrNDRTQICGIGEIGEIYVRAGGLAEGYRGLPELNKEKFvnnwfvekd 653
Cdd:cd05911 307 ------NPDGDDKPGSV---GRLLPNVEAKIVD-DDGKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETF--------- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 654 hwnylDKDNgepwrqfWLgprdrlyRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVREnitlvrk 733
Cdd:cd05911 368 -----DEDG-------WL-------HTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVAD------- 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 734 nadneptlitfmVPRFDKPDDLSkfqSDVPKEVetdpIVKGLiGYHLLSKDIRTFLKKRLASYAmpSL---IVVMDKLPL 810
Cdd:cd05911 422 ------------AAVIGIPDEVS---GELPRAY----VVRKP-GEKLTEKEVKDYVAKKVASYK--QLrggVVFVDEIPK 479
|
....*.
gi 6319591 811 NPNGKV 816
Cdd:cd05911 480 SASGKI 485
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
239-821 |
1.73e-38 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 151.88 E-value: 1.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 239 IHDIFQDNAEAFPERTCVVETptlnsdkSRSFTYRDINRTSNIVAHYLIKTGIKRGDVV--MIYSSRgvDLMVCVMGVLK 316
Cdd:PRK06187 8 IGRILRHGARKHPDKEAVYFD-------GRRTTYAELDERVNRLANALRALGVKKGDRVavFDWNSH--EYLEAYFAVPK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 317 AGATFSVIDPAYPPArQTIY-LGVAKPRGLIVIRA-AGQLDQlvedyINDELEIVSRInsIAIQENGTIEGGKLDNG-ED 393
Cdd:PRK06187 79 IGAVLHPINIRLKPE-EIAYiLNDAEDRVVLVDSEfVPLLAA-----ILPQLPTVRTV--IVEGDGPAAPLAPEVGEyEE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 394 VLAP-YDHYKDtrtgVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFNWMSKRFNLTENDKF--------TMLSGIa 464
Cdd:PRK06187 151 LLAAaSDTFDF----PDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYlvivpmfhVHAWGL- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 465 hdpiqrdMFTPLFLGAQLYVPTQDDigtPGRLAEWMSKYGCTVTHLTPAMGQ-LLTAQATTP--FPKLHHAFFVGDILTK 541
Cdd:PRK06187 226 -------PYLALMAGAKQVIPRRFD---PENLLDLIETERVTFFFAVPTIWQmLLKAPRAYFvdFSSLRLVIYGGAALPP 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 542 ---RDCLRLQtlaeNCRIVNMYGTTETQRAVSYfeVKSKNDDPNFLKKLKDvmpAGKGMLNVQLLVVNRNDRTQICGIGE 618
Cdd:PRK06187 296 allREFKEKF----GIDLVQGYGMTETSPVVSV--LPPEDQLPGQWTKRRS---AGRPLPGVEARIVDDDGDELPPDGGE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 619 IGEIYVRAGGLAEGYRGLPELNKEKFVNNWfvekdhwnyldkdngepwrqfwlgprdrlYRTGDLGRYLPNGDCECCGRA 698
Cdd:PRK06187 367 VGEIIVRGPWLMQGYWNRPEATAETIDGGW-----------------------------LHTGDVGYIDEDGYLYITDRI 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 699 DDQVKIRGFRIELGEIDTHISQHPLVREnitlvrknadneptlitfmVPRFDKPDDlskfQSD-------VPKEVET-DP 770
Cdd:PRK06187 418 KDVIISGGENIYPRELEDALYGHPAVAE-------------------VAVIGVPDE----KWGerpvavvVLKPGATlDA 474
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 6319591 771 ivkgligyhllsKDIRTFLKKRLASYAMPSLIVVMDKLPLNPNGKVDKPKL 821
Cdd:PRK06187 475 ------------KELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| MupV_like_SDR_e |
cd05263 |
Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family ... |
973-1233 |
4.65e-37 |
|
Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family domains have the characteristic active site tetrad and a well-conserved NAD(P)-binding motif. This subgroup is not well characterized, its members are annotated as having a variety of putative functions. One characterized member is Pseudomonas fluorescens MupV a protein involved in the biosynthesis of Mupirocin, a polyketide-derived antibiotic. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187573 [Multi-domain] Cd Length: 293 Bit Score: 141.74 E-value: 4.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 973 VFVTGVTGFLGSYILADLLGRSpknysFKVFAHVRAKDEEAAFARLQKAGItygtwnekFASNIKVVLGDLSKSQFGLSD 1052
Cdd:cd05263 1 VFVTGGTGFLGRHLVKRLLENG-----FKVLVLVRSESLGEAHERIEEAGL--------EADRVRVLEGDLTQPNLGLSA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 1053 EKWMDLANTVDIIIHNGALVHWVYPYAKLRDPNVISTINVMSLAAVGKPKFFDFVSststldTEYyfnlsdklVSEGKPG 1132
Cdd:cd05263 68 AASRELAGKVDHVIHCAASYDFQAPNEDAWRTNIDGTEHVLELAARLDIQRFHYVS------TAY--------VAGNREG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 1133 ILESDDLmNSASGLTGGYGQSKWAAEYIIRRAGERgLRGCIVRPGYVTGASANGSSNTDDFLLRFLKGSVQLGK---IPD 1209
Cdd:cd05263 134 NIRETEL-NPGQNFKNPYEQSKAEAEQLVRAAATQ-IPLTVYRPSIVVGDSKTGRIEKIDGLYELLNLLAKLGRwlpMPG 211
|
250 260
....*....|....*....|....*
gi 6319591 1210 IENS-VNMVPVDHVARVVVATSLNP 1233
Cdd:cd05263 212 NKGArLNLVPVDYVADAIVYLSKKP 236
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
246-818 |
2.34e-35 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 140.82 E-value: 2.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 246 NAEAFPERTCVVetptlnsDKSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFSVId 325
Cdd:cd17631 4 RARRHPDRTALV-------FGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPL- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 326 paypPARQTiylgvakprglivirAAGQLDQLvedyindeleivsrinsiaiqengtieggkldngedvlapydhyKDTR 405
Cdd:cd17631 76 ----NFRLT---------------PPEVAYIL--------------------------------------------ADSG 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 406 TGVVVgpDSNPTLSFTSGSEGIPKGVLGRHFSL-AYYFNWMSKrFNLTENDKFTMLSGIAHDPiQRDMFTP--LFLGAQL 482
Cdd:cd17631 93 AKVLF--DDLALLMYTSGTTGRPKGAMLTHRNLlWNAVNALAA-LDLGPDDVLLVVAPLFHIG-GLGVFTLptLLRGGTV 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 483 YVPTQDDigtPGRLAEWMSKYGCTVTHLTPAMGQLLTAQ---ATTPFPKLHHAFFVGDILTKRdcLRLQTLAENCRIVNM 559
Cdd:cd17631 169 VILRKFD---PETVLDLIERHRVTSFFLVPTMIQALLQHprfATTDLSSLRAVIYGGAPMPER--LLRALQARGVKFVQG 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 560 YGTTETQRAVSyfevksknddpnFLKKlKDVM----PAGKGMLNVQLLVVNRNDRTqiCGIGEIGEIYVRAGGLAEGYRG 635
Cdd:cd17631 244 YGMTETSPGVT------------FLSP-EDHRrklgSAGRPVFFVEVRIVDPDGRE--VPPGEVGEIVVRGPHVMAGYWN 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 636 LPELNKEKFVNNWFvekdhwnyldkdngepwrqfwlgprdrlyRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEID 715
Cdd:cd17631 309 RPEATAAAFRDGWF-----------------------------HTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVE 359
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 716 THISQHPLVRENITLVRKNADNEPTLITFMVPRfdkpddlskfqsdvPKEVETDPivkgligyhllskDIRTFLKKRLAS 795
Cdd:cd17631 360 DVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPR--------------PGAELDED-------------ELIAHCRERLAR 412
|
570 580
....*....|....*....|...
gi 6319591 796 YAMPSLIVVMDKLPLNPNGKVDK 818
Cdd:cd17631 413 YKIPKSVEFVDALPRNATGKILK 435
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
240-816 |
8.42e-35 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 141.79 E-value: 8.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 240 HDIFQDNAEAFPERTCVV---ETptlnsDKSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLK 316
Cdd:COG0365 12 YNCLDRHAEGRGDKVALIwegED-----GEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 317 AGATFSVIDPAYPPA----RqtiyLGVAKPRGLIVirAAGQLDQLVEDYINDEL-EIVSRINS----IAIQengtieggk 387
Cdd:COG0365 87 IGAVHSPVFPGFGAEaladR----IEDAEAKVLIT--ADGGLRGGKVIDLKEKVdEALEELPSlehvIVVG--------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 388 lDNGEDVLAPYDH-YKDTRTGVVVGPDSNPTLS-------FTSGSEGIPKGVLgrHFS------LAYYFNWMskrFNLTE 453
Cdd:COG0365 152 -RTGADVPMEGDLdWDELLAAASAEFEPEPTDAddplfilYTSGTTGKPKGVV--HTHggylvhAATTAKYV---LDLKP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 454 NDKF---------TMLSGIahdpiqrdMFTPLFLGAQ--LY--VPTQDDigtPGRLAEWMSKYGCTVTHLTPA-----MG 515
Cdd:COG0365 226 GDVFwctadigwaTGHSYI--------VYGPLLNGATvvLYegRPDFPD---PGRLWELIEKYGVTVFFTAPTairalMK 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 516 QLLTAQATTPFPKLHHAFFVGDILTkrdclrlqtlAE---------NCRIVNMYGTTETQRAVSyfevkskndDPNFLKK 586
Cdd:COG0365 295 AGDEPLKKYDLSSLRLLGSAGEPLN----------PEvwewwyeavGVPIVDGWGQTETGGIFI---------SNLPGLP 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 587 LKdvmP--AGKGMLNVQLLVVnrNDRTQICGIGEIGEIYVRAG--GLAEGYRGLPELNKEKfvnnwfvekdhwnYLDKDN 662
Cdd:COG0365 356 VK---PgsMGKPVPGYDVAVV--DEDGNPVPPGEEGELVIKGPwpGMFRGYWNDPERYRET-------------YFGRFP 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 663 GepwrqfwlgprdrLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVREniTLVrknadneptli 742
Cdd:COG0365 418 G-------------WYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAE--AAV----------- 471
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 743 tfmVPrfdKPDDLsKFQsdvpkevetdpIVKGLI----GYHL---LSKDIRTFLKKRLASYAMPSLIVVMDKLPLNPNGK 815
Cdd:COG0365 472 ---VG---VPDEI-RGQ-----------VVKAFVvlkpGVEPsdeLAKELQAHVREELGPYAYPREIEFVDELPKTRSGK 533
|
.
gi 6319591 816 V 816
Cdd:COG0365 534 I 534
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
268-822 |
2.10e-29 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 122.79 E-value: 2.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 268 RSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFSVIDPAYPPARQTIYLGVAKPRGLIV 347
Cdd:cd05934 2 RRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 348 iraagqldqlvedyinDELEIVsrinsiaiqengtieggkldngedvlapydhykdtrtgvvvgpdsnptlsFTSGSEGI 427
Cdd:cd05934 82 ----------------DPASIL--------------------------------------------------YTSGTTGP 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 428 PKGVLGRHFSLAYYFNWMSKRFNLTENDkfTMLSgiahdpiqrdmFTPLF-LGAQLYVPTQDdIGTPGRLA--------E 498
Cdd:cd05934 96 PKGVVITHANLTFAGYYSARRFGLGEDD--VYLT-----------VLPLFhINAQAVSVLAA-LSVGATLVllprfsasR 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 499 WMS---KYGCTVTHLTPAMGQLLTAQATTPFPKLHhaffvgdiltkrdCLRLQTLAEN-------------CRIVNMYGT 562
Cdd:cd05934 162 FWSdvrRYGATVTNYLGAMLSYLLAQPPSPDDRAH-------------RLRAAYGAPNppelheefeerfgVRLLEGYGM 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 563 TETQRAVSyfevkSKNDDPNflkklkDVMPAGKGMLNVQLLVVNRNDRTqiCGIGEIGEIYVRAG---GLAEGYRGLPEL 639
Cdd:cd05934 229 TETIVGVI-----GPRDEPR------RPGSIGRPAPGYEVRIVDDDGQE--LPAGEPGELVIRGLrgwGFFKGYYNMPEA 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 640 NKEKFVNNWFvekdhwnyldkdngepwrqfwlgprdrlyRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHIS 719
Cdd:cd05934 296 TAEAMRNGWF-----------------------------HTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAIL 346
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 720 QHPLVREnitlvrknadneptlitfmVPRFDKPDDLSkfQSDVPKEVETDPivkgliGYHLLSKDIRTFLKKRLASYAMP 799
Cdd:cd05934 347 RHPAVRE-------------------AAVVAVPDEVG--EDEVKAVVVLRP------GETLDPEELFAFCEGQLAYFKVP 399
|
570 580
....*....|....*....|...
gi 6319591 800 SLIVVMDKLPLNPNGKVDKPKLQ 822
Cdd:cd05934 400 RYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
264-821 |
6.30e-29 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 122.86 E-value: 6.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 264 SDKSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFSVIDPAYPPARQTIYLGVAKPR 343
Cdd:cd05959 24 IDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRAR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 344 GLIViraAGQLDQLVEDYINDELEIVSRInsIAIQENGTiEGGKLDNGEDVLAPYDHYKDTRTGvvvgPDSNPTLSFTSG 423
Cdd:cd05959 104 VVVV---SGELAPVLAAALTKSEHTLVVL--IVSGGAGP-EAGALLLAELVAAEAEQLKPAATH----ADDPAFWLYSSG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 424 SEGIPKGVLGRHFSLAYYFNWMSKR-FNLTENDKFTMLSGIAHD-PIQRDMFTPLFLGAQ-LYVPTQDdigTPGRLAEWM 500
Cdd:cd05959 174 STGRPKGVVHLHADIYWTAELYARNvLGIREDDVCFSAAKLFFAyGLGNSLTFPLSVGATtVLMPERP---TPAAVFKRI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 501 SKYGCTVTHLTPAMGQLLTAQATTP---FPKLHHAFFVGDILTKRDCLRLQTLAeNCRIVNMYGTTETQRAvsyfevksk 577
Cdd:cd05959 251 RRYRPTVFFGVPTLYAAMLAAPNLPsrdLSSLRLCVSAGEALPAEVGERWKARF-GLDILDGIGSTEMLHI--------- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 578 nddpnFLKKL-KDVMPAGKGM----LNVQLlvvnRNDRTQICGIGEIGEIYVRAGGLAEGYRGLPELNKEKFVNNWfvek 652
Cdd:cd05959 321 -----FLSNRpGRVRYGTTGKpvpgYEVEL----RDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQGEW---- 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 653 dhwnyldkdngepwrqfwlgprdrlYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVR 732
Cdd:cd05959 388 -------------------------TRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGV 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 733 KNADNEPTLITFMVPRfdkpddlskfqsdvpkevetdpivKGLIGYHLLSKDIRTFLKKRLASYAMPSLIVVMDKLPLNP 812
Cdd:cd05959 443 EDEDGLTKPKAFVVLR------------------------PGYEDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTA 498
|
....*....
gi 6319591 813 NGKVDKPKL 821
Cdd:cd05959 499 TGKIQRFKL 507
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
269-821 |
1.29e-28 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 121.65 E-value: 1.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 269 SFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFSVIDPAYPPARQTIYLGVAKPRGLIVi 348
Cdd:cd05926 14 ALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLT- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 349 raagqldQLVEDYINDELEIVSRINSIAIQENGTIEGGKLDNGEDVLAPYDHYKDTRTGVVVGPDSNPTLsFTSGSEGIP 428
Cdd:cd05926 93 -------PKGELGPASRAASKLGLAILELALDVGVLIRAPSAESLSNLLADKKNAKSEGVPLPDDLALIL-HTSGTTGRP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 429 KGVLGRHFSLAYYFNWMSKRFNLTENDKfTML-------SGIAhdpiqRDMFTPLFLGAQLYVPtqddigtPGRLA---- 497
Cdd:cd05926 165 KGVPLTHRNLAASATNITNTYKLTPDDR-TLVvmplfhvHGLV-----ASLLSTLAAGGSVVLP-------PRFSAstfw 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 498 EWMSKYGCTVTHLTPAMGQ-LLTAQATTPFPKLHHAFFVgdiltkRDC---LRLQTLAE-----NCRIVNMYGTTETQRA 568
Cdd:cd05926 232 PDVRDYNATWYTAVPTIHQiLLNRPEPNPESPPPKLRFI------RSCsasLPPAVLEAleatfGAPVLEAYGMTEAAHQ 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 569 VsyfevkSKNDDPNFLKKLKDVmpaGKGMlNVQLLVVNRNDRTQicGIGEIGEIYVRAGGLAEGYRGLPELNKEK-FVNN 647
Cdd:cd05926 306 M------TSNPLPPGPRKPGSV---GKPV-GVEVRILDEDGEIL--PPGVVGEICLRGPNVTRGYLNNPEANAEAaFKDG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 648 WFvekdhwnyldkdngepwrqfwlgprdrlyRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVREN 727
Cdd:cd05926 374 WF-----------------------------RTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEA 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 728 ITlvrknadneptlitfmvprFDKPDDlsKFQSDV-----PKEvetdpivkgliGYHLLSKDIRTFLKKRLASYAMPSLI 802
Cdd:cd05926 425 VA-------------------FGVPDE--KYGEEVaaavvLRE-----------GASVTEEELRAFCRKHLAAFKVPKKV 472
|
570
....*....|....*....
gi 6319591 803 VVMDKLPLNPNGKVDKPKL 821
Cdd:cd05926 473 YFVDELPKTATGKIQRRKV 491
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
241-821 |
1.91e-27 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 119.08 E-value: 1.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 241 DIFQDNAEAFPERTCVVEtptlnsDKSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGAT 320
Cdd:PRK06087 27 DYWQQTARAMPDKIAVVD------NHGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 321 FSVIDPAYPPARQTIYLGVAKPRGLIViraagqldQLVEDYINDELEIVSRINSI-AIQENGTIEGGKLDNGEDVLAPY- 398
Cdd:PRK06087 101 SVPLLPSWREAELVWVLNKCQAKMFFA--------PTLFKQTRPVDLILPLQNQLpQLQQIVGVDKLAPATSSLSLSQIi 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 399 DHYKDTRTGVVVGPDSNPTLSFTSGSEGIPKGVLGRH----FSLAYYfnwmSKRFNLTENDKFTMLSGIAHDP-IQRDMF 473
Cdd:PRK06087 173 ADYEPLTTAITTHGDELAAVLFTSGTEGLPKGVMLTHnnilASERAY----CARLNLTWQDVFMMPAPLGHATgFLHGVT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 474 TPLFLGAQLYVptqDDIGTPGRLAEWMSKYGCTVTH-LTPAMGQLLTA--QATTPFPKLHhaFFV--GDILTK---RDCL 545
Cdd:PRK06087 249 APFLIGARSVL---LDIFTPDACLALLEQQRCTCMLgATPFIYDLLNLleKQPADLSALR--FFLcgGTTIPKkvaRECQ 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 546 RlqtlaENCRIVNMYGTTETQravsyfevksknddPNFLKKLKDVMP-----AGKGMLNVQLLVVNRNDRTQICGigEIG 620
Cdd:PRK06087 324 Q-----RGIKLLSVYGSTESS--------------PHAVVNLDDPLSrfmhtDGYAAAGVEIKVVDEARKTLPPG--CEG 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 621 EIYVRAGGLAEGYRGLPELNKEKfvnnwfvekdhwnyLDKDNgepwrqfWlgprdrlYRTGDLGRYLPNGDCECCGRADD 700
Cdd:PRK06087 383 EEASRGPNVFMGYLDEPELTARA--------------LDEEG-------W-------YYSGDLCRMDEAGYIKITGRKKD 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 701 qVKIRGFR-IELGEIDTHISQHPLVRENITLVRKNADNEPTLITFMvprfdkpddlskfqsdVPKEVETDPIVKGLIGYh 779
Cdd:PRK06087 435 -IIVRGGEnISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYV----------------VLKAPHHSLTLEEVVAF- 496
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 6319591 780 llskdirtFLKKRLASYAMPSLIVVMDKLPLNPNGKVDKPKL 821
Cdd:PRK06087 497 --------FSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLL 530
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
270-821 |
4.93e-27 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 115.90 E-value: 4.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 270 FTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGAtfsvidpaypparqtiylgvakprglIVIR 349
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGA--------------------------VYVP 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 350 AAGQLDqlvedyindELEIVSRInsiaiqengtieggkldngedvlapydhyKDTRTGVVVGPDSNP-TLSFTSGSEGIP 428
Cdd:cd05972 55 LTTLLG---------PKDIEYRL-----------------------------EAAGAKAIVTDAEDPaLIYFTSGTTGLP 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 429 KGVLgrHFSLAYYFNWMSKRF--NLTENDKFTMLSgiahDP-----IQRDMFTPLFLGAQLYVPTQDDIgTPGRLAEWMS 501
Cdd:cd05972 97 KGVL--HTHSYPLGHIPTAAYwlGLRPDDIHWNIA----DPgwakgAWSSFFGPWLLGATVFVYEGPRF-DAERILELLE 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 502 KYGCTVTHLTPAMGQLLTAQATTP--FPKLHHAFFVGDILTK------RDCLRLQtlaencrIVNMYGTTETQRAVSYFe 573
Cdd:cd05972 170 RYGVTSFCGPPTAYRMLIKQDLSSykFSHLRLVVSAGEPLNPeviewwRAATGLP-------IRDGYGQTETGLTVGNF- 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 574 vksknddpnflkKLKDVMP--AGKGMLNVQLLVVNRNDRtqICGIGEIGEIYVRAG--GLAEGYRGLPELNKEKFVNNWf 649
Cdd:cd05972 242 ------------PDMPVKPgsMGRPTPGYDVAIIDDDGR--ELPPGEEGDIAIKLPppGLFLGYVGDPEKTEASIRGDY- 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 650 vekdhwnyldkdngepwrqfwlgprdrlYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVREnit 729
Cdd:cd05972 307 ----------------------------YLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAE--- 355
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 730 lvrknadneptliTFMVPRfdkPDDLskfQSDVPKEVETdpIVKGLIGYHLLSKDIRTFLKKRLASYAMPSLIVVMDKLP 809
Cdd:cd05972 356 -------------AAVVGS---PDPV---RGEVVKAFVV--LTSGYEPSEELAEELQGHVKKVLAPYKYPREIEFVEELP 414
|
570
....*....|..
gi 6319591 810 LNPNGKVDKPKL 821
Cdd:cd05972 415 KTISGKIRRVEL 426
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
269-821 |
3.66e-26 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 113.24 E-value: 3.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 269 SFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFSVIDPAYPPARQTIYLGVAKPRGLIVI 348
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 349 RAAGQLDQLVEdyindeleivsrinsiaiqengtieggkldngedvlapydhykdtrtgvvvgPDSNPTLSFTSGSEGIP 428
Cdd:cd05903 81 ERFRQFDPAAM----------------------------------------------------PDAVALLLFTSGTTGEP 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 429 KGVLGRHFSLAYYFNWMSKRFNLTENDKFTMLSGIAHDP-IQRDMFTPLFLGAQLYVptqDDIGTPGRLAEWMSKYGCTV 507
Cdd:cd05903 109 KGVMHSHNTLSASIRQYAERLGLGPGDVFLVASPMAHQTgFVYGFTLPLLLGAPVVL---QDIWDPDKALALMREHGVTF 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 508 TH-LTPAMGQLLTAQATTPFPKLHHAFFV--GDILTKRDCLRLQTLAEnCRIVNMYGTTETQRAVSyfevkSKNDDPNFL 584
Cdd:cd05903 186 MMgATPFLTDLLNAVEEAGEPLSRLRTFVcgGATVPRSLARRAAELLG-AKVCSAYGSTECPGAVT-----SITPAPEDR 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 585 KKLKDvmpaGKGMLNVQLLVVNrnDRTQICGIGEIGEIYVRAGGLAEGYRGLPELNKEKFVNNWFvekdhwnyldkdnge 664
Cdd:cd05903 260 RLYTD----GRPLPGVEIKVVD--DTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAAPEGWF--------------- 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 665 pwrqfwlgprdrlyRTGDLGRYLPNGDCECCGRADDqVKIR-GFRIELGEIDTHISQHPLVRENITLVRKNADNEPTLIT 743
Cdd:cd05903 319 --------------RTGDLARLDEDGYLRITGRSKD-IIIRgGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACA 383
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 744 FMVPRfdkpddlskfqsdvpkevetDPivkgligyHLLSKD--IRTFLKKRLASYAMPSLIVVMDKLPLNPNGKVDKPKL 821
Cdd:cd05903 384 VVVTK--------------------SG--------ALLTFDelVAYLDRQGVAKQYWPERLVHVDDLPRTPSGKVQKFRL 435
|
|
| FAR-N_SDR_e |
cd05236 |
fatty acyl CoA reductases (FARs), extended (e) SDRs; SDRs are Rossmann-fold NAD(P)H-binding ... |
972-1249 |
1.69e-25 |
|
fatty acyl CoA reductases (FARs), extended (e) SDRs; SDRs are Rossmann-fold NAD(P)H-binding proteins, many of which may function as fatty acyl CoA reductases (FAR), acting on medium and long chain fatty acids, and have been reported to be involved in diverse processes such as biosynthesis of insect pheromones, plant cuticular wax production, and mammalian wax biosynthesis. In Arabidopsis thaliana, proteins with this particular architecture have also been identified as the MALE STERILITY 2 (MS2) gene product, which is implicated in male gametogenesis. Mutations in MS2 inhibit the synthesis of exine (sporopollenin), rendering plants unable to reduce pollen wall fatty acids to corresponding alcohols. This N-terminal domain shares the catalytic triad (but not the upstream Asn) and characteristic NADP-binding motif of the extended SDR family. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187547 [Multi-domain] Cd Length: 320 Bit Score: 108.92 E-value: 1.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 972 NVFVTGVTGFLGSYILADLLGRSPKNYsfKVFAHVRAKDEEAAFARLQKAGITYG-----TWNEKFASNIKVVLGDLSKS 1046
Cdd:cd05236 2 SVLITGATGFLGKVLLEKLLRSCPDIG--KIYLLIRGKSGQSAEERLRELLKDKLfdrgrNLNPLFESKIVPIEGDLSEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 1047 QFGLSDEKWMDLANTVDIIIHNGALVHWVYPYAKLRDPNVISTINVMSLA-AVGKPKFFDFVSSTstldteyYFNLSDKL 1125
Cdd:cd05236 80 NLGLSDEDLQTLIEEVNIIIHCAATVTFDERLDEALSINVLGTLRLLELAkRCKKLKAFVHVSTA-------YVNGDRQL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 1126 VSE----------GKPGILES-DDLMNSASGLTGGYGQ------SKWAAEYIIRRAGErGLRGCIVRPGYVTGASA---- 1184
Cdd:cd05236 153 IEEkvypppadpeKLIDILELmDDLELERATPKLLGGHpntytfTKALAERLVLKERG-NLPLVIVRPSIVGATLKepfp 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6319591 1185 --NGSSNTDD-FLLRFLKGSVQLgkIPDIENSV-NMVPVDHVAR--VVVATSLNPPKENELAVAQVTGHPR 1249
Cdd:cd05236 232 gwIDNFNGPDgLFLAYGKGILRT--MNADPNAVaDIIPVDVVANalLAAAAYSGVRKPRELEVYHCGSSDV 300
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
290-821 |
1.72e-25 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 111.76 E-value: 1.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 290 GIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFSVI----DPAYPPARQTIYLGVAKPRglIVIRAAGQLDQLvedyinDE 365
Cdd:cd05922 14 GGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVfvplNPTLKESVLRYLVADAGGR--IVLADAGAADRL------RD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 366 LEIVSRINSIAIQENGtieggkldngedvlapYDHYKDTRTGVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFNWM 445
Cdd:cd05922 86 ALPASPDPGTVLDADG----------------IRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 446 SKRFNLTENDK-FTMLsgiahdPIQRD-----MFTPLFLGAQLyVPTQDdiGTPGR-LAEWMSKYGCTVTHLTPAMGQLL 518
Cdd:cd05922 150 AEYLGITADDRaLTVL------PLSYDyglsvLNTHLLRGATL-VLTND--GVLDDaFWEDLREHGATGLAGVPSTYAML 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 519 T--AQATTPFPKLHHAFFVGDILTKRDCLRLQTLAENCRIVNMYGTTETQRAVSYFevkskndDPNFLKKLKDvmPAGKG 596
Cdd:cd05922 221 TrlGFDPAKLPSLRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTYL-------PPERILEKPG--SIGLA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 597 MLNVQLLVvnRNDRTQICGIGEIGEIYVRAGGLAEGYrglpelnkekfvnnwfvekdhWNyldkdnGEPWRQFWLGPRDR 676
Cdd:cd05922 292 IPGGEFEI--LDDDGTPTPPGEPGEIVHRGPNVMKGY---------------------WN------DPPYRRKEGRGGGV 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 677 LYrTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVREniTLVRKNADNEPTLITFMVPRFDKPDDls 756
Cdd:cd05922 343 LH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIE--AAAVGLPDPLGEKLALFVTAPDKIDP-- 417
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6319591 757 kfqsdvpkevetdpivkgligyhllsKDIRTFLKKRLASYAMPSLIVVMDKLPLNPNGKVDKPKL 821
Cdd:cd05922 418 --------------------------KDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
241-822 |
1.25e-24 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 109.19 E-value: 1.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 241 DIFQDNAEAFPERTCVVEtptlnsdKSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGAT 320
Cdd:cd05936 3 DLLEEAARRFPDKTALIF-------MGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 321 FSVIDPAYPPARQTIYLGVAKPRGLIVIRAAgqldqlvedyindeleivsrinsiaiqengtieggkldngEDVLAPydh 400
Cdd:cd05936 76 VVPLNPLYTPRELEHILNDSGAKALIVAVSF----------------------------------------TDLLAA--- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 401 YKDTRTGVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAY----YFNWMSkrFNLTENDK----------FTMLSGiahd 466
Cdd:cd05936 113 GAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVAnalqIKAWLE--DLLEGDDVvlaalplfhvFGLTVA---- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 467 piqrdMFTPLFLGAQLY-VPTQDDIGTpgrLAEwMSKYGCTVTHLTPAM-GQLLTAQATT--PFPKLHHAFFVGDIL--- 539
Cdd:cd05936 187 -----LLLPLALGATIVlIPRFRPIGV---LKE-IRKHRVTIFPGVPTMyIALLNAPEFKkrDFSSLRLCISGGAPLpve 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 540 TKRDCLRLQtlaeNCRIVNMYGTTETQRAVSYfevksknDDPNFLKKLKDVmpaGKGMLNVQLLVVnrNDRTQICGIGEI 619
Cdd:cd05936 258 VAERFEELT----GVPIVEGYGLTETSPVVAV-------NPLDGPRKPGSI---GIPLPGTEVKIV--DDDGEELPPGEV 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 620 GEIYVRAGGLAEGYRGLPELNKEKFVNNWFvekdhwnyldkdngepwrqfwlgprdrlyRTGDLGRYLPNGDCECCGRAD 699
Cdd:cd05936 322 GELWVRGPQVMKGYWNRPEETAEAFVDGWL-----------------------------RTGDIGYMDEDGYFFIVDRKK 372
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 700 DQVKIRGFRIELGEIDTHISQHPLVRENITLVRKNADNEPTLITFMVPRFDKPddlskfqsdvpkevetdpivkgligyh 779
Cdd:cd05936 373 DMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGAS--------------------------- 425
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 6319591 780 LLSKDIRTFLKKRLASYAMPSLIVVMDKLPLNPNGKVDKPKLQ 822
Cdd:cd05936 426 LTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
269-821 |
2.15e-24 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 108.33 E-value: 2.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 269 SFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFSVIDPAYPPARQTIYLGVAKprglivi 348
Cdd:cd17654 16 TVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCH------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 349 raagqldqlvedyindeleiVSRInsiaiqengtieggkLDNGEDVLAPYDHYKDTRTGVVVGPDSNPTLSFTSGSEGIP 428
Cdd:cd17654 89 --------------------VSYL---------------LQNKELDNAPLSFTPEHRHFNIRTDECLAYVIHTSGTTGTP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 429 KGVLGRHFSLAYYFNWMSKRFNLTENDKFTMLSGIAHDPIQRDMFTPLFLGAQL-YVPTQDDIgTPGRLAEWM-SKYGCT 506
Cdd:cd17654 134 KIVAVPHKCILPNIQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLSLSSGATLlIVPTSVKV-LPSKLADILfKRHRIT 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 507 VTHLTPAMGQLLTAQATTPFpklhhaffvgdILTKRDCLRLQTLA-ENC----------------RIVNMYGTTETQRAV 569
Cdd:cd17654 213 VLQATPTLFRRFGSQSIKST-----------VLSATSSLRVLALGgEPFpslvilsswrgkgnrtRIFNIYGITEVSCWA 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 570 SYFEVKSKnDDPnflkklkdvmpagkgmlnVQL---LVVNRNDRTQICGIGEIGEIYVraGGLAEGYrglpelnkekfvn 646
Cdd:cd17654 282 LAYKVPEE-DSP------------------VQLgspLLGTVIEVRDQNGSEGTGQVFL--GGLNRVC------------- 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 647 nwfvekdhwnYLDKDNGEPWRQFwlgprdrlYRTGDLGRyLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHplvRE 726
Cdd:cd17654 328 ----------ILDDEVTVPKGTM--------RATGDFVT-VKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESC---LG 385
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 727 NITLVRKNADNEpTLITFMVprfdkpddlskfqsdvpkevetDPIVKGLIgyhllSKDIRTFLkkrLASYAMPSLIVVMD 806
Cdd:cd17654 386 VESCAVTLSDQQ-RLIAFIV----------------------GESSSSRI-----HKELQLTL---LSSHAIPDTFVQID 434
|
570
....*....|....*
gi 6319591 807 KLPLNPNGKVDKPKL 821
Cdd:cd17654 435 KLPLTSHGKVDKSEL 449
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
395-822 |
1.33e-23 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 105.62 E-value: 1.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 395 LAPYDH---YKDTRTGVVV-GPDSNPTLSFTSGSEGIPKGVLGRH-FSLAYYFNWMSKRFNLTENDKFTMLS------GI 463
Cdd:cd05919 69 LHPDDYayiARDCEARLVVtSADDIAYLLYSSGTTGPPKGVMHAHrDPLLFADAMAREALGLTPGDRVFSSAkmffgyGL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 464 AHDpiqrdMFTPLFLGAQLYVptQDDIGTPGRLAEWMSKYGCTVTHLTPAMGQLLTAQATTP---FPKLHHAFFVGDILT 540
Cdd:cd05919 149 GNS-----LWFPLAVGASAVL--NPGWPTAERVLATLARFRPTVLYGVPTFYANLLDSCAGSpdaLRSLRLCVSAGEALP 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 541 KRDCLRLqTLAENCRIVNMYGTTETqravsyFEVksknddpnFLKKLKDVMPAGKGMLNV---QLLVVNRNDRTqiCGIG 617
Cdd:cd05919 222 RGLGERW-MEHFGGPILDGIGATEV------GHI--------FLSNRPGAWRLGSTGRPVpgyEIRLVDEEGHT--IPPG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 618 EIGEIYVRAGGLAEGYRGLPELNKEKFVNNWfvekdhwnyldkdngepwrqfwlgprdrlYRTGDLGRYLPNGDCECCGR 697
Cdd:cd05919 285 EEGDLLVRGPSAAVGYWNNPEKSRATFNGGW-----------------------------YRTGDKFCRDADGWYTHAGR 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 698 ADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRKNADNEPTLITFMVPRfdkpddlskfqsdvpkevetdpivKGLIG 777
Cdd:cd05919 336 ADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLK------------------------SPAAP 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 6319591 778 YHLLSKDIRTFLKKRLASYAMPSLIVVMDKLPLNPNGKVDKPKLQ 822
Cdd:cd05919 392 QESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| WcaG |
COG0451 |
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis]; |
972-1284 |
1.07e-22 |
|
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440220 [Multi-domain] Cd Length: 295 Bit Score: 100.05 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 972 NVFVTGVTGFLGSYILADLLGRspknySFKVFAHVRAKDEEAAFARLQkagitygtwnekfasNIKVVLGDLsksqfgLS 1051
Cdd:COG0451 1 RILVTGGAGFIGSHLARRLLAR-----GHEVVGLDRSPPGAANLAALP---------------GVEFVRGDL------RD 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 1052 DEKWMDLANTVDIIIHNGALVH-WVYPYAKLRDPNVISTINVMSLA-AVGKPKFFdFVSSTSTldteyyFNLSDKLVSEG 1129
Cdd:COG0451 55 PEALAAALAGVDAVVHLAAPAGvGEEDPDETLEVNVEGTLNLLEAArAAGVKRFV-YASSSSV------YGDGEGPIDED 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 1130 KPGILESDdlmnsasgltggYGQSKWAAEYIIRRAGER-GLRGCIVRPGYVTGasANGSSNTDDFLLRFLKGsVQLGKIP 1208
Cdd:COG0451 128 TPLRPVSP------------YGASKLAAELLARAYARRyGLPVTILRPGNVYG--PGDRGVLPRLIRRALAG-EPVPVFG 192
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6319591 1209 DIENSVNMVPVDHVARVVVATSLNPPKENElAVAQVTGHPrILFKDYLYTLHD-YGYDVEIEsYSKWKKSLEASVID 1284
Cdd:COG0451 193 DGDQRRDFIHVDDVARAIVLALEAPAAPGG-VYNVGGGEP-VTLRELAEAIAEaLGRPPEIV-YPARPGDVRPRRAD 266
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
239-821 |
2.79e-22 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 102.82 E-value: 2.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 239 IHDIFQDNAEAFPERTCVVEtPTLNSDKSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAG 318
Cdd:PRK13295 26 INDDLDACVASCPDKTAVTA-VRLGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 319 AtfsVIDPAYPPARQ---TIYLGVAKPRGLIViraagqlDQLVEDYinDELEIVSRINSI--AIQENGTIEGGKLDNGED 393
Cdd:PRK13295 105 A---VLNPLMPIFRErelSFMLKHAESKVLVV-------PKTFRGF--DHAAMARRLRPElpALRHVVVVGGDGADSFEA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 394 VLAPYDHYKDTRTGVVV-----GPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFNWMSKRFNLTENDKFTMLSGIAHDP- 467
Cdd:PRK13295 173 LLITPAWEQEPDAPAILarlrpGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTg 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 468 IQRDMFTPLFLGAQLYVptqDDIGTPGRLAEWMSKYGCTVTHL-TPAMGQLLTAQAT--TPFPKLhHAFFVGD-----IL 539
Cdd:PRK13295 253 FMYGLMMPVMLGATAVL---QDIWDPARAAELIRTEGVTFTMAsTPFLTDLTRAVKEsgRPVSSL-RTFLCAGapipgAL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 540 TKRDCLRLQTlaencRIVNMYGTTETQrAVSYFEVksknDDPNFLKKLKDVMPagkgMLNVQLLVVNRNDrtQICGIGEI 619
Cdd:PRK13295 329 VERARAALGA-----KIVSAWGMTENG-AVTLTKL----DDPDERASTTDGCP----LPGVEVRVVDADG--APLPAGQI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 620 GEIYVRAGGLAEGYRGLPELNkekfvnnwfvekdhwnyldKDNGEPWrqfwlgprdrlYRTGDLGRYLPNGDCECCGRAD 699
Cdd:PRK13295 393 GRLQVRGCSNFGGYLKRPQLN-------------------GTDADGW-----------FDTGDLARIDADGYIRISGRSK 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 700 DqVKIRGFR-IELGEIDTHISQHPlvreNITLVRKNADNEPTL----ITFMVPRFDKPDDLskfqsdvpkevetdpivkg 774
Cdd:PRK13295 443 D-VIIRGGEnIPVVEIEALLYRHP----AIAQVAIVAYPDERLgeraCAFVVPRPGQSLDF------------------- 498
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 6319591 775 ligyhllsKDIRTFLK-KRLASYAMPSLIVVMDKLPLNPNGKVDKPKL 821
Cdd:PRK13295 499 --------EEMVEFLKaQKVAKQYIPERLVVRDALPRTPSGKIQKFRL 538
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
247-822 |
3.33e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 99.21 E-value: 3.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 247 AEAFPERTCVVetptlnsDKSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFSVIDP 326
Cdd:PRK07656 15 ARRFGDKEAYV-------FGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 327 AYPPARQTIYLGVAKPRGLIViraagqLDQLV-EDY-INDELEIVSRINSIAIqENGTIEGGKLDNGEDVLAPYDhykDT 404
Cdd:PRK07656 88 RYTADEAAYILARGDAKALFV------LGLFLgVDYsATTRLPALEHVVICET-EEDDPHTEKMKTFTDFLAAGD---PA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 405 RTGVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFNWMSKRFNLTENDKFtmlsgIAHDPiqrdMF----------T 474
Cdd:PRK07656 158 ERAPEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRY-----LAANP----FFhvfgykagvnA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 475 PLFLGAQLY-VPTQDdigtPGRLAEWMSKYGCTVTHLTPAMGQLL------------------TAQATTPfPKLHHAFfv 535
Cdd:PRK07656 229 PLMRGATILpLPVFD----PDEVFRLIETERITVLPGPPTMYNSLlqhpdrsaedlsslrlavTGAASMP-VALLERF-- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 536 gdiltkRDCLRLQTLAENcrivnmYGTTETQRAVSYfevkSKNDDPnflkklKDVMP--AGKGMLNVQLLVVNRNDrtQI 613
Cdd:PRK07656 302 ------ESELGVDIVLTG------YGLSEASGVTTF----NRLDDD------RKTVAgtIGTAIAGVENKIVNELG--EE 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 614 CGIGEIGEIYVRAGGLAEGYRGLPELNKEKfvnnwfvekdhwnyLDKDNgepwrqfWLgprdrlyRTGDLGRYLPNGDCE 693
Cdd:PRK07656 358 VPVGEVGELLVRGPNVMKGYYDDPEATAAA--------------IDADG-------WL-------HTGDLGRLDEEGYLY 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 694 CCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLvrknadneptlitfmvprfdkpddlskfqsDVPKEvETDPIVK 773
Cdd:PRK07656 410 IVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVI------------------------------GVPDE-RLGEVGK 458
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 6319591 774 GLI----GYHLLSKDIRTFLKKRLASYAMPSLIVVMDKLPLNPNGKVDKPKLQ 822
Cdd:PRK07656 459 AYVvlkpGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALR 511
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
242-821 |
1.87e-20 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 97.14 E-value: 1.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 242 IFQDNAEAFPERTCVVetptlnsDKSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATF 321
Cdd:PRK06155 26 MLARQAERYPDRPLLV-------FGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 322 SVIDPAYPPARQTIYLGVAKPRgLIVIRAAGqLDQLveDYINDELEIVSRINSIaiqenGTIEGGKLDNGEDVlAPYDHY 401
Cdd:PRK06155 99 VPINTALRGPQLEHILRNSGAR-LLVVEAAL-LAAL--EAADPGDLPLPAVWLL-----DAPASVSVPAGWST-APLPPL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 402 KDTRTGVVVGPDSNPTLSFTSGSEGIPKGVLGRHfslAYYFNW---MSKRFNLTENDK-FTMLSgIAHDPIQRDMFTPLF 477
Cdd:PRK06155 169 DAPAPAAAVQPGDTAAILYTSGTTGPSKGVCCPH---AQFYWWgrnSAEDLEIGADDVlYTTLP-LFHTNALNAFFQALL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 478 LGAQLYVPTQddiGTPGRLAEWMSKYGCTVTHLTPAMGQLLTAQATTPFPKLHhaffvgdilTKRDCLR-------LQTL 550
Cdd:PRK06155 245 AGATYVLEPR---FSASGFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAH---------RVRVALGpgvpaalHAAF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 551 AENC--RIVNMYGTTETQravSYFEVKSKNDDPNFLKKLKDvmpagkgmlNVQLLVVNRNDRTqiCGIGEIGEIYVRA-- 626
Cdd:PRK06155 313 RERFgvDLLDGYGSTETN---FVIAVTHGSQRPGSMGRLAP---------GFEARVVDEHDQE--LPDGEPGELLLRAde 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 627 -GGLAEGYRGLPelnkEKFVnnwfvekdhwnyldkdngEPWRQFWLGPRDRLYRTGDlgrylpnGDCECCGRADDQVKIR 705
Cdd:PRK06155 379 pFAFATGYFGMP----EKTV------------------EAWRNLWFHTGDRVVRDAD-------GWFRFVDRIKDAIRRR 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 706 GFRIELGEIDTHISQHPLVREnitlvrknadneptLITFMVPrfdkpddlSKFQSDvpkEVETDPIVKGliGYHLLSKDI 785
Cdd:PRK06155 430 GENISSFEVEQVLLSHPAVAA--------------AAVFPVP--------SELGED---EVMAAVVLRD--GTALEPVAL 482
|
570 580 590
....*....|....*....|....*....|....*.
gi 6319591 786 RTFLKKRLASYAMPSLIVVMDKLPLNPNGKVDKPKL 821
Cdd:PRK06155 483 VRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
252-821 |
2.29e-20 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 95.82 E-value: 2.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 252 ERTCVVetptlnsDKSRSFTYRDINRTSNIVAHYLI-KTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFSVIDPAYPP 330
Cdd:cd05941 1 DRIAIV-------DDGDSITYADLVARAARLANRLLaLGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 331 ARQTIYLGVAKPRglIVIRAAgqldqlvedyindeleivsrinsiaiqengtieggkldngedvlapydhykdtrtgvvv 410
Cdd:cd05941 74 AELEYVITDSEPS--LVLDPA----------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 411 gpdsnpTLSFTSGSEGIPKGVLGRHFSLAYYFNWMSKRFNLTENDKFTMLSGIAH-DPIQRDMFTPLFLGAQLyvptqdd 489
Cdd:cd05941 93 ------LILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHvHGLVNALLCPLFAGASV------- 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 490 igtpgrlaEWMSKYGCTVTHLTPAMGQ--LLTAQATTpFPKL---HHAFFVGDILTKRDC---LRL----------QTLA 551
Cdd:cd05941 160 --------EFLPKFDPKEVAISRLMPSitVFMGVPTI-YTRLlqyYEAHFTDPQFARAAAaerLRLmvsgsaalpvPTLE 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 552 ENC-----RIVNMYGTTETQRAVSyfevksknddpNFLKKLKDVMPAGKGMLNVQLLVVNRNdRTQICGIGEIGEIYVRA 626
Cdd:cd05941 231 EWEaitghTLLERYGMTEIGMALS-----------NPLDGERRPGTVGMPLPGVQARIVDEE-TGEPLPRGEVGEIQVRG 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 627 GGLAEGYRGLPELNKEkfvnnWFVEkdhwnyldkdngepwrqfwlgprDRLYRTGDLGRYLPNGDCECCGR-ADDQVKIR 705
Cdd:cd05941 299 PSVFKEYWNKPEATKE-----EFTD-----------------------DGWFKTGDLGVVDEDGYYWILGRsSVDIIKSG 350
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 706 GFRIELGEIDTHISQHPLVREnitlvrknadneptlitfmVPRFDKPDDlskfqsDVPKEVETdpIVKGLIGYHLLS-KD 784
Cdd:cd05941 351 GYKVSALEIERVLLAHPGVSE-------------------CAVIGVPDP------DWGERVVA--VVVLRAGAAALSlEE 403
|
570 580 590
....*....|....*....|....*....|....*..
gi 6319591 785 IRTFLKKRLASYAMPSLIVVMDKLPLNPNGKVDKPKL 821
Cdd:cd05941 404 LKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKEL 440
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
245-706 |
2.98e-20 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 96.54 E-value: 2.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 245 DNAEAFPERTCVVetpTLNSDKSR--SFTYRDINRTSNIVAHYLIKTGiKRGDVVMIYSSRGVDLMVCVMGVLKAGATfS 322
Cdd:cd05931 1 RRAAARPDRPAYT---FLDDEGGReeTLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAI-A 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 323 VidPAYPPAR-------QTIyLGVAKPRglIVIRAAGQLDQLVEDYINDELEIVSRINSIAIQENGTIeggkldngedvl 395
Cdd:cd05931 76 V--PLPPPTPgrhaerlAAI-LADAGPR--VVLTTAAALAAVRAFAASRPAAGTPRLLVVDLLPDTSA------------ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 396 apydhykDTRTGVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFNWMSKRFNLTENDkfTMLSGIahdPIQRDM--- 472
Cdd:cd05931 139 -------ADWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGD--VVVSWL---PLYHDMgli 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 473 ---FTPLFLGAQLY-VPTQDDIGTPGRLAEWMSKYGCTVThLTPAMGQLLTAQATTP-------FPKLHHAFFVG----- 536
Cdd:cd05931 207 gglLTPLYSGGPSVlMSPAAFLRRPLRWLRLISRYRATIS-AAPNFAYDLCVRRVRDedlegldLSSWRVALNGAepvrp 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 537 DILTK-----RDC-LRLQT------LAENCRIVNMyGTTETQRAVSYFEVKSKNDDPNFLKKLKD----VMPAGKGMLNV 600
Cdd:cd05931 286 ATLRRfaeafAPFgFRPEAfrpsygLAEATLFVSG-GPPGTGPVVLRVDRDALAGRAVAVAADDPaareLVSCGRPLPDQ 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 601 QLLVVNRNDRtQICGIGEIGEIYVRAGGLAEGYRGLPELNKEKFvnnwfvekdhwNYLDKDNGEPWrqfwlgprdrlYRT 680
Cdd:cd05931 365 EVRIVDPETG-RELPDGEVGEIWVRGPSVASGYWGRPEATAETF-----------GALAATDEGGW-----------LRT 421
|
490 500
....*....|....*....|....*.
gi 6319591 681 GDLGrYLPNGDCECCGRADDQVKIRG 706
Cdd:cd05931 422 GDLG-FLHDGELYITGRLKDLIIVRG 446
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
244-931 |
4.44e-20 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 97.93 E-value: 4.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 244 QDNAEAFPERTCV---VETPtlnsDKSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSrGVDLMVCVMGVLKAGat 320
Cdd:PRK05691 16 QRRAAQTPDRLALrflADDP----GEGVVLSYRDLDLRARTIAAALQARASFGDRAVLLFPS-GPDYVAAFFGCLYAG-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 321 fsVID-PAYPP--------ARQTIYLGVAKPRGLIVIRA-AGQLDQLVEDYINDELEIVSrinsiaiqengtieggkLDN 390
Cdd:PRK05691 89 --VIAvPAYPPesarrhhqERLLSIIADAEPRLLLTVADlRDSLLQMEELAAANAPELLC-----------------VDT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 391 GEDVLApydhykDTRTGVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYfNWMSKR-FNLTENDKFTMLSGIahdPIQ 469
Cdd:PRK05691 150 LDPALA------EAWQEPALQPDDIAFLQYTSGSTALPKGVQVSHGNLVAN-EQLIRHgFGIDLNPDDVIVSWL---PLY 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 470 RDM------FTPLFLGaqlyVP-----TQDDIGTPGRLAEWMSKYGCTVTHLTPAMGQLLTAQ-ATTPFPKLH----HAF 533
Cdd:PRK05691 220 HDMgligglLQPIFSG----VPcvlmsPAYFLERPLRWLEAISEYGGTISGGPDFAYRLCSERvSESALERLDlsrwRVA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 534 FVGDILTKRDCLRlqTLAEN---CRI-----VNMYGTTETQ---------RAVSYFEVksknDDPNFLKKLKD------V 590
Cdd:PRK05691 296 YSGSEPIRQDSLE--RFAEKfaaCGFdpdsfFASYGLAEATlfvsggrrgQGIPALEL----DAEALARNRAEpgtgsvL 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 591 MPAGKGMLNVQLLVVNRNdRTQICGIGEIGEIYVRAGGLAEGYRGLPELNKEKFVNNwfvekdhwnyldkdNGepwrQFW 670
Cdd:PRK05691 370 MSCGRSQPGHAVLIVDPQ-SLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFVEH--------------DG----RTW 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 671 LgprdrlyRTGDLGrYLPNGDCECCGRADDQVKIRGFRIELGEIDThisqhpLVRENITLVRK--------NADNEPTL- 741
Cdd:PRK05691 431 L-------RTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQDIEK------TVEREVEVVRKgrvaafavNHQGEEGIg 496
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 742 ITFMVPRfdkpddlsKFQSDVPKEVetdpivkgligyhlLSKDIRTFLKKrlASYAMPSLIVVMD--KLPLNPNGKVDK- 818
Cdd:PRK05691 497 IAAEISR--------SVQKILPPQA--------------LIKSIRQAVAE--ACQEAPSVVLLLNpgALPKTSSGKLQRs 552
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 819 ------------PKLQFPTPKQlnlvAENTVSETDDSQFTNVereVRDLWLSILptKPASVSPDDSFFDLGGHSILATKM 886
Cdd:PRK05691 553 acrlrladgsldSYALFPALQA----VEAAQTAASGDELQAR---IAAIWCEQL--KVEQVAADDHFFLLGGNSIAATQV 623
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 6319591 887 IFTLKKKLQVDLPLGTIFKYPTIKAFAAEIDRIKSSGGSSQGEVV 931
Cdd:PRK05691 624 VARLRDELGIDLNLRQLFEAPTLAAFSAAVARQLAGGGAAQAAIA 668
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
268-821 |
1.02e-19 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 94.62 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 268 RSFTYRDINRTSNIVAHYLIKTGIKRGDVV--MIYSS-RGVDLMVCVMGvlkAGATFSVIDPAYPPaRQTIYlgvakprg 344
Cdd:cd12119 24 HRYTYAEVAERARRLANALRRLGVKPGDRVatLAWNThRHLELYYAVPG---MGAVLHTINPRLFP-EQIAY-------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 345 liVIRAAGqlDQLVedYINDELE-----IVSRINSI-AIQENGTIEGGKLDNGEDVLApYDHYKDTRTGVVVGPD----S 414
Cdd:cd12119 92 --IINHAE--DRVV--FVDRDFLplleaIAPRLPTVeHVVVMTDDAAMPEPAGVGVLA-YEELLAAESPEYDWPDfdenT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 415 NPTLSFTSGSEGIPKGVLGRHFSLayYFNWMSKR----FNLTENDkfTMLsgiahdPIqrdmfTPLF------------- 477
Cdd:cd12119 165 AAAICYTSGTTGNPKGVVYSHRSL--VLHAMAALltdgLGLSESD--VVL------PV-----VPMFhvnawglpyaaam 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 478 LGAQLYVPTQDDigTPGRLAEWMSKYGCTVTHLTPAMGQ-LLTAQATTP--FPKLHHAFFVGDILTKRDCLRLqtLAENC 554
Cdd:cd12119 230 VGAKLVLPGPYL--DPASLAELIEREGVTFAAGVPTVWQgLLDHLEANGrdLSSLRRVVIGGSAVPRSLIEAF--EERGV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 555 RIVNMYGTTETQRAVSYFEVKSKNDDPNFLKKLKDVMPAGKGMLNVQLLVVNRNDRTQICGIGEIGEIYVRAGGLAEGYR 634
Cdd:cd12119 306 RVIHAWGMTETSPLGTVARPPSEHSNLSEDEQLALRAKQGRPVPGVELRIVDDDGRELPWDGKAVGELQVRGPWVTKSYY 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 635 GLPELNKEKFVNNWFvekdhwnyldkdngepwrqfwlgprdrlyRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEI 714
Cdd:cd12119 386 KNDEESEALTEDGWL-----------------------------RTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVEL 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 715 DTHISQHPLVRENITLVRKNA--DNEPTLITfmvprfdkpddlskfqsdVPKEVETdpivkgligyhLLSKDIRTFLKKR 792
Cdd:cd12119 437 ENAIMAHPAVAEAAVIGVPHPkwGERPLAVV------------------VLKEGAT-----------VTAEELLEFLADK 487
|
570 580
....*....|....*....|....*....
gi 6319591 793 LASYAMPSLIVVMDKLPLNPNGKVDKPKL 821
Cdd:cd12119 488 VAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
265-822 |
1.60e-19 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 93.75 E-value: 1.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 265 DKSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFSVIDPAYPpARQTIYLgVAKPRG 344
Cdd:TIGR02262 26 DDISSLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLT-ADDYAYM-LEDSRA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 345 LIVIrAAGQLDQLVEDYINDELEIVSRINSiaiqenGTIEGGKLDNGEDVLAPYDHYKDTRTGvvvgPDSNPTLSFTSGS 424
Cdd:TIGR02262 104 RVVF-VSGALLPVIKAALGKSPHLEHRVVV------GRPEAGEVQLAELLATESEQFKPAATQ----ADDPAFWLYSSGS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 425 EGIPKGVLGRHFSLAYYF-NWMSKRFNLTEND------KFTMLSGIAHDpiqrdMFTPLFLGAQLYVPTQDDigTPGRLA 497
Cdd:TIGR02262 173 TGMPKGVVHTHSNPYWTAeLYARNTLGIREDDvcfsaaKLFFAYGLGNA-----LTFPMSVGATTVLMGERP--TPDAVF 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 498 EWMSKYGCTVTHLTPAMGQLLTAQATTPFP---KLHHAFFVGDILTKRDCLRLQTLAeNCRIVNMYGTTETQRAvsyfev 574
Cdd:TIGR02262 246 DRLRRHQPTIFYGVPTLYAAMLADPNLPSEdqvRLRLCTSAGEALPAEVGQRWQARF-GVDIVDGIGSTEMLHI------ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 575 ksknddpnFLKKLKDVM---PAGKGMLNVQLLVVNrnDRTQICGIGEIGEIYVRAGGLAEGYRGLPELNKEKFVNNWfve 651
Cdd:TIGR02262 319 --------FLSNLPGDVrygTSGKPVPGYRLRLVG--DGGQDVADGEPGELLISGPSSATMYWNNRAKSRDTFQGEW--- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 652 kdhwnyldkdngepwrqfwlgprdrlYRTGDlgRYLPNGDCEC--CGRADDQVKIRGFRIELGEIDTHISQHPLVREnit 729
Cdd:TIGR02262 386 --------------------------TRSGD--KYVRNDDGSYtyAGRTDDMLKVSGIYVSPFEIESALIQHPAVLE--- 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 730 lvrknadneptliTFMVPRFDkPDDLSKFQS-DVPKEvetdpivkgliGYHLLSKDIRTFLKKRLASYAMPSLIVVMDKL 808
Cdd:TIGR02262 435 -------------AAVVGVAD-EDGLIKPKAfVVLRP-----------GQTALETELKEHVKDRLAPYKYPRWIVFVDDL 489
|
570
....*....|....
gi 6319591 809 PLNPNGKVDKPKLQ 822
Cdd:TIGR02262 490 PKTATGKIQRFKLR 503
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
270-816 |
1.82e-18 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 89.87 E-value: 1.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 270 FTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGAtfsVIDPAYpparqtiylgvakprglivir 349
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGA---VICPLF--------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 350 aagqlDQLVEDYINDELEivsriNSiaiqengtieggkldnGEDVLAPYDHYKDTRTgvvvgPDSNPTLSFTSGSEGIPK 429
Cdd:cd05969 57 -----SAFGPEAIRDRLE-----NS----------------EAKVLITTEELYERTD-----PEDPTLLHYTSGTTGTPK 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 430 GVLgrHFSLAYYFNWMSKR--FNLTENDKF------TMLSGIAHDpiqrdMFTPLFLGAQLYVptQDDIGTPGRLAEWMS 501
Cdd:cd05969 106 GVL--HVHDAMIFYYFTGKyvLDLHPDDIYwctadpGWVTGTVYG-----IWAPWLNGVTNVV--YEGRFDAESWYGIIE 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 502 KYGCTVTHLTPAMGQLLTAQATTPFPK-----LHHAFFVGDILTKrDCLRLQTLAENCRIVNMYGTTET--QRAVSYFEV 574
Cdd:cd05969 177 RVKVTVWYTAPTAIRMLMKEGDELARKydlssLRFIHSVGEPLNP-EAIRWGMEVFGVPIHDTWWQTETgsIMIANYPCM 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 575 KSKnddPNFLkklkdvmpaGKGMLNVQLLVVNRN-DRTQIcgiGEIGEIYVRAG--GLAEGYRGLPELNKEKFVNNWFVE 651
Cdd:cd05969 256 PIK---PGSM---------GKPLPGVKAAVVDENgNELPP---GTKGILALKPGwpSMFRGIWNDEERYKNSFIDGWYLT 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 652 KDhWNYLDKDNgepwrQFWLgprdrlyrtgdlgrylpngdcecCGRADDQVKIRGFRIELGEIDTHISQHPLVREnitlv 731
Cdd:cd05969 321 GD-LAYRDEDG-----YFWF-----------------------VGRADDIIKTSGHRVGPFEVESALMEHPAVAE----- 366
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 732 rknadneptlitfmVPRFDKPDDLSKFqsdvpkevetdpIVKGLI----GYH---LLSKDIRTFLKKRLASYAMPSLIVV 804
Cdd:cd05969 367 --------------AGVIGKPDPLRGE------------IIKAFIslkeGFEpsdELKEEIINFVRQKLGAHVAPREIEF 420
|
570
....*....|..
gi 6319591 805 MDKLPLNPNGKV 816
Cdd:cd05969 421 VDNLPKTRSGKI 432
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
241-821 |
8.08e-18 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 88.15 E-value: 8.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 241 DIFQDNAEAFPERTCVVetptlnsDKSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGAT 320
Cdd:cd05920 19 DLLARSAARHPDRIAVV-------DGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 321 FSVIDPAYPPARQTIYLGVAKPRGLIVIRAAGQLdqlveDYINDELEIVSRINSIAIqengtieggkldngedvlapydh 400
Cdd:cd05920 92 PVLALPSHRRSELSAFCAHAEAVAYIVPDRHAGF-----DHRALARELAESIPEVAL----------------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 401 ykdtrtgvvvgpdsnptLSFTSGSEGIPKGVLGRHFSLAYYFNWMSKRFNLTENDKFTMLSGIAHdpiQRDMFTPLFLGA 480
Cdd:cd05920 144 -----------------FLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAH---NFPLACPGVLGT 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 481 QLY----VPTQDdiGTPGRLAEWMSKYGCTVTHLTPAMGQL-LTAQATTPF-PKLHHAFFVGDILTKRDCLRLQTLAENC 554
Cdd:cd05920 204 LLAggrvVLAPD--PSPDAAFPLIEREGVTVTALVPALVSLwLDAAASRRAdLSSLRLLQVGGARLSPALARRVPPVLGC 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 555 RIVNMYGTTETqrAVSYfevkSKNDDPNFLKKLKDVMPAGKGMlnvQLLVVNRNDRTqiCGIGEIGEIYVRAGGLAEGYR 634
Cdd:cd05920 282 TLQQVFGMAEG--LLNY----TRLDDPDEVIIHTQGRPMSPDD---EIRVVDEEGNP--VPPGEEGELLTRGPYTIRGYY 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 635 GLPELNKEKFVNNWFvekdhwnyldkdngepwrqfwlgprdrlYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEI 714
Cdd:cd05920 351 RAPEHNARAFTPDGF----------------------------YRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEV 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 715 DTHISQHPLVREnITLVrknADNEPTL----ITFMVPRfdkpddlskfqsdvpkevetDPIVKGLigyhllskDIRTFLK 790
Cdd:cd05920 403 ENLLLRHPAVHD-AAVV---AMPDELLgersCAFVVLR--------------------DPPPSAA--------QLRRFLR 450
|
570 580 590
....*....|....*....|....*....|..
gi 6319591 791 KR-LASYAMPSLIVVMDKLPLNPNGKVDKPKL 821
Cdd:cd05920 451 ERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
270-757 |
5.37e-17 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 86.18 E-value: 5.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 270 FTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGAtFSVIDPAyPPARQTIYLGVAKPRGL---- 345
Cdd:cd05906 40 QSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGF-VPAPLTV-PPTYDEPNARLRKLRHIwqll 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 346 ----IVIRAAgqldqLVEDYinDELEIVSRINSIAIQEngtieggkLDNGEDVLAPYDhykdtrtGVVVGPDSNPTLSFT 421
Cdd:cd05906 118 gspvVLTDAE-----LVAEF--AGLETLSGLPGIRVLS--------IEELLDTAADHD-------LPQSRPDDLALLMLT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 422 SGSEGIPKGVLGRHFSLAYYFNWMSKRFNLTENDKFtmLS--------GIAHDPIQrdmftPLFLGA-QLYVPTQDDIGT 492
Cdd:cd05906 176 SGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVF--LNwvpldhvgGLVELHLR-----AVYLGCqQVHVPTEEILAD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 493 PGRLAEWMSKYGCTVTHLTPAMGQLLTAQATTPFPK------LHHAFFVGDILTKRDCLRLQTLAENCR-----IVNMYG 561
Cdd:cd05906 249 PLRWLDLIDRYRVTITWAPNFAFALLNDLLEEIEDGtwdlssLRYLVNAGEAVVAKTIRRLLRLLEPYGlppdaIRPAFG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 562 TTETQRAVSYFEVKSKNDDPNFLKklkdVMPAGKGMLNVQLLVVNRNDrtQICGIGEIGEIYVRAGGLAEGYRGLPELNK 641
Cdd:cd05906 329 MTETCSGVIYSRSFPTYDHSQALE----FVSLGRPIPGVSMRIVDDEG--QLLPEGEVGRLQVRGPVVTKGYYNNPEANA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 642 EKFVN-NWFvekdhwnyldkdngepwrqfwlgprdrlyRTGDLGrYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQ 720
Cdd:cd05906 403 EAFTEdGWF-----------------------------RTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEE 452
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 6319591 721 HPLVRENITL---VRKNADNEPTLITFMVPRFDKPDDLSK 757
Cdd:cd05906 453 VPGVEPSFTAafaVRDPGAETEELAIFFVPEYDLQDALSE 492
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
237-822 |
5.81e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 85.98 E-value: 5.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 237 GCIHDIFQDNAEAFPERTCVVETPtlnsdKSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLK 316
Cdd:PRK12583 18 QTIGDAFDATVARFPDREALVVRH-----QALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATAR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 317 AGATFSVIDPAYPPARQTIYLGVAKPRGLIVIRA------AGQLDQLV--------EDYINDELEIVSRINSIAIQENGt 382
Cdd:PRK12583 93 IGAILVNINPAYRASELEYALGQSGVRWVICADAfktsdyHAMLQELLpglaegqpGALACERLPELRGVVSLAPAPPP- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 383 ieggKLDNGEDVLAPYDHYKDTRTGVVVG---PDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFNWMSKRFNLTENDK--- 456
Cdd:PRK12583 172 ----GFLAWHELQARGETVSREALAERQAsldRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRlcv 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 457 -------FTM----LSGIAHdpiqrdmftplflGAQLYVPTqdDIGTPGRLAEWMSKYGCTVTHLTPAMgqlLTAQATTP 525
Cdd:PRK12583 248 pvplyhcFGMvlanLGCMTV-------------GACLVYPN--EAFDPLATLQAVEEERCTALYGVPTM---FIAELDHP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 526 -FPKLHHAFFVGDILTKRDCLR---LQTLAE-NCRIVNM-YGTTETqravSYFEVKSKNDDPnFLKKLKDVmpaGKGMLN 599
Cdd:PRK12583 310 qRGNFDLSSLRTGIMAGAPCPIevmRRVMDEmHMAEVQIaYGMTET----SPVSLQTTAADD-LERRVETV---GRTQPH 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 600 VQLLVVNRNDRTqiCGIGEIGEIYVRAGGLAEGYRGLPELNKEKfvnnwfVEKDHWNYldkdngepwrqfwlgprdrlyr 679
Cdd:PRK12583 382 LEVKVVDPDGAT--VPRGEIGELCTRGYSVMKGYWNNPEATAES------IDEDGWMH---------------------- 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 680 TGDLGRYLPNGDCECCGRADDQVkIRGFR-IELGEIDTHISQHPLVREnitlvrknadneptlitfmVPRFDKPDdlSKF 758
Cdd:PRK12583 432 TGDLATMDEQGYVRIVGRSKDMI-IRGGEnIYPREIEEFLFTHPAVAD-------------------VQVFGVPD--EKY 489
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6319591 759 QSDVPKEVETDPivkgliGYHLLSKDIRTFLKKRLASYAMPSLIVVMDKLPLNPNGKVDKPKLQ 822
Cdd:PRK12583 490 GEEIVAWVRLHP------GHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMR 547
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
270-816 |
6.23e-17 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 85.18 E-value: 6.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 270 FTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGAtfsvidpaypparqtiylgVAKPrglivir 349
Cdd:cd05971 7 VTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGA-------------------IAVP------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 350 aagqLDQLVedyindeleivsrinsiaiqengtieggkldnGEDVLApyDHYKDTRTGVVV--GPDSNPTLSFTSGSEGI 427
Cdd:cd05971 61 ----LFALF--------------------------------GPEALE--YRLSNSGASALVtdGSDDPALIIYTSGTTGP 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 428 PKGVLGRHFSLAYYFNWMSKRFNLTENDKFTMLS--------GIAhdpiqrDMFTP-LFLGAQL--YVPTQDDigtPGRL 496
Cdd:cd05971 103 PKGALHAHRVLLGHLPGVQFPFNLFPRDGDLYWTpadwawigGLL------DVLLPsLYFGVPVlaHRMTKFD---PKAA 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 497 AEWMSKYGCTVTHLTPAMGQLLTAQ--ATTPFPKLHHAFFVGDILTKRDCLRLQTLAENCRIVNMYGTTETQRAVSyfev 574
Cdd:cd05971 174 LDLMSRYGVTTAFLPPTALKMMRQQgeQLKHAQVKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECNLVIG---- 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 575 ksknddpnflkKLKDVMPAGKGML-------NVQLLvvnrNDRTQICGIGEIGEIYVRAGGLAE--GYRGLPELNKEKFV 645
Cdd:cd05971 250 -----------NCSALFPIKPGSMgkpipghRVAIV----DDNGTPLPPGEVGEIAVELPDPVAflGYWNNPSATEKKMA 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 646 NNWFvekdhwnyldkdngepwrqfwlgprdrlyRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVR 725
Cdd:cd05971 315 GDWL-----------------------------LTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVL 365
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 726 enitlvrknadneptlitfMVPRFDKPDdlskfqsdvpkEVETDpIVK-------GLIGYHLLSKDIRTFLKKRLASYAM 798
Cdd:cd05971 366 -------------------MAAVVGIPD-----------PIRGE-IVKafvvlnpGETPSDALAREIQELVKTRLAAHEY 414
|
570
....*....|....*...
gi 6319591 799 PSLIVVMDKLPLNPNGKV 816
Cdd:cd05971 415 PREIEFVNELPRTATGKI 432
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
239-823 |
9.97e-17 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 85.32 E-value: 9.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 239 IHDIFQDNAEAFPERTCVVETptlnsDKSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAG 318
Cdd:PRK05852 18 IADLVEVAATRLPEAPALVVT-----ADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRAD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 319 ATFSVIDPAYPPARQTIYLGVAKPRgLIVIRAAGQLDQLVEdyindeleiVSRINSIAIQENG--TIEGGKLDNGEDVLA 396
Cdd:PRK05852 93 LVVVPLDPALPIAEQRVRSQAAGAR-VVLIDADGPHDRAEP---------TTRWWPLTVNVGGdsGPSGGTLSVHLDAAT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 397 PYDHYKDTRTGvvVGPDsNPTLSFTSGSEGIPKGVLGRHFSLAYYFNWMSKRFNLTENDKFTMLSGIAH-DPIQRDMFTP 475
Cdd:PRK05852 163 EPTPATSTPEG--LRPD-DAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHgHGLIAALLAT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 476 LFLGAQLYVPTQ---------DDIGTPGrlAEWMSKygctvthlTPAMGQLLTAQATT-PFPKLHHAF-FVgdiltkRDC 544
Cdd:PRK05852 240 LASGGAVLLPARgrfsahtfwDDIKAVG--ATWYTA--------VPTIHQILLERAATePSGRKPAALrFI------RSC 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 545 ---LRLQTlAENCR------IVNMYGTTETQRAVSYFEVKSKNDDPNflkKLKDVMPAGKGMlNVQLLVVnRNDrTQICG 615
Cdd:PRK05852 304 sapLTAET-AQALQtefaapVVCAFGMTEATHQVTTTQIEGIGQTEN---PVVSTGLVGRST-GAQIRIV-GSD-GLPLP 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 616 IGEIGEIYVRAGGLAEGYRGLPELNKEKFVNNWFvekdhwnyldkdngepwrqfwlgprdrlyRTGDLGRYLPNGDCECC 695
Cdd:PRK05852 377 AGAVGEVWLRGTTVVRGYLGDPTITAANFTDGWL-----------------------------RTGDLGSLSAAGDLSIR 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 696 GRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRKNADNEPTLITFMVPRfdkpddlskfqsdvpkevetDPIvkgl 775
Cdd:PRK05852 428 GRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPR--------------------ESA---- 483
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 6319591 776 igyHLLSKDIRTFLKKRLASYAMPSLIVVMDKLPLNPNGKVDKP--KLQF 823
Cdd:PRK05852 484 ---PPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRavAEQF 530
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
386-818 |
1.08e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 85.04 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 386 GKLDNGEDVLAPYDHYKDTRTGVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFNWMSKRFNLTENDKFTMLSGIAH 465
Cdd:PRK06188 141 GPVPDGVDLLAAAAKFGPAPLVAAALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSH 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 466 dpIQRDMFTP-LFLGAQLYVPTQDDigtPGRLAEWMSKYGCTVTHLTPAMGQLLtaqattpfpkLHHAffvgdILTKRDC 544
Cdd:PRK06188 221 --AGGAFFLPtLLRGGTVIVLAKFD---PAEVLRAIEEQRITATFLVPTMIYAL----------LDHP-----DLRTRDL 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 545 LRLQT------------LAENCRI-----VNMYGTTETQRAVSYFEVKS-KNDDPNFLKKLKDVMPAgkgmLNVQLLvvn 606
Cdd:PRK06188 281 SSLETvyygaspmspvrLAEAIERfgpifAQYYGQTEAPMVITYLRKRDhDPDDPKRLTSCGRPTPG----LRVALL--- 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 607 rNDRTQICGIGEIGEIYVRAGGLAEGYRGLPELNKEKFVNNWFvekdhwnyldkdngepwrqfwlgprdrlyRTGDLGRY 686
Cdd:PRK06188 354 -DEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAFRDGWL-----------------------------HTGDVARE 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 687 LPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRenitlvrknadneptlitfMVPRFDKPDDlsKFQSDVPKEV 766
Cdd:PRK06188 404 DEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVA-------------------QVAVIGVPDE--KWGEAVTAVV 462
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 6319591 767 ETDPivkgliGYHLLSKDIRTFLKKRLASYAMPSLIVVMDKLPLNPNGKVDK 818
Cdd:PRK06188 463 VLRP------GAAVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDK 508
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
239-821 |
1.15e-16 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 85.20 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 239 IHDIFQDNAEAFPERTCVVetptlnsDKSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAG 318
Cdd:COG1021 27 LGDLLRRRAERHPDRIAVV-------DGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 319 ATfsvidP--AYPPARQT-I--YLGVAKPRGLIVIRAAGQLDqlvedyiNDEL--EIVSRINSIaiqENGTIEGgklDNG 391
Cdd:COG1021 100 AI-----PvfALPAHRRAeIshFAEQSEAVAYIIPDRHRGFD-------YRALarELQAEVPSL---RHVLVVG---DAG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 392 EDVlaPYDH-YKDTRTGVVVGPDSNP----TLSftSGSEGIPKGVLGRHFslAYYFNW--MSKRFNLTENDKFTMLSGIA 464
Cdd:COG1021 162 EFT--SLDAlLAAPADLSEPRPDPDDvaffQLS--GGTTGLPKLIPRTHD--DYLYSVraSAEICGLDADTVYLAALPAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 465 HDpiqrdmFT---PLFLGAqLYV-------PTqddiGTPGRLAEWMSKYGCTVTHLTPAMGQL-LTAQATTPFpklhhaf 533
Cdd:COG1021 236 HN------FPlssPGVLGV-LYAggtvvlaPD----PSPDTAFPLIERERVTVTALVPPLALLwLDAAERSRY------- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 534 fvgDILTkrdcLRL---------QTLAE------NCRIVNMYGTTE-----------------TQ-RAVSyfevkskNDD 580
Cdd:COG1021 298 ---DLSS----LRVlqvggaklsPELARrvrpalGCTLQQVFGMAEglvnytrlddpeeviltTQgRPIS-------PDD 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 581 pnflkklkdvmpagkgmlnvQLLVVNRNDRTqiCGIGEIGEIYVRAGGLAEGYRGLPELNKEKFVNNWFvekdhwnyldk 660
Cdd:COG1021 364 --------------------EVRIVDEDGNP--VPPGEVGELLTRGPYTIRGYYRAPEHNARAFTPDGF----------- 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 661 dngepwrqfwlgprdrlYRTGDLGRYLPNGDCECCGRADDQVkIRGfrielGE------IDTHISQHPLVReNITLV--- 731
Cdd:COG1021 411 -----------------YRTGDLVRRTPDGYLVVEGRAKDQI-NRG-----GEkiaaeeVENLLLAHPAVH-DAAVVamp 466
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 732 ------RKNAdneptlitFMVPRFDKPDdlskfqsdvpkevetdpivkgligyhllSKDIRTFLKKR-LASYAMPSLIVV 804
Cdd:COG1021 467 deylgeRSCA--------FVVPRGEPLT----------------------------LAELRRFLRERgLAAFKLPDRLEF 510
|
650
....*....|....*..
gi 6319591 805 MDKLPLNPNGKVDKPKL 821
Cdd:COG1021 511 VDALPLTAVGKIDKKAL 527
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
269-816 |
7.58e-16 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 81.76 E-value: 7.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 269 SFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFSVIDPAYPPaRQTIYlgVAKPRGLIVI 348
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKE-RELEY--ILNDSGAKVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 349 RAAGQLDQLVedyindeleivsrinsiaiqengtieggkldngedvLAPYdhykdtrtgvvvgpdsnptlsfTSGSEGIP 428
Cdd:cd05935 78 VVGSELDDLA------------------------------------LIPY----------------------TSGTTGLP 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 429 KGVLGRHFSLAYYFNWMSKRFNLTENDKFTMLSGIAHDP-IQRDMFTPLFLGAQLYVPTQDDIGTpgrLAEWMSKYGCTV 507
Cdd:cd05935 100 KGCMHTHFSAAANALQSAVWTGLTPSDVILACLPLFHVTgFVGSLNTAVYVGGTYVLMARWDRET---ALELIEKYKVTF 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 508 THLTPAMGQLLTAQ---ATTPFPKLHHAFFVGDILTKRDCLRLQTLAeNCRIVNMYGTTETQRAVsyfevkskNDDPNFL 584
Cdd:cd05935 177 WTNIPTMLVDLLATpefKTRDLSSLKVLTGGGAPMPPAVAEKLLKLT-GLRFVEGYGLTETMSQT--------HTNPPLR 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 585 KKLKDVmpaGKGMLNVQLLVVNRNDRTQIcGIGEIGEIYVRAGGLAEGYRGLPELNKEKFVnnwfvekdhwnyldKDNGE 664
Cdd:cd05935 248 PKLQCL---GIP*FGVDARVIDIETGREL-PPNEVGEIVVRGPQIFKGYWNRPEETEESFI--------------EIKGR 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 665 pwrqfwlgprdRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVREnitlvrknadneptlitf 744
Cdd:cd05935 310 -----------RFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*E------------------ 360
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6319591 745 mVPRFDKPDDLSkfqSDVPKE-VETDPIVKGLIGyhllSKDIRTFLKKRLASYAMPSLIVVMDKLPLNPNGKV 816
Cdd:cd05935 361 -VCVISVPDERV---GEEVKAfIVLRPEYRGKVT----EEDIIEWAREQMAAYKYPREVEFVDELPRSASGKI 425
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
240-816 |
8.07e-16 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 82.54 E-value: 8.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 240 HDIFQDNAEAFPERTCVVETPtlNSDKSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGA 319
Cdd:cd05970 20 YDVVDAMAKEYPDKLALVWCD--DAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 320 TfSVIDPAYPPARQTIYLGVAKPRGLIVIRAAGQLDQLVEDYInDELEIVSRINSIAIQE-NGTIEGGKL-DNGEDVLAP 397
Cdd:cd05970 98 I-AIPATHQLTAKDIVYRIESADIKMIVAIAEDNIPEEIEKAA-PECPSKPKLVWVGDPVpEGWIDFRKLiKNASPDFER 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 398 ydhykdtRTGVVVGPDSNPTL-SFTSGSEGIPKGV-------LGrHFSLAYYFNwmskrfNLTENDKFTMlsgIAHDPIQ 469
Cdd:cd05970 176 -------PTANSYPCGEDILLvYFSSGTTGMPKMVehdftypLG-HIVTAKYWQ------NVREGGLHLT---VADTGWG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 470 RDMFTPLF----LGAQLYVPTQDDIgTPGRLAEWMSKYGCTVTHLTPAMGQLLTAQATT--PFPKLHHAFFVGDILTKRD 543
Cdd:cd05970 239 KAVWGKIYgqwiAGAAVFVYDYDKF-DPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSryDLSSLRYCTTAGEALNPEV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 544 CLRLQTLAeNCRIVNMYGTTETQRAVSYF---EVKsknddPNFLkklkdvmpaGKGMLNVQLLVVNRNDRTqiCGIGEIG 620
Cdd:cd05970 318 FNTFKEKT-GIKLMEGFGQTETTLTIATFpwmEPK-----PGSM---------GKPAPGYEIDLIDREGRS--CEAGEEG 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 621 EIYVRAG-----GLAEGYRGlpelNKEKFVNNWFvekdhwnyldkdngepwrqfwlgprDRLYRTGDLGRYLPNGDCECC 695
Cdd:cd05970 381 EIVIRTSkgkpvGLFGGYYK----DAEKTAEVWH-------------------------DGYYHTGDAAWMDEDGYLWFV 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 696 GRADDQVKIRGFRIELGEIDTHISQHPLVRE-NITLVrknadneptlitfmvprfdkPDDLskfQSDVPKevETDPIVKG 774
Cdd:cd05970 432 GRTDDLIKSSGYRIGPFEVESALIQHPAVLEcAVTGV--------------------PDPI---RGQVVK--ATIVLAKG 486
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 6319591 775 LIGYHLLSKDIRTFLKKRLASYAMPSLIVVMDKLPLNPNGKV 816
Cdd:cd05970 487 YEPSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKI 528
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
239-822 |
2.04e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 80.98 E-value: 2.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 239 IHDIFQDNAEAFPERTCVVEtptlnsdKSRSFTYRDINRTSNIVAHYLIKTGiKRGDVVMIYSSRGVDLMVCVMGVLKAG 318
Cdd:PRK07638 3 ITKEYKKHASLQPNKIAIKE-------NDRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 319 ATFSVIDPAYPPARQTIYLGVAKPrGLIVIRAAgqldqlvedYINDELEIVSRInsIAIQE-NGTIEGGKLD--NGEDV- 394
Cdd:PRK07638 75 WTCVPLDIKWKQDELKERLAISNA-DMIVTERY---------KLNDLPDEEGRV--IEIDEwKRMIEKYLPTyaPIENVq 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 395 LAPYdhYkdtrtgvvvgpdsnptLSFTSGSEGIPKGVLGRHFSLAYYFNWMSKRFNLTENDKFTMLSGIAHDPIQRDMFT 474
Cdd:PRK07638 143 NAPF--Y----------------MGFTSGSTGKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTLVHSLFLYGAIS 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 475 PLFLGAQLYVPTQddiGTPGRLAEWMSKYGCTVTHLTPAMGQLLTAQATTPFPKLHhAFFVGDILTKRDCLRLQTLAENC 554
Cdd:PRK07638 205 TLYVGQTVHLMRK---FIPNQVLDKLETENISVMYTVPTMLESLYKENRVIENKMK-IISSGAKWEAEAKEKIKNIFPYA 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 555 RIVNMYGTTEtqraVSYFEVKSKNDD---PNflkklkdvmPAGKGMLNVQLLVvnRNDRTQICGIGEIGEIYVRAGGLAE 631
Cdd:PRK07638 281 KLYEFYGASE----LSFVTALVDEESerrPN---------SVGRPFHNVQVRI--CNEAGEEVQKGEIGTVYVKSPQFFM 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 632 GYRGLPELNKEKFVNNWFVEKDhWNYLDKDngepwrqfwlgprdrlyrtgdlgrylpnGDCECCGRADDQVKIRGFRIEL 711
Cdd:PRK07638 346 GYIIGGVLARELNADGWMTVRD-VGYEDEE----------------------------GFIYIVGREKNMILFGGINIFP 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 712 GEIDTHISQHPLVRENITLvrknadneptlitfmvprfDKPDDlskFQSDVPKevetdPIVKGligyHLLSKDIRTFLKK 791
Cdd:PRK07638 397 EEIESVLHEHPAVDEIVVI-------------------GVPDS---YWGEKPV-----AIIKG----SATKQQLKSFCLQ 445
|
570 580 590
....*....|....*....|....*....|.
gi 6319591 792 RLASYAMPSLIVVMDKLPLNPNGKVDKPKLQ 822
Cdd:PRK07638 446 RLSSFKIPKEWHFVDEIPYTNSGKIARMEAK 476
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
417-822 |
2.83e-15 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 78.53 E-value: 2.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 417 TLSFTSGSEGIPKGVLGRHFSLAYYFNWMSKRFNLTENDKFTMLSGIAHDPIQRDMFTPLFLGAQLYVPTQDDIgtpgrL 496
Cdd:cd17630 4 TVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLLERNQA-----L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 497 AEWMSKYGCTVTHLTPAM-GQLLTAQATTPFPKLHHAFFVGDILTKRDcLRLQTLAENCRIVNMYGTTETQRAVSyfevk 575
Cdd:cd17630 79 AEDLAPPGVTHVSLVPTQlQRLLDSGQGPAALKSLRAVLLGGAPIPPE-LLERAADRGIPLYTTYGMTETASQVA----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 576 sknddpnfLKKLKDVMPAGKGmlnvqllvvNRNDRTQICgIGEIGEIYVRAGGLAEGYR--GLPELNkekfvnnwfvekd 653
Cdd:cd17630 153 --------TKRPDGFGRGGVG---------VLLPGRELR-IVEDGEIWVGGASLAMGYLrgQLVPEF------------- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 654 hwnyldkdNGEPWrqfwlgprdrlYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRK 733
Cdd:cd17630 202 --------NEDGW-----------FTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVP 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 734 NADNEPTLITFMVPRFDKPDDlskfqsdvpkevetdpivkgligyhllskDIRTFLKKRLASYAMPSLIVVMDKLPLNPN 813
Cdd:cd17630 263 DEELGQRPVAVIVGRGPADPA-----------------------------ELRAWLKDKLARFKLPKRIYPVPELPRTGG 313
|
....*....
gi 6319591 814 GKVDKPKLQ 822
Cdd:cd17630 314 GKVDRRALR 322
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
239-821 |
3.21e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 80.36 E-value: 3.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 239 IHDIFQDNAEAFPERTCVVetptlnsDKSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAG 318
Cdd:PRK08316 13 IGDILRRSARRYPDKTALV-------FGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 319 ATFSVIDPAYPPARQTIYLGVAKPRGLIVIRA-AGQLDQLVEDYINDELEivsrinsIAIQENGTIEGGKLDNGEDVLAP 397
Cdd:PRK08316 86 AVHVPVNFMLTGEELAYILDHSGARAFLVDPAlAPTAEAALALLPVDTLI-------LSLVLGGREAPGGWLDFADWAEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 398 YDhykDTRTGVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSL-AYYfnwMSKRF--NLTENDKFtmlsgIAHDPI----QR 470
Cdd:PRK08316 159 GS---VAEPDVELADDDLAQILYTSGTESLPKGAMLTHRALiAEY---VSCIVagDMSADDIP-----LHALPLyhcaQL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 471 DMftplFLGAQLYVPTQDDI---GTPGRLAEWMSKYGCTVTHLTPamgqlltaqaTTPFPKLHHAFFvgdilTKRD--CL 545
Cdd:PRK08316 228 DV----FLGPYLYVGATNVIldaPDPELILRTIEAERITSFFAPP----------TVWISLLRHPDF-----DTRDlsSL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 546 R-------------LQTLAE---NCRIVNMYGTTETqraVSYFEVKSKNDDpnfLKKLKDvmpAGKGMLNVQLLVVNRND 609
Cdd:PRK08316 289 RkgyygasimpvevLKELRErlpGLRFYNCYGQTEI---APLATVLGPEEH---LRRPGS---AGRPVLNVETRVVDDDG 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 610 RTQIcgIGEIGEIYVRAGGLAEGYRGLPELNKEKFVNNWFvekdhwnyldkdngepwrqfwlgprdrlyRTGDLGRYLPN 689
Cdd:PRK08316 360 NDVA--PGEVGEIVHRSPQLMLGYWDDPEKTAEAFRGGWF-----------------------------HSGDLGVMDEE 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 690 GDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVREnitlvrknadneptlitfmVPRFDKPDdlskfqsdvPKEVE-- 767
Cdd:PRK08316 409 GYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAE-------------------VAVIGLPD---------PKWIEav 460
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 6319591 768 TDPIV-KGliGYHLLSKDIRTFLKKRLASYAMPSLIVVMDKLPLNPNGKVDKPKL 821
Cdd:PRK08316 461 TAVVVpKA--GATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKREL 513
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
846-918 |
3.38e-15 |
|
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440006 [Multi-domain] Cd Length: 80 Bit Score: 71.81 E-value: 3.38e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6319591 846 TNVEREVRDLWLSILPTKPASVSPDDSFF-DLGGHSILATKMIFTLKKKLQVDLPLGTIFKYPTIKAFAAEIDR 918
Cdd:COG0236 4 EELEERLAEIIAEVLGVDPEEITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEE 77
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
420-818 |
6.76e-15 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 77.45 E-value: 6.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 420 FTSGSEGIPKGVLGRHFSLAYYFNWMSKRFNLTENDKFTMLSGIAHDPIQRDMFTPLFLGAQLYVPTQDDigtPGRLAEW 499
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQRKFN---PKSWIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 500 MSKYGCTVTHLTPAMGQLLtAQATTPFPKLHHAFFVGDILTKRDCLRLQTLAENCRIVNMYGTTEtQRAVSYfevksknd 579
Cdd:cd17633 84 INQYNATVIYLVPTMLQAL-ARTLEPESKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSE-LSFITY-------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 580 dpNFLKKLKDVMPAGKGMLNVQLLVVNRNDrtqicgiGEIGEIYVRAGGLAEGYrglpelnkekfVNNWFVEKDHWnyld 659
Cdd:cd17633 154 --NFNQESRPPNSVGRPFPNVEIEIRNADG-------GEIGKIFVKSEMVFSGY-----------VRGGFSNPDGW---- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 660 kdngepwrqfwlgprdrlYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRKNAdnep 739
Cdd:cd17633 210 ------------------MSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDA---- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 740 tlitfmvpRFDKpddlskfqsdvpkevetdpIVKGLI-GYHLLSKDIRTFLKKRLASYAMPSLIVVMDKLPLNPNGKVDK 818
Cdd:cd17633 268 --------RFGE-------------------IAVALYsGDKLTYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
246-724 |
8.16e-15 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 78.82 E-value: 8.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 246 NAEAFPERTCVVETPTlnsdkSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFSVID 325
Cdd:cd05904 14 FASAHPSRPALIDAAT-----GRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTAN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 326 PAYPP---ARQtiyLGVAKPRGLIV-------IRAAGQLDQLVEDYINDELEIVSRInsiaiqengtieggKLDNGEDVL 395
Cdd:cd05904 89 PLSTPaeiAKQ---VKDSGAKLAFTtaelaekLASLALPVVLLDSAEFDSLSFSDLL--------------FEADEAEPP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 396 ApydhykdtrtgVVVGPDSNPTLSFTSGSEGIPKGVLGRHfslayyfnwmskRfNLTEN-DKFTMLSGIAHDPIQRDMFT 474
Cdd:cd05904 152 V-----------VVIKQDDVAALLYSSGTTGRSKGVMLTH------------R-NLIAMvAQFVAGEGSNSDSEDVFLCV 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 475 -PLF--------------LGAQLYVPTQDDIGTPGRLAEwmsKYGCTVTHLTPAMGQLLTAQAttpfpklhhaffvgdIL 539
Cdd:cd05904 208 lPMFhiyglssfalgllrLGATVVVMPRFDLEELLAAIE---RYKVTHLPVVPPIVLALVKSP---------------IV 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 540 TKRDCLRLQT-----------LAE-------NCRIVNMYGTTETQRAVSYFEVKSKNDDPnflkklkdvmPAGKGML--N 599
Cdd:cd05904 270 DKYDLSSLRQimsgaaplgkeLIEafrakfpNVDLGQGYGMTESTGVVAMCFAPEKDRAK----------YGSVGRLvpN 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 600 VQLLVVNRNDrTQICGIGEIGEIYVRAGGLAEGYRGLPELNKEKfvnnwfvekdhwnyLDKDNgepwrqfWLgprdrlyR 679
Cdd:cd05904 340 VEAKIVDPET-GESLPPNQTGELWIRGPSIMKGYLNNPEATAAT--------------IDKEG-------WL-------H 390
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 6319591 680 TGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLV 724
Cdd:cd05904 391 TGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEI 435
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
239-457 |
9.56e-15 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 78.99 E-value: 9.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 239 IHDIFQDNAEAFPERTCVVEtptLNSDKSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAG 318
Cdd:COG1022 13 LPDLLRRRAARFPDRVALRE---KEDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 319 ATfSVidPAYP--PARQTIY-LGVAKPRGLIViRAAGQLDQLVEdyINDELEIVSRInsIAIQENGTIEGGKLDNGEDVL 395
Cdd:COG1022 90 AV-TV--PIYPtsSAEEVAYiLNDSGAKVLFV-EDQEQLDKLLE--VRDELPSLRHI--VVLDPRGLRDDPRLLSLDELL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6319591 396 APYDHYKD----TRTGVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFNWMSKRFNLTENDKF 457
Cdd:COG1022 162 ALGREVADpaelEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRT 227
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
270-818 |
3.18e-14 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 76.79 E-value: 3.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 270 FTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFSVIDPAYPPARQTIYLGVAKPRglIVIR 349
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGAR--LVVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 350 AAGQLDQLvedyindeleivsrinsiaiqengtieggkldngedvlapydhykdtrtgvvvgpDSNPTLS-FTSGSEGIP 428
Cdd:cd05973 79 DAANRHKL-------------------------------------------------------DSDPFVMmFTSGTTGLP 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 429 KGVLGRHFSLAYYFNWMSKRFNLTENDKFTMLSgiahDP-----IQRDMFTPLFLGaqlyVPTQDDIG--TPGRLAEWMS 501
Cdd:cd05973 104 KGVPVPLRALAAFGAYLRDAVDLRPEDSFWNAA----DPgwaygLYYAITGPLALG----HPTILLEGgfSVESTWRVIE 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 502 KYGCTVTHLTPAMGQLL----TAQATTPFPKLHHAFFVGDILTKrDCLRLQTLAENCRIVNMYGTTETQRAVSyfevksk 577
Cdd:cd05973 176 RLGVTNLAGSPTAYRLLmaagAEVPARPKGRLRRVSSAGEPLTP-EVIRWFDAALGVPIHDHYGQTELGMVLA------- 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 578 ndDPNFLKKLKDVMPAGKGMLNVQLLVVNRNDRTQICGigeigeiyvRAGGLAEGYRGLPELnkekfvnnWFveKDHWNY 657
Cdd:cd05973 248 --NHHALEHPVHAGSAGRAMPGWRVAVLDDDGDELGPG---------EPGRLAIDIANSPLM--------WF--RGYQLP 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 658 LDKDngepwrqfwlgPRDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRKNADN 737
Cdd:cd05973 307 DTPA-----------IDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPER 375
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 738 EPTLITFMVPRfdkpddlskfqsdvpkevetdpivKGLIGYHLLSKDIRTFLKKRLASYAMPSLIVVMDKLPLNPNGKVD 817
Cdd:cd05973 376 TEVVKAFVVLR------------------------GGHEGTPALADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQ 431
|
.
gi 6319591 818 K 818
Cdd:cd05973 432 R 432
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
239-457 |
3.81e-14 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 77.22 E-value: 3.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 239 IHDIFQDNAEAFPERTCVVetptlnsDKSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAG 318
Cdd:PRK08279 39 LGDVFEEAAARHPDRPALL-------FEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 319 ATFSVIDPAYPPARQTIYLGVAKPRGLIViraAGQLDQLVEDyINDELEIVSRInSIAIQENGTIEGGKLD-NGEDVLAP 397
Cdd:PRK08279 112 AVVALLNTQQRGAVLAHSLNLVDAKHLIV---GEELVEAFEE-ARADLARPPRL-WVAGGDTLDDPEGYEDlAAAAAGAP 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6319591 398 yDHYKDTRTGVVVGpdsNPTLS-FTSGSEGIPKGVLGRHFSLAYYFNWMSKRFNLTENDKF 457
Cdd:PRK08279 187 -TTNPASRSGVTAK---DTAFYiYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVL 243
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
850-911 |
5.80e-14 |
|
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.
Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 67.59 E-value: 5.80e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6319591 850 REVRDLWLSILPTKPASVSPDDSFFDLGGHSILATKMIFTLKKKLQVDLPLGTIFKYPTIKA 911
Cdd:pfam00550 1 ERLRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
|
|
| PRK07201 |
PRK07201 |
SDR family oxidoreductase; |
972-1228 |
6.35e-14 |
|
SDR family oxidoreductase;
Pssm-ID: 235962 [Multi-domain] Cd Length: 657 Bit Score: 76.53 E-value: 6.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 972 NVFVTGVTGFLGSYILADLLGRSPKNysfKVFAHVRAkDEEAAFARLqkagitYGTWNekfASNIKVVLGDLSKSQFGLS 1051
Cdd:PRK07201 2 RYFVTGGTGFIGRRLVSRLLDRRREA---TVHVLVRR-QSLSRLEAL------AAYWG---ADRVVPLVGDLTEPGLGLS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 1052 DEKWMDLANtVDIIIHNGALVHWVYPYAKLRDPNVISTINVMSLAAVGKPKFFDFVSSTStldteyyfnlsdklVSEGKP 1131
Cdd:PRK07201 69 EADIAELGD-IDHVVHLAAIYDLTADEEAQRAANVDGTRNVVELAERLQAATFHHVSSIA--------------VAGDYE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 1132 GILESDDLmNSASGLTGGYGQSKWAAEYIIRRagERGLRGCIVRPGYVTGASANGSSNTDDFLLRFLKGSVQLGKIPD-- 1209
Cdd:PRK07201 134 GVFREDDF-DEGQGLPTPYHRTKFEAEKLVRE--ECGLPWRVYRPAVVVGDSRTGEMDKIDGPYYFFKVLAKLAKLPSwl 210
|
250 260
....*....|....*....|....
gi 6319591 1210 ----IE-NSVNMVPVDHVARVVVA 1228
Cdd:PRK07201 211 pmvgPDgGRTNIVPVDYVADALDH 234
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
251-816 |
1.35e-13 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 75.31 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 251 PERTCVV----ETPtlnsdKSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFSVIDP 326
Cdd:cd17634 67 GDRTAIIyegdDTS-----QSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 327 AYPPARQTIYLGVAKPRglIVIRAAG--------QLDQLVEDYINdeLEIVSRINSIAIQENGTIEGGklDNGEDVL--- 395
Cdd:cd17634 142 GFAPEAVAGRIIDSSSR--LLITADGgvragrsvPLKKNVDDALN--PNVTSVEHVIVLKRTGSDIDW--QEGRDLWwrd 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 396 ----APYDHYKdtrtgVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFNW-MSKRFNLTENDKFTMLSGI----AHD 466
Cdd:cd17634 216 liakASPEHQP-----EAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATtMKYVFDYGPGDIYWCTADVgwvtGHS 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 467 PIqrdMFTPLFLGAQ--LY--VPtqdDIGTPGRLAEWMSKYGCTVTHLTPAMGQLLTAQATtpfpklhhaffvgDILTKR 542
Cdd:cd17634 291 YL---LYGPLACGATtlLYegVP---NWPTPARMWQVVDKHGVNILYTAPTAIRALMAAGD-------------DAIEGT 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 543 DCLRLQTL--------------------AENCRIVNMYGTTETQRAVSyfevksknddPNflKKLKDVMPAG---KGMLN 599
Cdd:cd17634 352 DRSSLRILgsvgepinpeayewywkkigKEKCPVVDTWWQTETGGFMI----------TP--LPGAIELKAGsatRPVFG 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 600 VQLLVVNRNDRTQicGIGEIGEIYVRAG--GLAEGYRGLPELNKEKFvnnwfvekdhwnyldkdngepWRQFwlgprDRL 677
Cdd:cd17634 420 VQPAVVDNEGHPQ--PGGTEGNLVITDPwpGQTRTLFGDHERFEQTY---------------------FSTF-----KGM 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 678 YRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRKNADNEPTLITFMVPRfdkpddlsk 757
Cdd:cd17634 472 YFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLN--------- 542
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 6319591 758 fqsdvpkevetdpivKGLIGYHLLSKDIRTFLKKRLASYAMPSLIVVMDKLPLNPNGKV 816
Cdd:cd17634 543 ---------------HGVEPSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| SDR_e |
cd08946 |
extended (e) SDRs; Extended SDRs are distinct from classical SDRs. In addition to the Rossmann ... |
973-1238 |
2.20e-13 |
|
extended (e) SDRs; Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 212494 [Multi-domain] Cd Length: 200 Bit Score: 70.41 E-value: 2.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 973 VFVTGVTGFLGSYILADLLgrspknysfkvfahvrakdeeaafarlqkagitygtwnekfASNIKVVLGDLSksqfglsd 1052
Cdd:cd08946 1 ILVTGGAGFIGSHLVRRLL-----------------------------------------ERGHEVVVIDRL-------- 31
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 1053 ekwmdlantvDIIIHNGALVH----WVYPyAKLRDPNVISTINVMSLA-AVGKPKFFdFVSSTSTldteYYfnlsdklvs 1127
Cdd:cd08946 32 ----------DVVVHLAALVGvpasWDNP-DEDFETNVVGTLNLLEAArKAGVKRFV-YASSASV----YG--------- 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 1128 EGKPGILESDDLMNSASGltggYGQSKWAAEYIIRRAGER-GLRGCIVRPGYVTGASANGSSNTddFLLRFLKGSVQLGK 1206
Cdd:cd08946 87 SPEGLPEEEETPPRPLSP----YGVSKLAAEHLLRSYGESyGLPVVILRLANVYGPGQRPRLDG--VVNDFIRRALEGKP 160
|
250 260 270
....*....|....*....|....*....|....*
gi 6319591 1207 IP---DIENSVNMVPVDHVARVVVATSLNPPKENE 1238
Cdd:cd08946 161 LTvfgGGNQTRDFIHVDDVVRAILHALENPLEGGG 195
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
262-816 |
2.25e-13 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 74.55 E-value: 2.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 262 LNSDKSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFSVIDPAY--PPARQTIYLGV 339
Cdd:PRK04319 66 LDASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFmeEAVRDRLEDSE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 340 AKprglIVIRAAGQLDQLVEDYInDELEIVsrinsIAIQENGTIEGGKLDNGEDVLAPYDHYkdtrTGVVVGPDSNPTLS 419
Cdd:PRK04319 146 AK----VLITTPALLERKPADDL-PSLKHV-----LLVGEDVEEGPGTLDFNALMEQASDEF----DIEWTDREDGAILH 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 420 FTSGSEGIPKGVLgrHFSLAYYFNWMSKRF--NLTENDKF---------TMLS-GIahdpiqrdmFTPLFLGAQLYVptq 487
Cdd:PRK04319 212 YTSGSTGKPKGVL--HVHNAMLQHYQTGKYvlDLHEDDVYwctadpgwvTGTSyGI---------FAPWLNGATNVI--- 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 488 dDIG--TPGRLAEWMSKYGCTVTHLTP-AMGQLLTAQATTP----FPKLHHAFFVGDILTK------RDCLRLqtlaenc 554
Cdd:PRK04319 278 -DGGrfSPERWYRILEDYKVTVWYTAPtAIRMLMGAGDDLVkkydLSSLRHILSVGEPLNPevvrwgMKVFGL------- 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 555 RIVNMYGTTET--QRAVSYfevksknddPNFlkklkDVMPA--GKGMLNVQLLVVNRNDrtQICGIGEIGEIYVRAG--G 628
Cdd:PRK04319 350 PIHDNWWMTETggIMIANY---------PAM-----DIKPGsmGKPLPGIEAAIVDDQG--NELPPNRMGNLAIKKGwpS 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 629 LAEGYRGLPELNKEKFVNNWFVEKDHwNYLDKDnGEPWRQfwlgprdrlyrtgdlgrylpngdceccGRADDQVKIRGFR 708
Cdd:PRK04319 414 MMRGIWNNPEKYESYFAGDWYVSGDS-AYMDED-GYFWFQ---------------------------GRVDDVIKTSGER 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 709 IELGEIDTHISQHPLVREnitlvrknadneptlitfmVPRFDKPDDLskfqsdvpkeveTDPIVKGLI----GYHL---L 781
Cdd:PRK04319 465 VGPFEVESKLMEHPAVAE-------------------AGVIGKPDPV------------RGEIIKAFValrpGYEPseeL 513
|
570 580 590
....*....|....*....|....*....|....*
gi 6319591 782 SKDIRTFLKKRLASYAMPSLIVVMDKLPLNPNGKV 816
Cdd:PRK04319 514 KEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKI 548
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
412-822 |
3.26e-13 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 72.70 E-value: 3.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 412 PDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFNWMSKRFNLTENDK----------FTMLSGIahdpiqrdMFTPLFLGAQ 481
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRlcipvplfhcFGSVLGV--------LACLTHGATM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 482 LYVPTQDDigtPGRLAEWMSKYGCTVTHLTPAMgqlLTAQATTP-FPK--LHH---AFFVGDILTKRDCLRLQTLAENCR 555
Cdd:cd05917 73 VFPSPSFD---PLAVLEAIEKEKCTALHGVPTM---FIAELEHPdFDKfdLSSlrtGIMAGAPCPPELMKRVIEVMNMKD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 556 IVNMYGTTETQrAVSYfevKSKNDDPnFLKKLKDVmpaGKGMLNVQLLVVNRNDRTQiCGIGEIGEIYVRAGGLAEGYRG 635
Cdd:cd05917 147 VTIAYGMTETS-PVST---QTRTDDS-IEKRVNTV---GRIMPHTEAKIVDPEGGIV-PPVGVPGELCIRGYSVMKGYWN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 636 LPELNKEKfvnnwfVEKDHWnyldkdngepwrqfwlgprdrlYRTGDLGRYLPNGDCECCGRADDQVkIRGFR-IELGEI 714
Cdd:cd05917 218 DPEKTAEA------IDGDGW----------------------LHTGDLAVMDEDGYCRIVGRIKDMI-IRGGEnIYPREI 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 715 DTHISQHPLVREnitlvrknadneptlitfmVPRFDKPDDlsKFQSDVPKEVETDPivkgliGYHLLSKDIRTFLKKRLA 794
Cdd:cd05917 269 EEFLHTHPKVSD-------------------VQVVGVPDE--RYGEEVCAWIRLKE------GAELTEEDIKAYCKGKIA 321
|
410 420
....*....|....*....|....*...
gi 6319591 795 SYAMPSLIVVMDKLPLNPNGKVDKPKLQ 822
Cdd:cd05917 322 HYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
265-816 |
3.96e-13 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 73.70 E-value: 3.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 265 DKSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFSVIDPAYPPArqtiylgvakprg 344
Cdd:cd05923 24 ARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAA------------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 345 liviraagQLDQLVEdyiNDELEIVSRIN-SIAIQENGTIEGGKLDNGEDVlapydhykDTRTGVVVGP--------DSN 415
Cdd:cd05923 91 --------ELAELIE---RGEMTAAVIAVdAQVMDAIFQSGVRVLALSDLV--------GLGEPESAGPliedpprePEQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 416 PTLSF-TSGSEGIPKGVLGRHFSLAYYFNWMSKRFNLTENDKFTMLsGIAhdPIQRDM-FTPLFLGA-----QLYVPTQD 488
Cdd:cd05923 152 PAFVFyTSGTTGLPKGAVIPQRAAESRVLFMSTQAGLRHGRHNVVL-GLM--PLYHVIgFFAVLVAAlaldgTYVVVEEF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 489 DigtPGRLAEWMSKYGCTVTHLTPAMGQLLTA---QATTPFPKLHHAFFVGDILTKRDCLRLQTLAENcRIVNMYGTTET 565
Cdd:cd05923 229 D---PADALKLIEQERVTSLFATPTHLDALAAaaeFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPG-EKVNIYGTTEA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 566 QravsyfevksknddpNFLKkLKDVMP--AGKGMLNVQLLVVNRNDRTQ-ICGIGEIGEIYVRAGGLA--EGYRGLPELN 640
Cdd:cd05923 305 M---------------NSLY-MRDARTgtEMRPGFFSEVRIVRIGGSPDeALANGEEGELIVAAAADAafTGYLNQPEAT 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 641 KEKFVNNWfvekdhwnyldkdngepwrqfwlgprdrlYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQ 720
Cdd:cd05923 369 AKKLQDGW-----------------------------YRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSR 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 721 HPLVRENITLVRKNADNEPTLITFMVPRFDKP--DDLSKFQSDvpkevetdpivkgligyhllskdirtflkKRLASYAM 798
Cdd:cd05923 420 HPGVTEVVVIGVADERWGQSVTACVVPREGTLsaDELDQFCRA-----------------------------SELADFKR 470
|
570
....*....|....*...
gi 6319591 799 PSLIVVMDKLPLNPNGKV 816
Cdd:cd05923 471 PRRYFFLDELPKNAMNKV 488
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
246-821 |
4.33e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 73.81 E-value: 4.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 246 NAEAFPERTCVVetptlnsDKSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFSVID 325
Cdd:PRK07788 58 AARRAPDRAALI-------DERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLN 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 326 PAYPPaRQTIylGVAKPRGLIVIRAAGQLDQLVEDYINDeleiVSRINSIAIQ-ENGTIEGGKLDNGEDVLAPYDHYK-- 402
Cdd:PRK07788 131 TGFSG-PQLA--EVAAREGVKALVYDDEFTDLLSALPPD----LGRLRAWGGNpDDDEPSGSTDETLDDLIAGSSTAPlp 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 403 --DTRTGVVVgpdsnptlsFTSGSEGIPKGVLGRHFSLayyfnwmskrfnltendkFTMLSGI-AHDPIQRDMFT----P 475
Cdd:PRK07788 204 kpPKPGGIVI---------LTSGTTGTPKGAPRPEPSP------------------LAPLAGLlSRVPFRAGETTllpaP 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 476 LF-------------LGAQLYVPTQDDigtPGRLAEWMSKYGCTVTHLTPAMgqlltaqattpfpkLHHAFFVG-DILTK 541
Cdd:PRK07788 257 MFhatgwahltlamaLGSTVVLRRRFD---PEATLEDIAKHKATALVVVPVM--------------LSRILDLGpEVLAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 542 RDC--LRL------QTLAENCR---------IVNMYGTTEtqraVSYFEVKSKND---DPnflkklKDVMPAGKGMlNVQ 601
Cdd:PRK07788 320 YDTssLKIifvsgsALSPELATraleafgpvLYNLYGSTE----VAFATIATPEDlaeAP------GTVGRPPKGV-TVK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 602 LLVVNRNDRTQicgiGEIGEIYVRAGGLAEGYRGLPelNKEKFvnnwfvekdhwnyldkdngepwrqfwlgprDRLYRTG 681
Cdd:PRK07788 389 ILDENGNEVPR----GVVGRIFVGNGFPFEGYTDGR--DKQII------------------------------DGLLSSG 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 682 DLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVREnitLVRKNADNEPT---LITFMVPRFDKPDDlskf 758
Cdd:PRK07788 433 DVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVE---AAVIGVDDEEFgqrLRAFVVKAPGAALD---- 505
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6319591 759 qsdvpkevetdpivkgligyhllSKDIRTFLKKRLASYAMPSLIVVMDKLPLNPNGKVDKPKL 821
Cdd:PRK07788 506 -----------------------EDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKREL 545
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
267-726 |
4.59e-13 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 73.68 E-value: 4.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 267 SRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFSVIDPAYPPARQTIYLGVAKPRGLI 346
Cdd:cd05968 89 SRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALI 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 347 VIRAAGQLDQLVEdyINDELEIVSR----INSIAIQENGTIE-----GGKLDNGEDVLAPYDHYKDTrtgvvvGPDSNPT 417
Cdd:cd05968 169 TADGFTRRGREVN--LKEEADKACAqcptVEKVVVVRHLGNDftpakGRDLSYDEEKETAGDGAERT------ESEDPLM 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 418 LSFTSGSEGIPKGVLGRH--FSLAYYFNwMSKRFNLTENDKFTMLS--GIAHDPIQrdMFTPLFLGAQ--LY--VPTQDD 489
Cdd:cd05968 241 IIYTSGTTGKPKGTVHVHagFPLKAAQD-MYFQFDLKPGDLLTWFTdlGWMMGPWL--IFGGLILGATmvLYdgAPDHPK 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 490 igtPGRLAEWMSKYGCTVTHLTPAMGQLLTAQATTPfpklhhaffvgdiLTKRDCLRLQTLA------------------ 551
Cdd:cd05968 318 ---ADRLWRMVEDHEITHLGLSPTLIRALKPRGDAP-------------VNAHDLSSLRVLGstgepwnpepwnwlfetv 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 552 --ENCRIVNMYGTTETQRAVSyfevkskndDPNFLKKLKdvmPAG-----KGMLNVQLlvvnrnDRTQICGIGEIGEIYV 624
Cdd:cd05968 382 gkGRNPIINYSGGTEISGGIL---------GNVLIKPIK---PSSfngpvPGMKADVL------DESGKPARPEVGELVL 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 625 RAG--GLAEGYrglpelnkekfvnnWfveKDHWNYLDKdngePWRQFwlgprDRLYRTGDLGRYLPNGDCECCGRADDQV 702
Cdd:cd05968 444 LAPwpGMTRGF--------------W---RDEDRYLET----YWSRF-----DNVWVHGDFAYYDEEGYFYILGRSDDTI 497
|
490 500
....*....|....*....|....
gi 6319591 703 KIRGFRIELGEIDTHISQHPLVRE 726
Cdd:cd05968 498 NVAGKRVGPAEIESVLNAHPAVLE 521
|
|
| AR_FR_like_1_SDR_e |
cd05228 |
uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, ... |
973-1228 |
5.74e-13 |
|
uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, extended (e) SDRs; This subgroup contains proteins of unknown function related to aldehyde reductase and flavonoid reductase of the extended SDR-type. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it has an NADP-binding motif consensus that is slightly different from the canonical SDR form and lacks the Asn of the extended SDR active site tetrad. Aldehyde reductase I catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. The related flavonoid reductases act in the NADP-dependent reduction of flavonoids, ketone-containing plant secondary metabolites. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187539 [Multi-domain] Cd Length: 318 Bit Score: 71.55 E-value: 5.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 973 VFVTGVTGFLGSYILADLLGRSpknysFKVFAHVRAKDEeaafARLQKAGitygtwnekfasNIKVVLGDLSksqfglsD 1052
Cdd:cd05228 1 ILVTGATGFLGSNLVRALLAQG-----YRVRALVRSGSD----AVLLDGL------------PVEVVEGDLT-------D 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 1053 EKWMDLA-NTVDIIIHNGALVHWVYPYAK-LRDPNVISTINVMSLAAVGKPKFFDFVSSTSTLdteyyfnlsdklvseGK 1130
Cdd:cd05228 53 AASLAAAmKGCDRVFHLAAFTSLWAKDRKeLYRTNVEGTRNVLDAALEAGVRRVVHTSSIAAL---------------GG 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 1131 PGILESDDLMNSASGLTGG-YGQSKWAAEYIIRRAGERGLRGCIVRPGYVTGASANGSSNTDDFLLRFLKGSVQlGKIPD 1209
Cdd:cd05228 118 PPDGRIDETTPWNERPFPNdYYRSKLLAELEVLEAAAEGLDVVIVNPSAVFGPGDEGPTSTGLDVLDYLNGKLP-AYPPG 196
|
250
....*....|....*....
gi 6319591 1210 ienSVNMVPVDHVARVVVA 1228
Cdd:cd05228 197 ---GTSFVDVRDVAEGHIA 212
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
410-821 |
1.22e-12 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 71.61 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 410 VGPDSNPTLSFTSGSEGIPKGVL---GRHfslayYFNWMSKRFNL--TENDKFTMLSGIAHDPIQRDMFTPLFLGAQLYV 484
Cdd:cd05912 74 VKLDDIATIMYTSGTTGKPKGVQqtfGNH-----WWSAIGSALNLglTEDDNWLCALPLFHISGLSILMRSVIYGMTVYL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 485 PTQDDigtPGRLAEWMSKYGCTVTHLTPAMGQLLTAQATTPFPKlhhaffvgdilTKRdCLRL------QTLAENCR--- 555
Cdd:cd05912 149 VDKFD---AEQVLHLINSGKVTIISVVPTMLQRLLEILGEGYPN-----------NLR-CILLgggpapKPLLEQCKekg 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 556 --IVNMYGTTETQRAVSYFevksknddpNFLKKLKDVMPAGKGMLNVQLLVVNRNDRTqicgiGEIGEIYVRAGGLAEGY 633
Cdd:cd05912 214 ipVYQSYGMTETCSQIVTL---------SPEDALNKIGSAGKPLFPVELKIEDDGQPP-----YEVGEILLKGPNVTKGY 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 634 RGLPELNKEKFVNNWFvekdhwnyldkdngepwrqfwlgprdrlyRTGDLGrYLPN-GDCECCGRADDQVKIRGFRIELG 712
Cdd:cd05912 280 LNRPDATEESFENGWF-----------------------------KTGDIG-YLDEeGFLYVLDRRSDLIISGGENIYPA 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 713 EIDTHISQHPLVREnITLVrknadneptlitfmvprfDKPDDlsKFQSdVPkevetdpiVKGLIGYHLLSKD-IRTFLKK 791
Cdd:cd05912 330 EIEEVLLSHPAIKE-AGVV------------------GIPDD--KWGQ-VP--------VAFVVSERPISEEeLIAYCSE 379
|
410 420 430
....*....|....*....|....*....|
gi 6319591 792 RLASYAMPSLIVVMDKLPLNPNGKVDKPKL 821
Cdd:cd05912 380 KLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
672-918 |
2.17e-12 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 69.39 E-value: 2.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 672 GPRDRLYRTGDLGRYLPNGDceccGRADDQVKIRGFRIELGEIDTHISQHPLVREnitlvrknadneptlitfmvprfdk 751
Cdd:COG3433 77 QPGRQADDLRLLLRRGLGPG----GGLERLVQQVVIRAERGEEEELLLVLRAAAV------------------------- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 752 pddlsKFQSDVPKEVETDPIVKGLIGYH-----LLSKDIRTFLKKRLASYAMPSLIVVMDKLPLNPNGKVDKPKLQFPTP 826
Cdd:COG3433 128 -----VRVAVLAALRGAGVGLLLIVGAVaaldgLAAAAALAALDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 827 KQLNLVAentvSETDDSQFTNVEREVRDLWLSILPTKPASVSPDDSFFDLGGHSILATKMIFTLKKKlQVDLPLGTIFKY 906
Cdd:COG3433 203 EALLAAA----SPAPALETALTEEELRADVAELLGVDPEEIDPDDNLFDLGLDSIRLMQLVERWRKA-GLDVSFADLAEH 277
|
250
....*....|..
gi 6319591 907 PTIKAFAAEIDR 918
Cdd:COG3433 278 PTLAAWWALLAA 289
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
239-438 |
4.33e-12 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 70.39 E-value: 4.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 239 IHD-IFQdNAEAFPERTCVVETPTlnsdkSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKA 317
Cdd:PLN02246 25 LHDyCFE-RLSEFSDRPCLIDGAT-----GRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 318 GATFSVIDPAYPP---ARQTIYLGvAKprglIVIRAAGQLDQLVEDYINDELEIVsrinSIAIQENGTIEGGKLDNGEDV 394
Cdd:PLN02246 99 GAVTTTANPFYTPaeiAKQAKASG-AK----LIITQSCYVDKLKGLAEDDGVTVV----TIDDPPEGCLHFSELTQADEN 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 6319591 395 LAPydhykdtrtGVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSL 438
Cdd:PLN02246 170 ELP---------EVEISPDDVVALPYSSGTTGLPKGVMLTHKGL 204
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
245-818 |
2.06e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 68.14 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 245 DNAEAFPERTCVVEtptlnsdKSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFSvi 324
Cdd:PRK07470 15 QAARRFPDRIALVW-------GDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWV-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 325 dpaypPA--RQT----IYLGvakprgliviRAAGQLDQLVEDYINDELEIVSrinSIAIQENGTIEGGKLDNGEDVLAPY 398
Cdd:PRK07470 86 -----PTnfRQTpdevAYLA----------EASGARAMICHADFPEHAAAVR---AASPDLTHVVAIGGARAGLDYEALV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 399 DHYKDTRTGVVVGPDSNPT-LSFTSGSEGIPKGVLGRHFSLAYYF-NWMSKRF-NLTENDKFTM---LS---GIaHDPIQ 469
Cdd:PRK07470 148 ARHLGARVANAAVDHDDPCwFFFTSGTTGRPKAAVLTHGQMAFVItNHLADLMpGTTEQDASLVvapLShgaGI-HQLCQ 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 470 --RDMFTPLFLGAQLyvptqdDIGTPGRLAEwmsKYGCTVTHLTPAMGQLLT---AQATTPFPKLHHAFFVGDILTKRDC 544
Cdd:PRK07470 227 vaRGAATVLLPSERF------DPAEVWALVE---RHRVTNLFTVPTILKMLVehpAVDRYDHSSLRYVIYAGAPMYRADQ 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 545 LR-LQTLAEncRIVNMYGTTETQRAVSYF--EVKSKNDDPNflkklKDVMPAG---KGMlNVQLLvvnrNDRTQICGIGE 618
Cdd:PRK07470 298 KRaLAKLGK--VLVQYFGLGEVTGNITVLppALHDAEDGPD-----ARIGTCGferTGM-EVQIQ----DDEGRELPPGE 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 619 IGEIYVRAGGLAEGYRGLPELNKEKFVNNWFvekdhwnyldkdngepwrqfwlgprdrlyRTGDLGRYLPNGDCECCGRA 698
Cdd:PRK07470 366 TGEICVIGPAVFAGYYNNPEANAKAFRDGWF-----------------------------RTGDLGHLDARGFLYITGRA 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 699 DDQVKIRGFRIELGEIDTHISQHPLVREnitlvrknadneptlitfmVPRFDKPDdlskfqsdvPK--EVETDPIVKGlI 776
Cdd:PRK07470 417 SDMYISGGSNVYPREIEEKLLTHPAVSE-------------------VAVLGVPD---------PVwgEVGVAVCVAR-D 467
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 6319591 777 GYHLLSKDIRTFLKKRLASYAMPSLIVVMDKLPLNPNGKVDK 818
Cdd:PRK07470 468 GAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITK 509
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
247-742 |
2.82e-11 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 68.00 E-value: 2.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 247 AEAFPERTCVVETPTLNSD---KSRSFTYRDINRTSNIVAHYLIKTGIKRGD--VVMIysSRGVDLMVCVMGVLKAGATF 321
Cdd:PRK09274 16 AQERPDQLAVAVPGGRGADgklAYDELSFAELDARSDAIAHGLNAAGIGRGMraVLMV--TPSLEFFALTFALFKAGAVP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 322 SVIDPAypparqtiyLGV---------AKPRGLIVIRAAgqldqlvedyindelEIVSRINSIA---IQENGTIEGGKLD 389
Cdd:PRK09274 94 VLVDPG---------MGIknlkqclaeAQPDAFIGIPKA---------------HLARRLFGWGkpsVRRLVTVGGRLLW 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 390 NGEdVLAPYDHykDTRTGVVVGPDSNPT----LSFTSGSEGIPKGVLGRHFSLAYYFNWMSKRFnltendkftmlsGIAH 465
Cdd:PRK09274 150 GGT-TLATLLR--DGAAAPFPMADLAPDdmaaILFTSGSTGTPKGVVYTHGMFEAQIEALREDY------------GIEP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 466 DpiQRDMFT-PLF------LGAQLYVPTQD-------DigtPGRLAEWMSKYGCTVTHLTPAMGQLLTAQATT---PFPK 528
Cdd:PRK09274 215 G--EIDLPTfPLFalfgpaLGMTSVIPDMDptrpatvD---PAKLFAAIERYGVTNLFGSPALLERLGRYGEAngiKLPS 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 529 LHHAFFVGDILTKRDCLRLQT-LAENCRIVNMYGTTE-------TQRAVsyfevksknddpnfLKKLKDVMPAGKGML-- 598
Cdd:PRK09274 290 LRRVISAGAPVPIAVIERFRAmLPPDAEILTPYGATEalpissiESREI--------------LFATRAATDNGAGICvg 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 599 ----NVQLLVVNRNDR-------TQICGIGEIGEIYVRAGGLAEGYRGLPELNKEKFVNnwfvekdhwnyldkdngEPWR 667
Cdd:PRK09274 356 rpvdGVEVRIIAISDApipewddALRLATGEIGEIVVAGPMVTRSYYNRPEATRLAKIP-----------------DGQG 418
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6319591 668 QFWlgprdrlYRTGDLGRYLPNGDCECCGRADDQVKIRG---FRIELGEIdthISQHPLV-RENITLVRKNADNEPTLI 742
Cdd:PRK09274 419 DVW-------HRMGDLGYLDAQGRLWFCGRKAHRVETAGgtlYTIPCERI---FNTHPGVkRSALVGVGVPGAQRPVLC 487
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
416-726 |
7.57e-11 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 65.36 E-value: 7.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 416 PTLSFTSGSEGIPKGVLGRHFSL-AYYFNWMSKRFNLTENDKFTMLSGIAHDPIQRDMFTPLFLGAqLYVPTQDDIgTPG 494
Cdd:cd17635 4 LAVIFTSGTTGEPKAVLLANKTFfAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGG-LCVTGGENT-TYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 495 RLAEWMSKYGCTVTHLTP-AMGQL--LTAQATTPFPKLHHAFFVGDILTKRDcLRLQTLAENCRIVNMYGTTETQRAVSy 571
Cdd:cd17635 82 SLFKILTTNAVTTTCLVPtLLSKLvsELKSANATVPSLRLIGYGGSRAIAAD-VRFIEATGLTNTAQVYGLSETGTALC- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 572 feVKSKNDdpnflkkLKDVMPAGKGMLNVQLLVVNrNDRTQICGiGEIGEIYVRAGGLAEGYRGLPELNKEKFVNNWFve 651
Cdd:cd17635 160 --LPTDDD-------SIEINAVGRPYPGVDVYLAA-TDGIAGPS-ASFGTIWIKSPANMLGYWNNPERTAEVLIDGWV-- 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6319591 652 kdhwnyldkdngepwrqfwlgprdrlyRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRE 726
Cdd:cd17635 227 ---------------------------NTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQE 274
|
|
| UDP_G4E_4_SDR_e |
cd05232 |
UDP-glucose 4 epimerase, subgroup 4, extended (e) SDRs; UDP-glucose 4 epimerase (aka ... |
972-1235 |
9.13e-11 |
|
UDP-glucose 4 epimerase, subgroup 4, extended (e) SDRs; UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup is comprised of bacterial proteins, and includes the Staphylococcus aureus capsular polysaccharide Cap5N, which may have a role in the synthesis of UDP-N-acetyl-d-fucosamine. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187543 [Multi-domain] Cd Length: 303 Bit Score: 64.68 E-value: 9.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 972 NVFVTGVTGFLGSYILADLLGRspkNYSfkVFAHVRaKDEEAAfarlqkagitygtwnekfASNIKVVLGDLSKSQfgls 1051
Cdd:cd05232 1 KVLVTGANGFIGRALVDKLLSR---GEE--VRIAVR-NAENAE------------------PSVVLAELPDIDSFT---- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 1052 dekwmDLANTVDIIIHNGALVH-----WVYPYAKLRDPNVISTINVMSLAAVGKPKFFDFVSSTstldteyyfnlsdKLV 1126
Cdd:cd05232 53 -----DLFLGVDAVVHLAARVHvmndqGADPLSDYRKVNTELTRRLARAAARQGVKRFVFLSSV-------------KVN 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 1127 SEGKPG-ILESDDLMNSASGltggYGQSKWAAEYIIRRAGER-GLRGCIVRPG--YVTGASANGSSntddfLLRFLKgsv 1202
Cdd:cd05232 115 GEGTVGaPFDETDPPAPQDA----YGRSKLEAERALLELGASdGMEVVILRPPmvYGPGVRGNFAR-----LMRLID--- 182
|
250 260 270
....*....|....*....|....*....|....*..
gi 6319591 1203 qlGKIPDIENSVN----MVPVDHVArVVVATSLNPPK 1235
Cdd:cd05232 183 --RGLPLPPGAVKnrrsLVSLDNLV-DAIYLCISLPK 216
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
412-721 |
2.30e-10 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 64.66 E-value: 2.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 412 PDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFNWMSKRFNLTENDKFtmlsgIAHDPI------QRDMFTPLFLGAQLYV- 484
Cdd:cd05909 146 PDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVV-----FGALPFfhsfglTGCLWLPLLSGIKVVFh 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 485 --PTQddigtPGRLAEWMSKYGCTVTHLTPA--MGQLLTAQATTpFPKLHHAFFVGDILtkRDCLRlqTLAEN---CRIV 557
Cdd:cd05909 221 pnPLD-----YKKIPELIYDKKATILLGTPTflRGYARAAHPED-FSSLRLVVAGAEKL--KDTLR--QEFQEkfgIRIL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 558 NMYGTTETQRAVSYFEVKSKNddpnflkklkdvMPAGKGML--NVQLLVVNRNDRTQIcGIGEIGEIYVRAGGLAEGYRG 635
Cdd:cd05909 291 EGYGTTECSPVISVNTPQSPN------------KEGTVGRPlpGMEVKIVSVETHEEV-PIGEGGLLLVRGPNVMLGYLN 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 636 LPELNKEKFVNNWfvekdhwnyldkdngepwrqfwlgprdrlYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEID 715
Cdd:cd05909 358 EPELTSFAFGDGW-----------------------------YDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIE 408
|
....*.
gi 6319591 716 THISQH 721
Cdd:cd05909 409 DILSEI 414
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
251-821 |
2.58e-10 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 64.60 E-value: 2.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 251 PERTCVVetptlnsDKSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFSVIDPAYPP 330
Cdd:PRK03640 16 PDRTAIE-------FEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 331 ARQTIYLGVAKPRGLIViraagqldqlvEDYINDELEIVSRI--NSIAIQENGTIEggkldngedVLAPYDHykdtrtgv 408
Cdd:PRK03640 89 EELLWQLDDAEVKCLIT-----------DDDFEAKLIPGISVkfAELMNGPKEEAE---------IQEEFDL-------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 409 vvgpDSNPTLSFTSGSEGIPKGVL---GRHFSLAyyfnwMSKRFNL--TENDKFTMLSGIAHDPIQRDMFTPLFLGAQLY 483
Cdd:PRK03640 141 ----DEVATIMYTSGTTGKPKGVIqtyGNHWWSA-----VGSALNLglTEDDCWLAAVPIFHISGLSILMRSVIYGMRVV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 484 VPTQDDigtPGRLAEWMSKYGCTVTHLTPAMGQLLTAQattpFPKLH-HAFFvgdiltkRdCLRL------QTLAENCR- 555
Cdd:PRK03640 212 LVEKFD---AEKINKLLQTGGVTIISVVSTMLQRLLER----LGEGTyPSSF-------R-CMLLgggpapKPLLEQCKe 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 556 ----IVNMYGTTETQRAVSYFevkskndDPNF-LKKLKDvmpAGKGMLNVQLLVVnrnDRTQICGIGEIGEIYVRAGGLA 630
Cdd:PRK03640 277 kgipVYQSYGMTETASQIVTL-------SPEDaLTKLGS---AGKPLFPCELKIE---KDGVVVPPFEEGEIVVKGPNVT 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 631 EGYRGLPELNKEKFVNNWFvekdhwnyldkdngepwrqfwlgprdrlyRTGDLGrYLpngDCE----CCGRADDQVKIRG 706
Cdd:PRK03640 344 KGYLNREDATRETFQDGWF-----------------------------KTGDIG-YL---DEEgflyVLDRRSDLIISGG 390
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 707 FRIELGEIDTHISQHPLVrENITLVrknadneptlitfmvprfDKPDDlsKFQSdVPKEVetdpIVKgliGYHLLSKDIR 786
Cdd:PRK03640 391 ENIYPAEIEEVLLSHPGV-AEAGVV------------------GVPDD--KWGQ-VPVAF----VVK---SGEVTEEELR 441
|
570 580 590
....*....|....*....|....*....|....*
gi 6319591 787 TFLKKRLASYAMPSLIVVMDKLPLNPNGKVDKPKL 821
Cdd:PRK03640 442 HFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHEL 476
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
266-816 |
3.49e-10 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 64.64 E-value: 3.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 266 KSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFSVIDPAYPPARQTIYLGVAKPRgL 345
Cdd:cd05967 79 TERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPK-L 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 346 IVIRAAG-QLDQLVE--DYINDELEI-VSRINSIAIQENGTIEGGKLDNGEDVLApYDHYKDTRTGVVVGPDSNPTLS-- 419
Cdd:cd05967 158 IVTASCGiEPGKVVPykPLLDKALELsGHKPHHVLVLNRPQVPADLTKPGRDLDW-SELLAKAEPVDCVPVAATDPLYil 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 420 FTSGSEGIPKGVL---GRHfslAYYFNW-MSKRFNLTENDKFTMLSGIA----HDPIqrdMFTPLFLGAQ--LY--VPTq 487
Cdd:cd05967 237 YTSGTTGKPKGVVrdnGGH---AVALNWsMRNIYGIKPGDVWWAASDVGwvvgHSYI---VYGPLLHGATtvLYegKPV- 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 488 ddiGTPGRLAEW--MSKYGctVTHLTpamgqlltaQATTPFPKLHHAFFVGDILTKRDCLRLQTL---AENCR------- 555
Cdd:cd05967 310 ---GTPDPGAFWrvIEKYQ--VNALF---------TAPTAIRAIRKEDPDGKYIKKYDLSSLRTLflaGERLDpptlewa 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 556 -------IVNMYGTTETQRAV--SYFEVKSKNDDPNflkklkdvmPAGKGMLNVQLLVVNrnDRTQICGIGEIGEIyVRA 626
Cdd:cd05967 376 entlgvpVIDHWWQTETGWPItaNPVGLEPLPIKAG---------SPGKPVPGYQVQVLD--EDGEPVGPNELGNI-VIK 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 627 GGLAEGYrgLPEL--NKEKFVNNwfvekdhwnYLDKDNGepwrqfwlgprdrLYRTGDLGRYLPNGDCECCGRADDQVKI 704
Cdd:cd05967 444 LPLPPGC--LLTLwkNDERFKKL---------YLSKFPG-------------YYDTGDAGYKDEDGYLFIMGRTDDVINV 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 705 RGFRIELGEIDTHISQHPLVRENITLVRKNADNEPTLITFMVPRFDKPDDLSKfqsdvpkevetdpivkgligyhlLSKD 784
Cdd:cd05967 500 AGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKITAEE-----------------------LEKE 556
|
570 580 590
....*....|....*....|....*....|..
gi 6319591 785 IRTFLKKRLASYAMPSLIVVMDKLPLNPNGKV 816
Cdd:cd05967 557 LVALVREQIGPVAAFRLVIFVKRLPKTRSGKI 588
|
|
| PLN02503 |
PLN02503 |
fatty acyl-CoA reductase 2 |
972-1109 |
1.38e-09 |
|
fatty acyl-CoA reductase 2
Pssm-ID: 215279 [Multi-domain] Cd Length: 605 Bit Score: 62.57 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 972 NVFVTGVTGFLGSYILADLLGRSPKnySFKVFAHVRAKDEEAAFARLQKAGI----------TYGTWNEKFASNIKV-VL 1040
Cdd:PLN02503 121 NFLITGATGFLAKVLIEKILRTNPD--VGKIYLLIKAKDKEAAIERLKNEVIdaelfkclqeTHGKSYQSFMLSKLVpVV 198
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 1041 GDLSKSQFGLSDEKWMDLANTVDIIIHNGALVHWVYPYAKLRDPNVISTINVMSLAA-VGKPKFFDFVSS 1109
Cdd:PLN02503 199 GNVCESNLGLEPDLADEIAKEVDVIINSAANTTFDERYDVAIDINTRGPCHLMSFAKkCKKLKLFLQVST 268
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
268-822 |
1.56e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 62.10 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 268 RSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFSVIDPAYPPARQTIYLGVAKPRGLIV 347
Cdd:PRK07786 41 NTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 348 IRAAGQLDQLVEDyINDELEIVsrinsiaIQENGTIEGGKLDNgEDVLAPydhyKDTRTGVVVGPDSNPTL-SFTSGSEG 426
Cdd:PRK07786 121 EAALAPVATAVRD-IVPLLSTV-------VVAGGSSDDSVLGY-EDLLAE----AGPAHAPVDIPNDSPALiMYTSGTTG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 427 IPKGVLGRHFSLAYYFNWMSKRFNLTENDKFTML-SGIAHDPIQRDMFTPLFLGAQLYV-PTqddiGT--PGRLAEWMSK 502
Cdd:PRK07786 188 RPKGAVLTHANLTGQAMTCLRTNGADINSDVGFVgVPLFHIAGIGSMLPGLLLGAPTVIyPL----GAfdPGQLLDVLEA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 503 YGCTVTHLTPAMGQLLTAQATTPFPKLHHAFFVGDILTKRDCLrLQTLAE---NCRIVNMYGTTETQravsyfEVKSKND 579
Cdd:PRK07786 264 EKVTGIFLVPAQWQAVCAEQQARPRDLALRVLSWGAAPASDTL-LRQMAAtfpEAQILAAFGQTEMS------PVTCMLL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 580 DPNFLKKLKDVmpaGKGMLNVQLLVV--NRNDrtqiCGIGEIGEIYVRAGGLAEGYRGLPELNKEKFVNNWFvekdhwny 657
Cdd:PRK07786 337 GEDAIRKLGSV---GKVIPTVAARVVdeNMND----VPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWF-------- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 658 ldkdngepwrqfwlgprdrlyRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRKNADN 737
Cdd:PRK07786 402 ---------------------HSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKW 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 738 EPTLITFMVPRfDKPDDLskfqsdvpkEVEtdpivkgligyhllskDIRTFLKKRLASYAMPSLIVVMDKLPLNPNGKVD 817
Cdd:PRK07786 461 GEVPVAVAAVR-NDDAAL---------TLE----------------DLAEFLTDRLARYKHPKALEIVDALPRNPAGKVL 514
|
....*
gi 6319591 818 KPKLQ 822
Cdd:PRK07786 515 KTELR 519
|
|
| AR_SDR_e |
cd05227 |
aldehyde reductase, extended (e) SDRs; This subgroup contains aldehyde reductase of the ... |
973-1238 |
1.60e-09 |
|
aldehyde reductase, extended (e) SDRs; This subgroup contains aldehyde reductase of the extended SDR-type and related proteins. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it has an NADP-binding motif consensus that is slightly different from the canonical SDR form and lacks the Asn of the extended SDR active site tetrad. Aldehyde reductase I catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187538 [Multi-domain] Cd Length: 301 Bit Score: 60.75 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 973 VFVTGVTGFLGSYILADLLGRspkNYsfKVFAHVRAKDEEAAFARLQKAGITYGtwnekfasNIKVVLGDLSksqfgLSD 1052
Cdd:cd05227 2 VLVTGATGFIASHIVEQLLKA---GY--KVRGTVRSLSKSAKLKALLKAAGYND--------RLEFVIVDDL-----TAP 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 1053 EKWMDLANTVDIIIHNGALVHWVYPYAK--LRDPNVISTINVM-SLAAVGKPKFFDFVSSTSTLDTEYYFNlSDKLVSeg 1129
Cdd:cd05227 64 NAWDEALKGVDYVIHVASPFPFTGPDAEddVIDPAVEGTLNVLeAAKAAGSVKRVVLTSSVAAVGDPTAED-PGKVFT-- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 1130 kpgilESD--DLMNSASGLTGGYGQSKWAAEYIIRRAGERGLRG---CIVRPGYVTG----ASANGSSNtdDFLLRFLKG 1200
Cdd:cd05227 141 -----EEDwnDLTISKSNGLDAYIASKTLAEKAAWEFVKENKPKfelITINPGYVLGpsllADELNSSN--ELINKLLDG 213
|
250 260 270
....*....|....*....|....*....|....*...
gi 6319591 1201 SvqLGKIPDIENsVNMVPVDHVARVVVATSLNPPKENE 1238
Cdd:cd05227 214 K--LPAIPPNLP-FGYVDVRDVADAHVRALESPEAAGQ 248
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
559-818 |
2.76e-09 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 60.36 E-value: 2.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 559 MYGTTETQRAVSYFEVkskNDDPNflkklkdvmPAGKGMLNVQLLVVNRNDRTQicGIGEIGEIYVRAGGLAEGYRGLPE 638
Cdd:cd17637 142 LYGQTETSGLVTLSPY---RERPG---------SAGRPGPLVRVRIVDDNDRPV--PAGETGEIVVRGPLVFQGYWNLPE 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 639 LNKEKFVNNWfvekdhwnyldkdngepwrqfwlgprdrlYRTGDLGRYLPNGDCECCGR--ADDQVKIRGFRIELGEIDT 716
Cdd:cd17637 208 LTAYTFRNGW-----------------------------HHTGDLGRFDEDGYLWYAGRkpEKELIKPGGENVYPAEVEK 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 717 HISQHPLVRENITlvrknadneptlitfmvprFDKPDdlSKFQSDVPKEVETDPivkgliGYHLLSKDIRTFLKKRLASY 796
Cdd:cd17637 259 VILEHPAIAEVCV-------------------IGVPD--PKWGEGIKAVCVLKP------GATLTADELIEFVGSRIARY 311
|
250 260
....*....|....*....|..
gi 6319591 797 AMPSLIVVMDKLPLNPNGKVDK 818
Cdd:cd17637 312 KKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
238-821 |
7.31e-09 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 60.21 E-value: 7.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 238 CIHDIFQDNAEAFPERTCVVEtptlnSDKSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKA 317
Cdd:PRK08315 17 TIGQLLDRTAARYPDREALVY-----RDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 318 GATFSVIDPAYPPARQTIYLGVAKPRGLIVIRA-------------AGQLDQLVEDYINDE----LEIVSRInsiaiqen 380
Cdd:PRK08315 92 GAILVTINPAYRLSELEYALNQSGCKALIAADGfkdsdyvamlyelAPELATCEPGQLQSArlpeLRRVIFL-------- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 381 GTIEGGKLDNGEDVLAPYDHYKDTRTGVV---VGPDSNPTLSFTSGSEGIPKGVLGRHFSL---AYyfnWMSKRFNLTEN 454
Cdd:PRK08315 164 GDEKHPGMLNFDELLALGRAVDDAELAARqatLDPDDPINIQYTSGTTGFPKGATLTHRNIlnnGY---FIGEAMKLTEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 455 DK----------FTM----LSGIAHdpiqrdmftplflGAQLYVPTqdDIGTPGRLAEWMSKYGCTVTHLTPAMgqlLTA 520
Cdd:PRK08315 241 DRlcipvplyhcFGMvlgnLACVTH-------------GATMVYPG--EGFDPLATLAAVEEERCTALYGVPTM---FIA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 521 QattpfpkLHHAFFvgdilTKRD--CLRLQTLA-ENC------RIV---NM------YGTTET-----QRAVsyfevksk 577
Cdd:PRK08315 303 E-------LDHPDF-----ARFDlsSLRTGIMAgSPCpievmkRVIdkmHMsevtiaYGMTETspvstQTRT-------- 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 578 nDDPnFLKKLKDVmpaGKGMLNVQLLVVNrNDRTQICGIGEIGEIYVRAGGLAEGYRGLPELNKEKfvnnwfvekdhwny 657
Cdd:PRK08315 363 -DDP-LEKRVTTV---GRALPHLEVKIVD-PETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEA-------------- 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 658 LDKDNgepwrqfWLgprdrlyRTGDLGRYLPNGDCECCGRADDQVkIRGfrielG------EIDTHISQHPLVREnitlv 731
Cdd:PRK08315 423 IDADG-------WM-------HTGDLAVMDEEGYVNIVGRIKDMI-IRG-----GeniyprEIEEFLYTHPKIQD----- 477
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 732 rknadneptlitfmVPRFDKPDDlsKFQSDV-----PKEvetdpivkgliGYHLLSKDIRTFLKKRLASYAMPSLIVVMD 806
Cdd:PRK08315 478 --------------VQVVGVPDE--KYGEEVcawiiLRP-----------GATLTEEDVRDFCRGKIAHYKIPRYIRFVD 530
|
650
....*....|....*
gi 6319591 807 KLPLNPNGKVDKPKL 821
Cdd:PRK08315 531 EFPMTVTGKIQKFKM 545
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
268-776 |
8.37e-09 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 59.53 E-value: 8.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 268 RSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGAtfsVIDPAYPPArqtiylgvakprgliv 347
Cdd:cd05907 4 QPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGA---VPVPIYPTS---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 348 irAAGQLDQLVEDyindeleivSRINSIaiqengtieggkldngedvlapydhykdtrtgVVVGPDSNPTLSFTSGSEGI 427
Cdd:cd05907 65 --SAEQIAYILND---------SEAKAL--------------------------------FVEDPDDLATIIYTSGTTGR 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 428 PKGVLGRHFSLAYYFNWMSKRFNLTENDKF-TMLSgIAHDPIQR-DMFTPLFLGAQLYVPTQDDIGTPGrLAEWMSKYGC 505
Cdd:cd05907 102 PKGVMLSHRNILSNALALAERLPATEGDRHlSFLP-LAHVFERRaGLYVPLLAGARIYFASSAETLLDD-LSEVRPTVFL 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 506 TVTHLTPAMGQLLTAQATTPFPKLHHAFFVGDILTKRDC------LRLQTLAE--NCRIVNMYGTTETQRAVSYfevksk 577
Cdd:cd05907 180 AVPRVWEKVYAAIKVKAVPGLKRKLFDLAVGGRLRFAASggaplpAELLHFFRalGIPVYEGYGLTETSAVVTL------ 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 578 nddpNFLKKLK--DVMPAGKGMlnvqllvvnrndrtqICGIGEIGEIYVRAGGLAEGYRGLPELNKEKFvnnwfvekdhw 655
Cdd:cd05907 254 ----NPPGDNRigTVGKPLPGV---------------EVRIADDGEILVRGPNVMLGYYKNPEATAEAL----------- 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 656 nylDKDNgepwrqfWLgprdrlyRTGDLGRYLPNGDCECCGRADD-QVKIRGFRIELGEIDTHISQHPLVrENITLVrkn 734
Cdd:cd05907 304 ---DADG-------WL-------HTGDLGEIDEDGFLHITGRKKDlIITSGGKNISPEPIENALKASPLI-SQAVVI--- 362
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 6319591 735 ADNEPTLITFMVPRFDKPDDLSKFQSDVPK---EVETDPIVKGLI 776
Cdd:cd05907 363 GDGRPFLVALIVPDPEALEAWAEEHGIAYTdvaELAANPAVRAEI 407
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
678-819 |
1.01e-08 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 59.76 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 678 YRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRKNADNEPTLITFMVPRFDKPD---D 754
Cdd:PTZ00237 494 YNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQSNqsiD 573
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6319591 755 LSKFQSDVPKevetdpivkgligyhLLSKDIrtflkkrlASYAMPSLIVVMDKLPLNPNGKVDKP 819
Cdd:PTZ00237 574 LNKLKNEINN---------------IITQDI--------ESLAVLRKIIIVNQLPKTKTGKIPRQ 615
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
239-435 |
1.03e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 59.51 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 239 IHDIFQDNAEAFPERTCVVETPtlnsdksRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAG 318
Cdd:PRK07798 5 IADLFEAVADAVPDRVALVCGD-------RRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 319 ATFSVIDPAYPPARQTIYLGVAKPRGLIVIRaagQLDQLVEDyINDELEIVSRINSIaiqENGTieGGKLDNG----EDV 394
Cdd:PRK07798 78 AVPVNVNYRYVEDELRYLLDDSDAVALVYER---EFAPRVAE-VLPRLPKLRTLVVV---EDGS--GNDLLPGavdyEDA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 6319591 395 LAPYDhykDTRTGVVVGPDSNPTLsFTSGSEGIPKGVLGRH 435
Cdd:PRK07798 149 LAAGS---PERDFGERSPDDLYLL-YTGGTTGMPKGVMWRQ 185
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
848-918 |
1.06e-08 |
|
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.
Pssm-ID: 214834 [Multi-domain] Cd Length: 86 Bit Score: 53.41 E-value: 1.06e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6319591 848 VEREVRDLWLSILPTKPAS-VSPDDSFFDLGGHSILATKMIFTLKKKLQVDLPLGTIFKYPTIKAFAAEIDR 918
Cdd:smart00823 13 LLDLVREQVAAVLGHAAAEaIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAA 84
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
7-223 |
1.41e-08 |
|
Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.
Pssm-ID: 395541 [Multi-domain] Cd Length: 454 Bit Score: 58.88 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 7 WIEKLD--NPTLSvLPHDFLRPQQEPYtKQATYSLQLPQLDV--------PHDSfsNKYAVALSVWAALIYRVTGDDDIV 76
Cdd:pfam00668 198 WLEQLEgeLPVLQ-LPKDYARPADRSF-KGDRLSFTLDEDTEellrklakAHGT--TLNDVLLAAYGLLLSRYTGQDDIV 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 77 --LYIAN--------------NKI-LRFNIQPTWSFNELYSTINNELNKLNSiEANFSFDELAEKIQSCQDLERTPQLFR 139
Cdd:pfam00668 274 vgTPGSGrpspdiermvgmfvNTLpLRIDPKGGKTFSELIKRVQEDLLSAEP-HQGYPFGDLVNDLRLPRDLSRHPLFDP 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 140 LAFLEN---QDFKLDEF------------KHHLVDFALNL--DTSNNAHVLNLIYNSLLYSNERVTIVADQFTQYLTAAL 202
Cdd:pfam00668 353 MFSFQNylgQDSQEEEFqlseldlsvssvIEEEAKYDLSLtaSERGGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAI 432
|
250 260
....*....|....*....|.
gi 6319591 203 SDPSNCITKISLITASSKDSL 223
Cdd:pfam00668 433 AHPSQPLSELDLLSDAEKQKL 453
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
543-821 |
2.00e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 58.46 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 543 DCLRLQTLAENcRIVNMYGTTETQRAVSyfevkSKNDDPnflKKLKDVMPAGKGmlnVQLLVVNRNDRTQICGIGEIGEI 622
Cdd:PRK07787 257 VFDRLAALTGH-RPVERYGMTETLITLS-----TRADGE---RRPGWVGLPLAG---VETRLVDEDGGPVPHDGETVGEL 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 623 YVRAGGLAEGYRGLPELNKEKFVNnwfvekDHWnyldkdngepwrqfwlgprdrlYRTGDLGRYLPNGDCECCGR-ADDQ 701
Cdd:PRK07787 325 QVRGPTLFDGYLNRPDATAAAFTA------DGW----------------------FRTGDVAVVDPDGMHRIVGReSTDL 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 702 VKIRGFRIELGEIDTHISQHPLVRENITLVRKNADNEPTLITFMVPRfdkpddlskfqsdvpkeveTDPIVKGLIGyhll 781
Cdd:PRK07787 377 IKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGA-------------------DDVAADELID---- 433
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 6319591 782 skdirtFLKKRLASYAMPSLIVVMDKLPLNPNGKVDKPKL 821
Cdd:PRK07787 434 ------FVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQL 467
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
246-822 |
2.90e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 58.10 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 246 NAEAFPERTCVVETPTlnsdkSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFSVID 325
Cdd:PRK13390 6 HAQIAPDRPAVIVAET-----GEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAIN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 326 PAYPPARQTIYLGVAKPRGLIvirAAGQLDQLVEDyINDELEIvsRINSiaiqengtieGGKLDNgedvlapYDHYKDTR 405
Cdd:PRK13390 81 HHLTAPEADYIVGDSGARVLV---ASAALDGLAAK-VGADLPL--RLSF----------GGEIDG-------FGSFEAAL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 406 TGvvVGP--DSNP---TLSFTSGSEGIPKGVL----GRH--------FSLAYYFnwmskrFNLTENDKFTMLSGIAHDPI 468
Cdd:PRK13390 138 AG--AGPrlTEQPcgaVMLYSSGTTGFPKGIQpdlpGRDvdapgdpiVAIARAF------YDISESDIYYSSAPIYHAAP 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 469 QRDMFTPLFLGAQLYVPTQDDIGTPGRLAEwmsKYGCTVTHLTPAMG-QLLTAQAttpfpklhhaffvgDILTKRDCLRL 547
Cdd:PRK13390 210 LRWCSMVHALGGTVVLAKRFDAQATLGHVE---RYRITVTQMVPTMFvRLLKLDA--------------DVRTRYDVSSL 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 548 QTL---AENCR--------------IVNMYGTTETQrAVSYFevksknDDPNFLKKLKDVMPAGKGMLNVQllvvnrNDR 610
Cdd:PRK13390 273 RAVihaAAPCPvdvkhamidwlgpiVYEYYSSTEAH-GMTFI------DSPDWLAHPGSVGRSVLGDLHIC------DDD 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 611 TQICGIGEIGEIYVRAGGLAEGYRGLPELNkekfvnnwfVEKDHwnyldkdngePWRQFWLgprdrlyRTGDLGRYLPNG 690
Cdd:PRK13390 340 GNELPAGRIGTVYFERDRLPFRYLNDPEKT---------AAAQH----------PAHPFWT-------TVGDLGSVDEDG 393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 691 DCECCGRADDQVKIRGFRIELGEIDTHISQHPLVREnitlvrknadneptlitfmVPRFDKPDdlSKFQSDVPKEVEtdp 770
Cdd:PRK13390 394 YLYLADRKSFMIISGGVNIYPQETENALTMHPAVHD-------------------VAVIGVPD--PEMGEQVKAVIQ--- 449
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 6319591 771 IVKGLIGYHLLSKDIRTFLKKRLASYAMPSLIVVMDKLPLNPNGKVDKPKLQ 822
Cdd:PRK13390 450 LVEGIRGSDELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
251-566 |
3.33e-08 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 57.83 E-value: 3.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 251 PERTCVVETPtlNSDKSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFSVIDPAYPP 330
Cdd:cd05921 9 PDRTWLAERE--GNGGWRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYSL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 331 -----ARQTIYLGVAKPRGLIVIRAAGQLDQLVEDYINDELEIVSR-----INSIAIQEN-GTIEGGKLDNGEDvlapyd 399
Cdd:cd05921 87 msqdlAKLKHLFELLKPGLVFAQDAAPFARALAAIFPLGTPLVVSRnavagRGAISFAELaATPPTAAVDAAFA------ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 400 hykdtrtgvVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLA---------YYF---------NWMSKRFNLTENDKFTMLs 461
Cdd:cd05921 161 ---------AVGPDTVAKFLFTSGSTGLPKAVINTQRMLCanqamleqtYPFfgeeppvlvDWLPWNHTFGGNHNFNLV- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 462 giahdpiqrdmftpLFLGAQLYVptqdDIG--TPGRLAEW---MSKYGCTVTHLTPAMGQLLT-------AQATTPFPKL 529
Cdd:cd05921 231 --------------LYNGGTLYI----DDGkpMPGGFEETlrnLREISPTVYFNVPAGWEMLVaalekdeALRRRFFKRL 292
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 6319591 530 HHAFFVG-----DILTKRDCLRLQTLAENCRIVNMYGTTETQ 566
Cdd:cd05921 293 KLMFYAGaglsqDVWDRLQALAVATVGERIPMMAGLGATETA 334
|
|
| 3b-HSD_HSDB1_like_SDR_e |
cd09811 |
human 3beta-HSD (hydroxysteroid dehydrogenase) and HSD3B1(delta 5-delta 4-isomerase)-like, ... |
975-1196 |
2.04e-07 |
|
human 3beta-HSD (hydroxysteroid dehydrogenase) and HSD3B1(delta 5-delta 4-isomerase)-like, extended (e) SDRs; This extended-SDR subgroup includes human 3 beta-HSD/HSD3B1 and C(27) 3beta-HSD/ [3beta-hydroxy-delta(5)-C(27)-steroid oxidoreductase; HSD3B7], and related proteins. These proteins have the characteristic active site tetrad and NAD(P)-binding motif of extended SDRs. 3 beta-HSD catalyzes the oxidative conversion of delta 5-3 beta-hydroxysteroids to the delta 4-3-keto configuration; this activity is essential for the biosynthesis of all classes of hormonal steroids. C(27) 3beta-HSD is a membrane-bound enzyme of the endoplasmic reticulum, it catalyzes the isomerization and oxidation of 7alpha-hydroxylated sterol intermediates, an early step in bile acid biosynthesis. Mutations in the human gene encoding C(27) 3beta-HSD underlie a rare autosomal recessive form of neonatal cholestasis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187671 [Multi-domain] Cd Length: 354 Bit Score: 54.82 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 975 VTGVTGFLGSYILADLLGRSPKNYSFKVFAHVRAKDEEAAFARLQkaGITYgtwnekfasnIKVVLGDLSKSQFglsdek 1054
Cdd:cd09811 4 VTGGGGFLGQHIIRLLLERKEELKEIRVLDKAFGPELIEHFEKSQ--GKTY----------VTDIEGDIKDLSF------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 1055 WMDLANTVDIIIHNGALVHWVYP--YAKLRDPNVISTINVMSLAAVGKPKFFDFVSSTSTLDTEYYfnlsdklvseGKPg 1132
Cdd:cd09811 66 LFRACQGVSVVIHTAAIVDVFGPpnYEELEEVNVNGTQAVLEACVQNNVKRLVYTSSIEVAGPNFK----------GRP- 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 1133 ILESDDLMNSASGLTGGYGQSKWAAEYIIRRAGERGLRG------CIVRPGYVTGASANGSSNTDDFLLR 1196
Cdd:cd09811 135 IFNGVEDTPYEDTSTPPYASSKLLAENIVLNANGAPLKQggylvtCALRPMYIYGEGSHFLTEIFDFLLT 204
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
271-725 |
2.46e-07 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 54.77 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 271 TYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFSVIDPAYPPARQTIYLGVAKPRGLIVIRA 350
Cdd:cd05910 4 SFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAFIGIPK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 351 AgqldqlvedyindeleivsrinsiaiqengtieggkldngEDVLApydhykdtrtgvvvgpdsnptLSFTSGSEGIPKG 430
Cdd:cd05910 84 A----------------------------------------DEPAA---------------------ILFTSGSTGTPKG 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 431 VLGRHFSLAYYFNWMSKRFnltendkftmlsGIAHDpiQRDMFT-PLF------LGAQLYVPTQDDI----GTPGRLAEW 499
Cdd:cd05910 103 VVYRHGTFAAQIDALRQLY------------GIRPG--EVDLATfPLFalfgpaLGLTSVIPDMDPTrparADPQKLVGA 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 500 MSKYGCTVTHLTPAMGQLLT---AQATTPFPKLHHAFFVGDILTKRDCLRL-QTLAENCRIVNMYGTTETQ--RAVSYFE 573
Cdd:cd05910 169 IRQYGVSIVFGSPALLERVArycAQHGITLPSLRRVLSAGAPVPIALAARLrKMLSDEAEILTPYGATEALpvSSIGSRE 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 574 VKSKNDDPNflKKLKDVMpAGKGMLNVQLLVVNRND-------RTQICGIGEIGEIYVRAGGLAEGYRGLPELNKekfvn 646
Cdd:cd05910 249 LLATTTAAT--SGGAGTC-VGRPIPGVRVRIIEIDDepiaewdDTLELPRGEIGEITVTGPTVTPTYVNRPVATA----- 320
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6319591 647 nwfVEKDHwnyldkDNGEpwrQFWlgprdrlYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVR 725
Cdd:cd05910 321 ---LAKID------DNSE---GFW-------HRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVR 380
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
556-824 |
2.61e-07 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 55.09 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 556 IVNMYGTTETQrAVSYfevkskNDDPNFLKKLKDVmpaGKGMLNVQLLVVNRNDRtqICGIGEIGEIYVRAGGLAE-GYR 634
Cdd:PRK12406 299 IYEYYGSTESG-AVTF------ATSEDALSHPGTV---GKAAPGAELRFVDEDGR--PLPQGEIGEIYSRIAGNPDfTYH 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 635 GLPELNKEkfvnnwfvekdhwnyLDkdngepwrqfwlgpRDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEI 714
Cdd:PRK12406 367 NKPEKRAE---------------ID--------------RGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEI 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 715 DTHISQHPLVRENITlvrknadneptlitfmvprFDKPDdlSKFQSDVPKEVETDPivkgliGYHLLSKDIRTFLKKRLA 794
Cdd:PRK12406 418 EAVLHAVPGVHDCAV-------------------FGIPD--AEFGEALMAVVEPQP------GATLDEADIRAQLKARLA 470
|
250 260 270
....*....|....*....|....*....|
gi 6319591 795 SYAMPSLIVVMDKLPLNPNGKVDKPKLQFP 824
Cdd:PRK12406 471 GYKVPKHIEIMAELPREDSGKIFKRRLRDP 500
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
556-824 |
4.48e-07 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 54.38 E-value: 4.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 556 IVNMYGTTEtqraVSYFEVKSKNDdpnfLKKLKDVmpAGKGMLNVQLLVVNRNDRTqiCGIGEIGEIYVRAGGLAEGYRg 635
Cdd:PRK13382 340 IYNNYNATE----AGMIATATPAD----LRAAPDT--AGRPAEGTEIRILDQDFRE--VPTGEVGTIFVRNDTQFDGYT- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 636 lPELNKEKfvnnwfvekdhwnyldkdngepwrqfwlgpRDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEID 715
Cdd:PRK13382 407 -SGSTKDF------------------------------HDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 716 THISQHPLVREniTLVRKNADNE--PTLITFMVPRfdkpDDLSKFQSDVPKEVetdpivkgligyhllskdirtflKKRL 793
Cdd:PRK13382 456 KTLATHPDVAE--AAVIGVDDEQygQRLAAFVVLK----PGASATPETLKQHV-----------------------RDNL 506
|
250 260 270
....*....|....*....|....*....|.
gi 6319591 794 ASYAMPSLIVVMDKLPLNPNGKVDKPKLQFP 824
Cdd:PRK13382 507 ANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| 3b-HSD-like_SDR_e |
cd05241 |
3beta-hydroxysteroid dehydrogenases (3b-HSD)-like, extended (e) SDRs; Extended SDR family ... |
972-1235 |
5.37e-07 |
|
3beta-hydroxysteroid dehydrogenases (3b-HSD)-like, extended (e) SDRs; Extended SDR family domains belonging to this subgroup have the characteristic active site tetrad and a fairly well-conserved NAD(P)-binding motif. 3b-HSD catalyzes the NAD-dependent conversion of various steroids, such as pregnenolone to progesterone, or androstenediol to testosterone. This subgroup includes an unusual bifunctional 3b-HSD/C-4 decarboxylase from Arabidopsis thaliana, and Saccharomyces cerevisiae ERG26, a 3b-HSD/C-4 decarboxylase, involved in the synthesis of ergosterol, the major sterol of yeast. It also includes human 3 beta-HSD/HSD3B1 and C(27) 3beta-HSD/ [3beta-hydroxy-delta(5)-C(27)-steroid oxidoreductase; HSD3B7]. C(27) 3beta-HSD/HSD3B7 is a membrane-bound enzyme of the endoplasmic reticulum, that catalyzes the isomerization and oxidation of 7alpha-hydroxylated sterol intermediates, an early step in bile acid biosynthesis. Mutations in the human NSDHL (NAD(P)H steroid dehydrogenase-like protein) cause CHILD syndrome (congenital hemidysplasia with ichthyosiform nevus and limb defects), an X-linked dominant, male-lethal trait. Mutations in the human gene encoding C(27) 3beta-HSD underlie a rare autosomal recessive form of neonatal cholestasis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187552 [Multi-domain] Cd Length: 331 Bit Score: 53.20 E-value: 5.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 972 NVFVTGVTGFLGSYILADLLGRSPknysfkvfAHVRAKDeeaafarLQKAGITYGTWNEkfaSNIKVVLGDLSKSQFGLS 1051
Cdd:cd05241 1 SVLVTGGSGFFGERLVKQLLERGG--------TYVRSFD-------IAPPGEALSAWQH---PNIEFLKGDITDRNDVEQ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 1052 DEkwmdlaNTVDIIIHNGALVHWVYPYAKLRDPNVISTINVMSL-AAVGKPKFFdFVSSTStldteyyfnlsdklVSEGK 1130
Cdd:cd05241 63 AL------SGADCVFHTAAIVPLAGPRDLYWEVNVGGTQNVLDAcQRCGVQKFV-YTSSSS--------------VIFGG 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 1131 PGILESDDLMNSASGLTGGYGQSKWAAEYIIRRA-GERGLRGCIVRPGYVTGasangssNTDDFLLRFLKGSVQLG---- 1205
Cdd:cd05241 122 QNIHNGDETLPYPPLDSDMYAETKAIAEIIVLEAnGRDDLLTCALRPAGIFG-------PGDQGLVPILFEWAEKGlvkf 194
|
250 260 270
....*....|....*....|....*....|..
gi 6319591 1206 KIPDIENSVNMVPVDHV--ARVVVATSLNPPK 1235
Cdd:cd05241 195 VFGRGNNLVDFTYVHNLahAHILAAAALVKGK 226
|
|
| Epimerase |
pfam01370 |
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ... |
973-1200 |
5.97e-07 |
|
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. The proteins in this family use nucleotide-sugar substrates for a variety of chemical reactions.
Pssm-ID: 396097 [Multi-domain] Cd Length: 238 Bit Score: 52.30 E-value: 5.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 973 VFVTGVTGFLGSYILAdllgrspknysfkvfahvrakdeeaafaRLQKAGIT-YGTWNEKFASNIKVvLGDLSKSQFGLS 1051
Cdd:pfam01370 1 ILVTGATGFIGSHLVR----------------------------RLLEKGYEvIGLDRLTSASNTAR-LADLRFVEGDLT 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 1052 DEKWMD---LANTVDIIIHNGALVHW----VYPYAKLRDpNVISTINVMSLA-AVGKPKFFdFVSSTStldtEYyfnlsd 1123
Cdd:pfam01370 52 DRDALEkllADVRPDAVIHLAAVGGVgasiEDPEDFIEA-NVLGTLNLLEAArKAGVKRFL-FASSSE----VY------ 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 1124 klvseGK-PGILESDDLMNSASGLTGGYGQSKWAAEYIIRRAGER-GLRGCIVRPGYVTGASANGSSNT---DDFLLRFL 1198
Cdd:pfam01370 120 -----GDgAEIPQEETTLTGPLAPNSPYAAAKLAGEWLVLAYAAAyGLRAVILRLFNVYGPGDNEGFVSrviPALIRRIL 194
|
..
gi 6319591 1199 KG 1200
Cdd:pfam01370 195 EG 196
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
410-779 |
6.85e-07 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 53.67 E-value: 6.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 410 VGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFNWMSKRFNLTENDkfTMLSGIAhdPIQRDMFT-----PLFLGAQL-- 482
Cdd:PRK06334 180 KDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDD--VMMSFLP--PFHAYGFNsctlfPLLSGVPVvf 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 483 -YVPTQddigtPGRLAEWMSKYGCTVTHLTPA-MGQLLTA--QATTPFPKLHHAFFVGDILtkRDCLRLQTLAENCRIV- 557
Cdd:PRK06334 256 aYNPLY-----PKKIVEMIDEAKVTFLGSTPVfFDYILKTakKQESCLPSLRFVVIGGDAF--KDSLYQEALKTFPHIQl 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 558 -NMYGTTETQRAVSYFEVKSKnddpnflKKLKDV-MPAgKGMlnvQLLVVNRNDRTQICGiGEIGEIYVRAGGLAEGYRG 635
Cdd:PRK06334 329 rQGYGTTECSPVITINTVNSP-------KHESCVgMPI-RGM---DVLIVSEETKVPVSS-GETGLVLTRGTSLFSGYLG 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 636 LPElnkekfvNNWFVEKDhwnyldkdnGEPWrqfwlgprdrlYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEID 715
Cdd:PRK06334 397 EDF-------GQGFVELG---------GETW-----------YVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALE 449
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 716 THISQH---PLVRENITLVRKNADNEPT---LITFMvprfdkPDDLSKFqSDVPKEVETDPIVKglIGYH 779
Cdd:PRK06334 450 SILMEGfgqNAADHAGPLVVCGLPGEKVrlcLFTTF------PTSISEV-NDILKNSKTSSILK--ISYH 510
|
|
| 3Beta_HSD |
pfam01073 |
3-beta hydroxysteroid dehydrogenase/isomerase family; The enzyme 3 beta-hydroxysteroid ... |
975-1259 |
7.23e-07 |
|
3-beta hydroxysteroid dehydrogenase/isomerase family; The enzyme 3 beta-hydroxysteroid dehydrogenase/5-ene-4-ene isomerase (3 beta-HSD) catalyzes the oxidation and isomerization of 5-ene-3 beta-hydroxypregnene and 5-ene-hydroxyandrostene steroid precursors into the corresponding 4-ene-ketosteroids necessary for the formation of all classes of steroid hormones.
Pssm-ID: 366449 [Multi-domain] Cd Length: 279 Bit Score: 52.37 E-value: 7.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 975 VTGVTGFLGSYILADLLGRSPKNysfkvfaHVRAKDeeaafarlqkagITYGTWNEKFASN---IKVVLGDLSKSQFgls 1051
Cdd:pfam01073 2 VTGGGGFLGRHIIKLLVREGELK-------EVRVFD------------LRESPELLEDFSKsnvIKYIQGDVTDKDD--- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 1052 dekwMDLA-NTVDIIIHNGAL--VHWVYPYAKLRDPNVISTINVMSLAAVGKPKFFDFVSSTSTLDTEYYfnlsdklvse 1128
Cdd:pfam01073 60 ----LDNAlEGVDVVIHTASAvdVFGKYTFDEIMKVNVKGTQNVLEACVKAGVRVLVYTSSAEVVGPNSY---------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 1129 GKPgILESDDLMNSASGLTGGYGQSKWAAEYIIRRAGERGLRG------CIVRPGYVTGASangssntDDFLLRFLKGSV 1202
Cdd:pfam01073 126 GQP-ILNGDEETPYESTHQDAYPRSKAIAEKLVLKANGRPLKNggrlytCALRPAGIYGEG-------DRLLVPFIVNLA 197
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6319591 1203 QLG----KIPDIENSVNMVPVDHVA--RVVVATSLNPPKENELAVAQV----TGHPRILFKDYLYTL 1259
Cdd:pfam01073 198 KLGlakfKTGDDNNLSDRVYVGNVAwaHILAARALQDPKKMSSIAGNAyfiyDDTPVQSYDDFNRTL 264
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
271-708 |
7.75e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 53.46 E-value: 7.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 271 TYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFSVidpAYPPArqtiylgvakPRGLIVIRA 350
Cdd:PRK07768 31 TWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTM---LHQPT----------PRTDLAVWA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 351 AGQLDqlVEDYINDELEIVSRINSIAIQENGTiEGGKLDNGEDVLAPydhykDTRTGVVVGPDSNPTLSFTSGSEGIPKG 430
Cdd:PRK07768 98 EDTLR--VIGMIGAKAVVVGEPFLAAAPVLEE-KGIRVLTVADLLAA-----DPIDPVETGEDDLALMQLTSGSTGSPKA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 431 VLGRHFSLAYYFNWMSKRFNLTEnDKFTMLSGIahdPIQRDM------FTPLFLGAQLYVPTQDD-IGTPGRLAEWMSKY 503
Cdd:PRK07768 170 VQITHGNLYANAEAMFVAAEFDV-ETDVMVSWL---PLFHDMgmvgflTVPMYFGAELVKVTPMDfLRDPLLWAELISKY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 504 GCTVThLTPA-----MGQLLTAQATtpfpklHHAFfvgDILTKR---------DCLRLQTLAENCR--------IVNMYG 561
Cdd:PRK07768 246 RGTMT-AAPNfayalLARRLRRQAK------PGAF---DLSSLRfalngaepiDPADVEDLLDAGArfglrpeaILPAYG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 562 TTETQRAVSYFEVKS--KND--DPNFLKKLKDVMPAGKG-----------MLNVQLLVVNRNDrtQICGIGEIGEIYVRA 626
Cdd:PRK07768 316 MAEATLAVSFSPCGAglVVDevDADLLAALRRAVPATKGntrrlatlgppLPGLEVRVVDEDG--QVLPPRGVGVIELRG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 627 GGLAEGYrglpeLNKEKFVNnwFVEKDHWnyldkdngepwrqfwlgprdrlYRTGDLGRYLPNGDCECCGRADDqVKIRG 706
Cdd:PRK07768 394 ESVTPGY-----LTMDGFIP--AQDADGW----------------------LDTGDLGYLTEEGEVVVCGRVKD-VIIMA 443
|
..
gi 6319591 707 FR 708
Cdd:PRK07768 444 GR 445
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
417-822 |
9.58e-07 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 53.24 E-value: 9.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 417 TLSFTSGSEGIPKGVLGRHFSLAYYFNWMSKRF-NLTENDKFTMLS--GIAHDPIQrDMFTPLFLGAQLYV---PTQDdi 490
Cdd:cd05928 178 AIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWlDLTASDIMWNTSdtGWIKSAWS-SLFEPWIQGACVFVhhlPRFD-- 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 491 gtPGRLAEWMSKYGCTVTHLTPAMGQLLTAQATTP--FPKLHHAFFVGDILTKRDC--LRLQTLAEncrIVNMYGTTETQ 566
Cdd:cd05928 255 --PLVILKTLSSYPITTFCGAPTVYRMLVQQDLSSykFPSLQHCVTGGEPLNPEVLekWKAQTGLD---IYEGYGQTETG 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 567 RAVSYFevKSKNDDPNFLkklkdvmpaGKGML--NVQLLVVNRNdrtqICGIGEIGEIYVRAG-----GLAEGYRGLPEL 639
Cdd:cd05928 330 LICANF--KGMKIKPGSM---------GKASPpyDVQIIDDNGN----VLPPGTEGDIGIRVKpirpfGLFSGYVDNPEK 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 640 NKEKFVNNwfvekdhwnyldkdngepwrqFWLgprdrlyrTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHIS 719
Cdd:cd05928 395 TAATIRGD---------------------FYL--------TGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALI 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 720 QHPLVRENITLVRKNADNEPTLITFMVPRfdkpddlSKFQSDVPKEvetdpivkgligyhlLSKDIRTFLKKRLASYAMP 799
Cdd:cd05928 446 EHPAVVESAVVSSPDPIRGEVVKAFVVLA-------PQFLSHDPEQ---------------LTKELQQHVKSVTAPYKYP 503
|
410 420
....*....|....*....|...
gi 6319591 800 SLIVVMDKLPLNPNGKVDKPKLQ 822
Cdd:cd05928 504 RKVEFVQELPKTVTGKIQRNELR 526
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
555-850 |
1.88e-06 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 52.33 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 555 RIVNMYGTTETQRAVSYFEVKsknDDPNFLKKLKDV-MPAGKGMLNVQLLVVN-RNDRTQ--ICGIGE-IGEIYVRAGGL 629
Cdd:PLN03102 326 QVMHAYGLTEATGPVLFCEWQ---DEWNRLPENQQMeLKARQGVSILGLADVDvKNKETQesVPRDGKtMGEIVIKGSSI 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 630 AEGYRGLPELNKEKFVNNWFvekdhwnyldkdngepwrqfwlgprdrlyRTGDLGRYLPNGDCECCGRADDQVKIRGFRI 709
Cdd:PLN03102 403 MKGYLKNPKATSEAFKHGWL-----------------------------NTGDVGVIHPDGHVEIKDRSKDIIISGGENI 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 710 ELGEIDTHISQHPLVRENITLVRKNADNEPTLITFMVPRFDKPDDLSKFQSDVPKEvetdpivkgligyhllsKDIRTFL 789
Cdd:PLN03102 454 SSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETTKEDRVDKLVTRE-----------------RDLIEYC 516
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6319591 790 KKRLASYAMPSLIVVMDKLPLNPNGKVDKPKLQFptpkqlnlVAENTVSETDDSQFTNVER 850
Cdd:PLN03102 517 RENLPHFMCPRKVVFLQELPKNGNGKILKPKLRD--------IAKGLVVEDEDNVIKKVHQ 569
|
|
| C_PKS-NRPS |
cd20483 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
59-204 |
4.13e-06 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380471 [Multi-domain] Cd Length: 430 Bit Score: 51.11 E-value: 4.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 59 LSVWAALIYRVTGDDDIVLYIA-----------------NNKILRFNIQPTWSFNELYSTInnelnKLNSIEA----NFS 117
Cdd:cd20483 254 LAAFRAFLYRYTEDEDLTIGMVdgdrphpdfddlvgffvNMLPIRCRMDCDMSFDDLLEST-----KTTCLEAyehsAVP 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 118 FDELAEKIqscqDLERTPQLFRL-----------AFLE--NQDFKLDEFKHHLV----DFALN-LDTSNNAHVLNLIYNS 179
Cdd:cd20483 329 FDYIVDAL----DVPRSTSHFPIgqiavnyqvhgKFPEydTGDFKFTDYDHYDIptacDIALEaEEDPDGGLDLRLEFST 404
|
170 180
....*....|....*....|....*
gi 6319591 180 LLYSNERVTIVADQFTQYLTAALSD 204
Cdd:cd20483 405 TLYDSADMERFLDNFVTFLTSVIRD 429
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
678-741 |
6.57e-06 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 50.15 E-value: 6.57e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6319591 678 YRTGDLGRYLPnGDCEC----------CGRADDQVKIRGFRIELGEIDTHISQHPLVREN--ITLVRKNADNEPTL 741
Cdd:COG1541 297 YRTGDLTRLLP-EPCPCgrthprigriLGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEyqIVVDREGGLDELTV 371
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
421-822 |
1.45e-05 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 49.02 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 421 TSGSEGIPKGVLGRHFSLAYYfNWMSKRFNLTENDKfTMLSGI------AHDPIqrdMFTPLFLGAQLYVPTQDDIGTPG 494
Cdd:cd05944 10 TGGTTGTPKLAQHTHSNEVYN-AWMLALNSLFDPDD-VLLCGLplfhvnGSVVT---LLTPLASGAHVVLAGPAGYRNPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 495 RLAE-W--MSKYGCTVTHLTP-AMGQLLTAQATTPFPKLHHAFFVGDILTKRDCLRLQTlAENCRIVNMYGTTETQRAVS 570
Cdd:cd05944 85 LFDNfWklVERYRITSLSTVPtVYAALLQVPVNADISSLRFAMSGAAPLPVELRARFED-ATGLPVVEGYGLTEATCLVA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 571 YfevksknDDPNFLKKLKDV---MPAGKgmlnVQLLVVNRNDRTQI-CGIGEIGEIYVRAGGLAEGYrglpeLNKEKfvn 646
Cdd:cd05944 164 V-------NPPDGPKRPGSVglrLPYAR----VRIKVLDGVGRLLRdCAPDEVGEICVAGPGVFGGY-----LYTEG--- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 647 nwfvEKDHWnyldkdngepwrqfwlgPRDRLYRTGDLGRYLPNGDCECCGRADDQVkIR-GFRIELGEIDTHISQHPLVr 725
Cdd:cd05944 225 ----NKNAF-----------------VADGWLNTGDLGRLDADGYLFITGRAKDLI-IRgGHNIDPALIEEALLRHPAV- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 726 enitlvrknadneptliTFmVPRFDKPDdlsKFQSDVP-KEVETDPivkgliGYHLLSKDIRTFLKKRLASY-AMPSLIV 803
Cdd:cd05944 282 -----------------AF-AGAVGQPD---AHAGELPvAYVQLKP------GAVVEEEELLAWARDHVPERaAVPKHIE 334
|
410
....*....|....*....
gi 6319591 804 VMDKLPLNPNGKVDKPKLQ 822
Cdd:cd05944 335 VLEELPVTAVGKVFKPALR 353
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
777-815 |
1.95e-05 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 44.07 E-value: 1.95e-05
10 20 30
....*....|....*....|....*....|....*....
gi 6319591 777 GYHLLSKDIRTFLKKRLASYAMPSLIVVMDKLPLNPNGK 815
Cdd:pfam13193 38 GVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| YbjT |
COG0702 |
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ... |
972-1238 |
2.13e-05 |
|
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General function prediction only];
Pssm-ID: 440466 [Multi-domain] Cd Length: 215 Bit Score: 47.15 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 972 NVFVTGVTGFLGSYILADLLGRSpknysFKVFAHVRAKDEEAAFARLQkagitygtwnekfasnIKVVLGDLSKSQfgls 1051
Cdd:COG0702 1 KILVTGATGFIGRRVVRALLARG-----HPVRALVRDPEKAAALAAAG----------------VEVVQGDLDDPE---- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 1052 dekwmDLANT---VDIIIHngaLVHwVYPYAKLRDPnVISTINVMSLAAVGKPKFFDFVSSTSTldteyyfnlsdklvse 1128
Cdd:COG0702 56 -----SLAAAlagVDAVFL---LVP-SGPGGDFAVD-VEGARNLADAAKAAGVKRIVYLSALGA---------------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 1129 gkpgilesDDLMNSasgltgGYGQSKWAAEYIIRRAgerGLRGCIVRPGYVTGasangssntddFLLRFLKGSVQLGKI- 1207
Cdd:COG0702 110 --------DRDSPS------PYLRAKAAVEEALRAS---GLPYTILRPGWFMG-----------NLLGFFERLRERGVLp 161
|
250 260 270
....*....|....*....|....*....|..
gi 6319591 1208 -PDIENSVNMVPVDHVARVVVATSLNPPKENE 1238
Cdd:COG0702 162 lPAGDGRVQPIAVRDVAEAAAAALTDPGHAGR 193
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
247-433 |
6.03e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 47.38 E-value: 6.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 247 AEAFPERTCVVETPTlnsdkSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFSVIDP 326
Cdd:PRK13391 7 AQTTPDKPAVIMAST-----GEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 327 AYPPARQTIYLGVAKPRGLIVIRAAgqldqlvedyindeLEIVSRinsiAIQENGTIEGGKLDNGEDVLAPYDHYKDTRT 406
Cdd:PRK13391 82 HLTPAEAAYIVDDSGARALITSAAK--------------LDVARA----LLKQCPGVRHRLVLDGDGELEGFVGYAEAVA 143
|
170 180 190
....*....|....*....|....*....|.
gi 6319591 407 GVVVGP-DSNPT---LSFTSGSEGIPKGVLG 433
Cdd:PRK13391 144 GLPATPiADESLgtdMLYSSGTTGRPKGIKR 174
|
|
| UDP_invert_4-6DH_SDR_e |
cd05237 |
UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; ... |
966-1187 |
6.29e-05 |
|
UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; UDP-Glcnac inverting 4,6-dehydratase was identified in Helicobacter pylori as the hexameric flaA1 gene product (FlaA1). FlaA1 is hexameric, possesses UDP-GlcNAc-inverting 4,6-dehydratase activity, and catalyzes the first step in the creation of a pseudaminic acid derivative in protein glycosylation. Although this subgroup has the NADP-binding motif characteristic of extended SDRs, its members tend to have a Met substituted for the active site Tyr found in most SDR families. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187548 [Multi-domain] Cd Length: 287 Bit Score: 46.46 E-value: 6.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 966 EGKTtinVFVTGVTGFLGSYILADLLGRSPKnysfKVfaHVRAKDEEAAFARLQKAGITYGtwnekfASNIKVVLGDlsk 1045
Cdd:cd05237 1 KGKT---ILVTGGAGSIGSELVRQILKFGPK----KL--IVFDRDENKLHELVRELRSRFP------HDKLRFIIGD--- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 1046 sqfgLSDEKWMDLANT---VDIIIHNGALVHwV----YPYAKLRDPNVISTINVMSLAAVGKPKFFDFVSststldteyy 1118
Cdd:cd05237 63 ----VRDKERLRRAFKergPDIVFHAAALKH-VpsmeDNPEEAIKTNVLGTKNVIDAAIENGVEKFVCIS---------- 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6319591 1119 fnlSDKLVSegkPgilesddlmnsasglTGGYGQSKWAAEYIIRRAGERGLRG--CIVRPGYVTGasANGS 1187
Cdd:cd05237 128 ---TDKAVN---P---------------VNVMGATKRVAEKLLLAKNEYSSSTkfSTVRFGNVLG--SRGS 175
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
265-324 |
9.80e-05 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 46.79 E-value: 9.80e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 265 DKSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFSVI 324
Cdd:cd05966 80 DQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVV 139
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
617-817 |
1.71e-04 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 45.37 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 617 GEIGEIYVRAGGLAEGYRGLPELNKEKFVNNWfvekdhwnyldkdngepwrqfwlgprdrlYRTGDLGRYLPNGDCECCG 696
Cdd:cd17636 187 GEVGEIVARGPTVMAGYWNRPEVNARRTRGGW-----------------------------HHTNDLGRREPDGSLSFVG 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 697 RADDQVKIRGFRIELGEIDTHISQHPLVRenitlvrknadnEPTLITFMVPRFDkpddlskfQSdvpkevetdpiVKGLI 776
Cdd:cd17636 238 PKTRMIKSGAENIYPAEVERCLRQHPAVA------------DAAVIGVPDPRWA--------QS-----------VKAIV 286
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 6319591 777 ----GYHLLSKDIRTFLKKRLASYAMPSLIVVMDKLPLNPNGKVD 817
Cdd:cd17636 287 vlkpGASVTEAELIEHCRARIASYKKPKSVEFADALPRTAGGADD 331
|
|
| SDR_e_a |
cd05226 |
Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases ... |
973-1181 |
1.80e-04 |
|
Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases (SDRs, aka tyrosine-dependent oxidoreductases) are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187537 [Multi-domain] Cd Length: 176 Bit Score: 43.93 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 973 VFVTGVTGFLGSYILADLLGRspknySFKVFAHVRAKDEEAAFARLQKAgitygtwnekfasnikVVLGDLSKSQfGLSd 1052
Cdd:cd05226 1 ILILGATGFIGRALARELLEQ-----GHEVTLLVRNTKRLSKEDQEPVA----------------VVEGDLRDLD-SLS- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 1053 ekwmDLANTVDIIIHngaLVHWVYPYAKLRDPNVISTINVMSLAAVGKPKFFDFVSSTSTLDTEyyfnlsdklvsegkpg 1132
Cdd:cd05226 58 ----DAVQGVDVVIH---LAGAPRDTRDFCEVDVEGTRNVLEAAKEAGVKHFIFISSLGAYGDL---------------- 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6319591 1133 ILESDDLMNSAsgltggYGQSKWAAEYIIRRAGERGLrgcIVRPGYVTG 1181
Cdd:cd05226 115 HEETEPSPSSP------YLAVKAKTEAVLREASLPYT---IVRPGVIYG 154
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
590-708 |
2.26e-04 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 45.42 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 590 VMPAGKGMLNVQLLVVNrNDRTQICGIGEIGEIYVRAGGLAEGYRGLP-ELNKEKFVNNWFvekdhwNYLDKDNGEPWrq 668
Cdd:cd05905 360 LQDSGKVLPGAQVAIVN-PETKGLCKDGEIGEIWVNSPANASGYFLLDgETNDTFKVFPST------RLSTGITNNSY-- 430
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 6319591 669 fwlgprdrlYRTGDLGrYLPNGDCEC-----------CGRADDQVKIRGFR 708
Cdd:cd05905 431 ---------ARTGLLG-FLRPTKCTDlnveehdllfvVGSIDETLEVRGLR 471
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
57-205 |
5.44e-04 |
|
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380456 [Multi-domain] Cd Length: 419 Bit Score: 44.28 E-value: 5.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 57 VALSVWAALIYRVTGDDDIVL-----------------YIANNKILRFNIQPTWSFNELYSTINNELNKLNSiEANFSFD 119
Cdd:cd19533 245 FFIALVAAYLHRLTGANDVVLgvpvmgrlgaaarqtpgMVANTLPLRLTVDPQQTFAELVAQVSRELRSLLR-HQRYRYE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 120 ELAEKIQSCQDLER--TPQLFRLAFLENQDFKLDEFKHHLV------DFALNL--DTSNNAHVLNLIYNSLLYSNERVTI 189
Cdd:cd19533 324 DLRRDLGLTGELHPlfGPTVNYMPFDYGLDFGGVVGLTHNLssgptnDLSIFVydRDDESGLRIDFDANPALYSGEDLAR 403
|
170
....*....|....*.
gi 6319591 190 VADQFTQYLTAALSDP 205
Cdd:cd19533 404 HQERLLRLLEEAAADP 419
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
268-350 |
1.33e-03 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 42.73 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 268 RSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFSVIDPAYPPARQTIYLGVAKPRGLIV 347
Cdd:cd05940 2 EALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVV 81
|
...
gi 6319591 348 IRA 350
Cdd:cd05940 82 DAA 84
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
270-726 |
1.51e-03 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 42.55 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 270 FTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGAtfsvidpaypparqtiylgvakprglIVIR 349
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGA--------------------------VVIP 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 350 AAgqlDQLVEDYINDELEIVSRInsIAIQENGTieggkldNGEDVLAPYdhykdtrtgvvvgpdsnptlsFTSGSEGIPK 429
Cdd:cd05974 55 AT---TLLTPDDLRDRVDRGGAV--YAAVDENT-------HADDPMLLY---------------------FTSGTTSKPK 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 430 GVLGRHFSlaYYFNWMSKRF--NLTENDKFTMLS--GIAHDPIQrDMFTPLFLGAQLYVPTQDDIgTPGRLAEWMSKYGC 505
Cdd:cd05974 102 LVEHTHRS--YPVGHLSTMYwiGLKPGDVHWNISspGWAKHAWS-CFFAPWNAGATVFLFNYARF-DAKRVLAALVRYGV 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 506 TVTHLTPAMGQLLTAQATTPFP-KLHHAFFVGDILTKRDCLRLQTlAENCRIVNMYGTTETQRAVSyfevksknDDPNfl 584
Cdd:cd05974 178 TTLCAPPTVWRMLIQQDLASFDvKLREVVGAGEPLNPEVIEQVRR-AWGLTIRDGYGQTETTALVG--------NSPG-- 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 585 kklKDVMPAGKGM----LNVQLLVVNRNDRTQicgigeiGEIYV-----RAGGLAEGYRGLPELNKEKFvnnwfvekdhw 655
Cdd:cd05974 247 ---QPVKAGSMGRplpgYRVALLDPDGAPATE-------GEVALdlgdtRPVGLMKGYAGDPDKTAHAM----------- 305
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6319591 656 nyldkdngepwrqfwlgpRDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRE 726
Cdd:cd05974 306 ------------------RGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAE 358
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
412-483 |
1.59e-03 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 42.78 E-value: 1.59e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6319591 412 PDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFNWMSKRFNLTENDKFTMLSGIAHD-PIQRDMFTPLFLGAQLY 483
Cdd:PRK08043 364 PEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSfGLTVGLFTPLLTGAEVF 436
|
|
| AR_like_SDR_e |
cd05193 |
aldehyde reductase, flavonoid reductase, and related proteins, extended (e) SDRs; This ... |
973-1183 |
1.68e-03 |
|
aldehyde reductase, flavonoid reductase, and related proteins, extended (e) SDRs; This subgroup contains aldehyde reductase and flavonoid reductase of the extended SDR-type and related proteins. Proteins in this subgroup have a complete SDR-type active site tetrad and a close match to the canonical extended SDR NADP-binding motif. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. The related flavonoid reductases act in the NADP-dependent reduction of flavonoids, ketone-containing plant secondary metabolites. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187536 [Multi-domain] Cd Length: 295 Bit Score: 42.22 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 973 VFVTGVTGFLGSYILADLLGRspknySFKVFAHVRAKDeeaafaRLQKAGITyGTWNEKfasnikvvLGDLSKSQFGLSD 1052
Cdd:cd05193 1 VLVTGASGFVASHVVEQLLER-----GYKVRATVRDPS------KVKKVNHL-LDLDAK--------PGRLELAVADLTD 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 1053 EKWMDLA-NTVDIIIHNGALVH-WVYPYAKLRDPNVISTINVM-SLAAVGKPKFFDFVSSTSTLDTEYYFNlsDKLVSEG 1129
Cdd:cd05193 61 EQSFDEViKGCAGVFHVATPVSfSSKDPNEVIKPAIGGTLNALkAAAAAKSVKRFVLTSSAGSVLIPKPNV--EGIVLDE 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6319591 1130 KPGILESDDlmNSASGLTGGYGQSKWAAEYI-IRRAGERGLRGCIVRPGYVTGAS 1183
Cdd:cd05193 139 KSWNLEEFD--SDPKKSAWVYAASKTLAEKAaWKFADENNIDLITVIPTLTIGTI 191
|
|
| CDP_TE_SDR_e |
cd05258 |
CDP-tyvelose 2-epimerase, extended (e) SDRs; CDP-tyvelose 2-epimerase is a tetrameric SDR that ... |
973-1187 |
2.08e-03 |
|
CDP-tyvelose 2-epimerase, extended (e) SDRs; CDP-tyvelose 2-epimerase is a tetrameric SDR that catalyzes the conversion of CDP-D-paratose to CDP-D-tyvelose, the last step in tyvelose biosynthesis. This subgroup is a member of the extended SDR subfamily, with a characteristic active site tetrad and NAD-binding motif. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187568 [Multi-domain] Cd Length: 337 Bit Score: 41.89 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 973 VFVTGVTGFLGSYiLADLLGRspKNYSFKVFAHVRAKDEEAAFARLQKAGITygtwnekfaSNIKVVLGDLSKSQfglsd 1052
Cdd:cd05258 3 VLITGGAGFIGSN-LARFFLK--QGWEVIGFDNLMRRGSFGNLAWLKANRED---------GGVRFVHGDIRNRN----- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 1053 ekwmDLANTV---DIIIHNGA--LVHWVYpyaklRDP------NVISTINVMSLAAVGKPKFFDFVSSTSTL--DTEYYF 1119
Cdd:cd05258 66 ----DLEDLFediDLIIHTAAqpSVTTSA-----SSPrldfetNALGTLNVLEAARQHAPNAPFIFTSTNKVygDLPNYL 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6319591 1120 NLSD-------KLVSEGKPGILESDDLMNSASgltgGYGQSKWAAEYIIRRAGER-GLRGCIVRPGYVTGASANGS 1187
Cdd:cd05258 137 PLEEletryelAPEGWSPAGISESFPLDFSHS----LYGASKGAADQYVQEYGRIfGLKTVVFRCGCLTGPRQFGT 208
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
617-706 |
2.26e-03 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 42.42 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319591 617 GEIGEIYVRAGGLAEGYRGLPELNKEKFVNNWFVEKDHWNYLDkdnGEPWRQFWLgprdrlyRTGDLGRYLpNGDCECCG 696
Cdd:PRK12476 427 GEVGEIWLHGDNIGRGYWGRPEETERTFGAKLQSRLAEGSHAD---GAADDGTWL-------RTGDLGVYL-DGELYITG 495
|
90
....*....|
gi 6319591 697 RADDQVKIRG 706
Cdd:PRK12476 496 RIADLIVIDG 505
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
781-821 |
3.07e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 41.81 E-value: 3.07e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 6319591 781 LSKDIRTFLKKRLASYAMPSLIVVMDKLPLNPNGKVDKPKL 821
Cdd:PRK08276 450 LAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRL 490
|
|
| |
