|
Name |
Accession |
Description |
Interval |
E-value |
| PabB-fungal |
TIGR01823 |
aminodeoxychorismate synthase, fungal clade; This model represents the fungal clade of a ... |
3-708 |
0e+00 |
|
aminodeoxychorismate synthase, fungal clade; This model represents the fungal clade of a para-aminobenzoate synthesis enzyme, aminodeoxychorismate synthase, which acts on chorismate in a pathway that yields PABA, a precursor of folate.
Pssm-ID: 273821 [Multi-domain] Cd Length: 742 Bit Score: 1207.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 3 EISNRLQILLIDCYDSYTFNLYDLLYKASEN-ACVIVVHWDKMSPDLWEDILQFDAIVVGPGPGHP--AEYSSILNRIWQ 79
Cdd:TIGR01823 1 QQQQRLHVLFIDSYDSFTYNVVRLLEQQTDIsVHVTTVHSDTFQDQLLELLPLFDAIVVGPGPGNPnnAQDMGIISELWE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 80 LN----IPVMGICLGFQSLALYHGATIERMPnLPWHGRVSSVTTSKTFIFDGISAVKGMRYHSLYANKIPIDSL--QILA 153
Cdd:TIGR01823 81 LAnldeVPVLGICLGFQSLCLAQGADISRLP-TPKHGQVYEMHTNDAAIFCGLFSVKSTRYHSLYANPEGIDTLlpLCLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 154 QSDEDNIVMSIKATKFPHFGILYHPESVGSSK-SLKIFKNFLSLADTPNIQCVNS----FSKSANGFSHNLNRYDISPAA 228
Cdd:TIGR01823 160 EDEEGIILMSAQTKKKPWFGVQYHPESCCSELgSGKLVSNFLKLAFINNVKTGRWekkkLNGSFSDISSRLDRTDDRDPI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 229 FILKSGSPS-LQIHSVEIPWVEPLALADCIQKSGNPICFLDSAKKPGRYSILGILTG----------PLARIIHYEKATN 297
Cdd:TIGR01823 240 YKVKEKYPSgTTYVKQFEVSEDPKLTFEICNIIREPKFVMSSSVITGRYSIIALPNSasqvfthygaMLKTTVHYWQDTE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 298 TTEIRICKDNSFVR---INNDLWSTVADFMNQHKAIKPDTNLPFYGGIMGIIGYEC-SDLSTKSVSNASFPLDFQQTTVD 373
Cdd:TIGR01823 320 ISYTRLKKCLSGVDsdlDKSQFWITLGKFMENKKIDNPHREIPFIGGLVGILGYEIgSDLSTQYIACGRCNDDENSLVPD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 374 AELAFVDRSFVFDLEIKKLFVQTLTPLNETCSEWWGELLASTCNTKLDNLSCLHSFDGKQNFGLVQSFPKKEVYCESVKA 453
Cdd:TIGR01823 400 AKLVFINRSIVIDHKQGKLYVQSLDNTFPVALEWSGELRDSFVRKKNIKQSLSWPFYLPEEIDFVITFPDKEDYAKAFKA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 454 CQEHLLAGDSYEMCLTDTTFVSAPPELS-DFEMYMRARSLNPATFAGFVRLNHFTLLCCSPERFLQF-RDDRCLFSPIKG 531
Cdd:TIGR01823 480 CQDYLHAGDSYEMCLTTQTKVVPPAVISpDWEIYQRLRQRNPAPFSGFFRLKHIIFLSTSPEKFLEVgMDTHAKLRPIKG 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 532 TLKREGHMSLEEARKKLLNEKDMGELNMIIDLIRNDLHQLAKKNSVHVPELYSVEEHSNVYSLLSNIYGRIESPIT---- 607
Cdd:TIGR01823 560 TVKKGPQMNLEKARRILKTPKEMGENLMILDLIRNDLYELVPKNDVHVEELMSVEEHATVYQLVSVVKAHGLTSASkktr 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 608 --AWDVLSKSFPPGSMTGAPKLRSVRMLEPLEQHGRGIYSGTLGYWDVTGSAEFNVIIRSAFKYKADDYWRIGAGGAVTI 685
Cdd:TIGR01823 640 ysGIDVLKHSLPPGSMTGAPKKRSVQLLQDVEGGARGIYSGVTGYWDVNGNGDFSVNIRCAFSYNGGTSWRIGAGGAVTV 719
|
730 740
....*....|....*....|...
gi 19113328 686 LSSPEGEYEEMVLKANSILPAFV 708
Cdd:TIGR01823 720 LSTPEGELEEMYNKLESNLQIFM 742
|
|
| PLN02889 |
PLN02889 |
oxo-acid-lyase/anthranilate synthase |
1-716 |
3.86e-99 |
|
oxo-acid-lyase/anthranilate synthase
Pssm-ID: 215481 [Multi-domain] Cd Length: 918 Bit Score: 326.03 E-value: 3.86e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 1 MSEISNRLQI---LLIDCYDSYTFNLYDLLYKASENACVIVVH----WDKMSPDLWEDIlQFDAIVVGPGPGHPAEYSSI 73
Cdd:PLN02889 72 LEEPSQKLEFvrtLLIDNYDSYTYNIYQELSIVNGVPPVVVRNdewtWEEVYHYLYEEK-AFDNIVISPGPGSPTCPADI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 74 ---LNRIWQL-NIPVMGICLGFQSLALYHGATIERMPNlPWHGRVSSVTTSKTFIFDGI-----SAVKGMRYHSLYANK- 143
Cdd:PLN02889 151 gicLRLLLECrDIPILGVCLGHQALGYVHGARIVHAPE-PVHGRLSEIEHNGCRLFDDIpsgrnSGFKVVRYHSLVIDAe 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 144 ------IPI------DSLQILAQSDED----------------------------------------NIVMSIKATKFPH 171
Cdd:PLN02889 230 slpkelVPIawtsssDTLSFLESQKSGlvpdayesqigqsgssdpfssklkngtswpsshsermqngKILMGIMHSTRPH 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 172 FGILYHPESVGSSKSLKIFKNFLSLA------------------DTPNIQC--------VNSFSKSANGFSHNLNRYDIS 225
Cdd:PLN02889 310 YGLQFHPESIATCYGRQIFKNFREITqdywlrlrstslrrrnsnLTANMQVpdasqlfkVPRRGQLGNGEDALGNRELSR 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 226 PAAF--------ILKSGSPSLQIHSVEIPWVEPLALADCIQKSGNPIC------------FLDSA---KKPGRYSILGIL 282
Cdd:PLN02889 390 RAQLrgsvdvfsLLNLSEPSSGVKFLKLKWRKFNKLAAQVGGARNIFCelfgknkaentfWLDSSsteKKRGRFSFMGGK 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 283 TGPLARIIHYeKATNTTEIrICKDNSFVRINNDLWSTVA--------DFMNQH-KAIKPDTN----LPF--YGGIMGIIG 347
Cdd:PLN02889 470 GGSLWKQMTF-RLSHQSDM-DSKGGGHLSIEDSQGSIEStflekgflDFLNKElLSIRYDEKdfegLPFdfHGGYVGYIG 547
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 348 Y----ECSDLSTKSVSNasfpldfqqtTVDAELAFVDRSFVFDLEIKKLFVQTLTPLNETCSEWWGE-------LLASTC 416
Cdd:PLN02889 548 YdlkvECGMASNRHKST----------TPDACFFFADNVVVIDHHYDDVYILSLHEGSTATTQWLDDteqkllgLKASAT 617
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 417 NTKLDNLSCLHSFD-GKQNFglvqsFPKK--EVYCESVKACQEHLLAGDSYEMCLTdTTFVSAPPELSDFEMYMRARSLN 493
Cdd:PLN02889 618 RKLEVQTSPTATFSpSKAGF-----LADKsrEQYIKDVQKCLKYIKDGESYELCLT-TQMRKRIGEIDSLGLYLHLREKN 691
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 494 PATFAGFVRLNHFTL-LCCS-PERFLQFRDDRCLFS-PIKGTLKReGHMSLEEARKKL---LNEKDMGELNMIIDLIRND 567
Cdd:PLN02889 692 PAPYAAWLNFSNENLcICSSsPERFLKLDRNGMLEAkPIKGTIAR-GSTPEEDEQLKLqlqYSEKDQAENLMIVDLLRND 770
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 568 LHQLAKKNSVHVPELYSVEEHSNVYSLLSNIYGRIESPITAWDVLSKSFPPGSMTGAPKLRSVRMLEPLEQHGRGIYSGT 647
Cdd:PLN02889 771 LGRVCEPGSVHVPNLMDVESYTTVHTMVSTIRGKKRSNMSPVDCVRAAFPGGSMTGAPKLRSMELLDSLESSSRGIYSGS 850
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19113328 648 LGYWDVTGSAEFNVIIRSAFKYkaDDYWRIGAGGAVTILSSPEGEYEEMVLKANSILPAFVNLKNKKRS 716
Cdd:PLN02889 851 IGFFSYNQTFDLNIVIRTVVIH--EGEASIGAGGAIVALSNPEDEYEEMILKTRAPANAVIEFQKDQRS 917
|
|
| Chorismate_bind |
pfam00425 |
chorismate binding enzyme; This family includes the catalytic regions of the chorismate ... |
445-699 |
1.05e-96 |
|
chorismate binding enzyme; This family includes the catalytic regions of the chorismate binding enzymes anthranilate synthase, isochorismate synthase, aminodeoxychorismate synthase and para-aminobenzoate synthase.
Pssm-ID: 425674 [Multi-domain] Cd Length: 255 Bit Score: 299.08 E-value: 1.05e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 445 EVYCESVKACQEHLLAGDSYEMCLTDTTFVSAPPELSDFEMYMRARSLNPATFAGFVRLNHFTLLCCSPERFLQFRDDRC 524
Cdd:pfam00425 1 EDYLAAVEKAKEAIRAGDLYKVVLSRRLTLPLAGDIDPLALYRRLRARNPAPYSFYFRTGDFTFLGASPERLLSVDGGRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 525 LFSPIKGTLKREGHMSLEEARKK--LLNEKDMGELNMIIDLIRNDLHQLAKKNSVHVPELYSVEEHSNVYSLLSNIYGRI 602
Cdd:pfam00425 81 ITEPIAGTRPRGKDPAEDEALAAelLADPKERAEHLMVVDLIRNDLGRVCVPGSVKVPELPEVERYGTVQHLVSTISGRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 603 ESPITAWDVLSKSFPPGSMTGAPKLRSVRMLEPLEQHGRGIYSGTLGYWDVTGSAEFNVIIRSAFkyKADDYWRIGAGGA 682
Cdd:pfam00425 161 KPGLSLLDLLKALFPTGAVTGAPKKRAMEIIRELEPFPRGLYAGAVGYLDPDGDADFAVAIRTAL--VDNGRARLYAGAG 238
|
250
....*....|....*..
gi 19113328 683 VTILSSPEGEYEEMVLK 699
Cdd:pfam00425 239 IVADSDPEAEWEETEAK 255
|
|
| TrpE |
COG0147 |
Anthranilate/para-aminobenzoate synthases component I [Amino acid transport and metabolism, ... |
241-706 |
1.01e-94 |
|
Anthranilate/para-aminobenzoate synthases component I [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Anthranilate/para-aminobenzoate synthases component I is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 439917 [Multi-domain] Cd Length: 416 Bit Score: 299.71 E-value: 1.01e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 241 HSVEIPWVE-PLALADCIQKSGNPIcFLDSA---KKPGRYSILGIltGPLARIIhyekaTNTTEIRICKDNSFVRINNDL 316
Cdd:COG0147 5 VYRELLALEtPVSLFLKLADGPYAF-LLESAeggEKWGRYSFIGA--DPLATLT-----VRGGRVTIEGGGEVEPSEGDP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 317 WSTVADFMNQHKAIKPDTNLPFYGGIMGIIGYE----CSDLSTKSVSNASFPldfqqttvDAELAFVDRSFVFDleikkl 392
Cdd:COG0147 77 LDALRALLARFRLPPLPGLPPFTGGLVGYFGYDlvryFERLPDLAPDDLGLP--------DAALGLYDRLLVFD------ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 393 fvqtltplnetcsewwgellastcntkldnlsclHsFDGKQ-NFGlvqsfpkKEVYCESVKACQEHLLAGDSYEMCLTDT 471
Cdd:COG0147 143 ----------------------------------H-LKGTRsNFT-------REEYLAAVERAKEYIRAGDIFQVVLSQR 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 472 tfVSAPPELSDFEMYMRARSLNPATFAGFVRLNHFTLLCCSPERFLQFRDDRCLFSPIKGTLKReGHMSLEEAR--KKLL 549
Cdd:COG0147 181 --FSAPFEGDPLALYRALRRINPSPYMFYLRFGDFAIVGSSPERLVRVEDGRVETRPIAGTRPR-GATPEEDAAlaEELL 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 550 N-EKDMGELNMIIDLIRNDLHQLAKKNSVHVPELYSVEEHSNVYSLLSNIYGRIESPITAWDVLSKSFPPGSMTGAPKLR 628
Cdd:COG0147 258 AdEKERAEHLMLVDLARNDLGRVCEPGSVKVPELMVVERYSHVMHLVSTVTGRLRPGLDALDALRATFPAGTLTGAPKIR 337
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19113328 629 SVRMLEPLEQHGRGIYSGTLGYWDVTGSAEFNVIIRSAFKYkaDDYWRIGAGGAVTILSSPEGEYEEMVLKANSILPA 706
Cdd:COG0147 338 AMEIIDELEPTRRGVYGGAVGYLSFDGNMDLAIAIRTAVVK--DGRAYVQAGAGIVADSDPEAEYQETLNKARALLRA 413
|
|
| GATase1_Anthranilate_Synthase |
cd01743 |
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ... |
10-194 |
2.79e-68 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase (ASase). This group contains proteins similar to para-aminobenzoate (PABA) synthase and ASase. These enzymes catalyze similar reactions and produce similar products, PABA and ortho-aminobenzoate (anthranilate). Each enzyme is composed of non-identical subunits: a glutamine amidotransferase subunit (component II) and a subunit that produces an aminobenzoate products (component I). ASase catalyses the synthesis of anthranilate from chorismate and glutamine and is a tetrameric protein comprising two copies each of components I and II. Component II of ASase belongs to the family of triad GTases which hydrolyze glutamine and transfer nascent ammonia between the active sites. In some bacteria, such as Escherichia coli, component II can be much larger than in other organisms, due to the presence of phosphoribosyl-anthranilate transferase (PRTase) activity. PRTase catalyses the second step in tryptophan biosynthesis and results in the addition of 5-phosphoribosyl-1-pyrophosphate to anthranilate to create N-5'-phosphoribosyl-anthranilate. In E.coli, the first step in the conversion of chorismate to PABA involves two proteins: PabA and PabB which co-operate to transfer the amide nitrogen of glutamine to chorismate forming 4-amino-4 deoxychorismate (ADC). PabA acts as a glutamine amidotransferase, supplying an amino group to PabB, which carries out the amination reaction. A third protein PabC then mediates elimination of pyruvate and aromatization to give PABA. Several organisms have bipartite proteins containing fused domains homologous to PabA and PabB commonly called PABA synthases. These hybrid PABA synthases may produce ADC and not PABA.
Pssm-ID: 153214 [Multi-domain] Cd Length: 184 Bit Score: 222.02 E-value: 2.79e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 10 ILLIDCYDSYTFNLYDLLykASENACVIVVHWDKMSPDLwEDILQFDAIVVGPGPGHPAEYS---SILNRIWQlNIPVMG 86
Cdd:cd01743 1 ILLIDNYDSFTYNLVQYL--RELGAEVVVVRNDEITLEE-LELLNPDAIVISPGPGHPEDAGislEIIRALAG-KVPILG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 87 ICLGFQSLALYHGATIERMPNlPWHGRVSSVTTSKTFIFDGI-SAVKGMRYHSLYANKIPIDSLQILAQSDEDNIVMSIK 165
Cdd:cd01743 77 VCLGHQAIAEAFGGKVVRAPE-PMHGKTSEIHHDGSGLFKGLpQPFTVGRYHSLVVDPDPLPDLLEVTASTEDGVIMALR 155
|
170 180
....*....|....*....|....*....
gi 19113328 166 ATKFPHFGILYHPESVGSSKSLKIFKNFL 194
Cdd:cd01743 156 HRDLPIYGVQFHPESILTEYGLRLLENFL 184
|
|
| pabB |
TIGR00553 |
aminodeoxychorismate synthase, component I, bacterial clade; Members of this family, ... |
447-703 |
2.09e-60 |
|
aminodeoxychorismate synthase, component I, bacterial clade; Members of this family, aminodeoxychorismate synthase, component I (PabB), were designated para-aminobenzoate synthase component I until it was recognized that PabC, a lyase, completes the pathway of PABA synthesis. This family is closely related to anthranilate synthase component I (trpE), and both act on chorismate. The clade of PabB enzymes represented by this model includes sequences from Gram-positive and alpha and gamma Proteobacteria as well as Chlorobium, Nostoc, Fusobacterium and Arabidopsis. A closely related clade of fungal PabB enzymes is identified by TIGR01823, while another bacterial clade of potential PabB enzymes is more closely related to TrpE (TIGR01824). [Biosynthesis of cofactors, prosthetic groups, and carriers, Folic acid]
Pssm-ID: 273133 Cd Length: 328 Bit Score: 206.08 E-value: 2.09e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 447 YCESVKACQEHLLAGDSYEMCLTdtTFVSAPPELSDFEMYMRARSLNPATFAGFVRLNHFTLLCCSPERFLQFRDDRCLF 526
Cdd:TIGR00553 74 YGEAIDQLQDYIRAGDCYQANLT--QQFHATWDGDPLAAFRKLRRRQPAPFSAFLDLGDGAILSLSPELFFSIDGSEIET 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 527 SPIKGTLKR--EGHMSLEEARKKLLNEKDMGELNMIIDLIRNDLHQLAKKNSVHVPELYSVEEHSNVYSLLSNIYGRIES 604
Cdd:TIGR00553 152 RPIKGTLPRgaDPQEDRAQASALAESAKDRAENLMIVDLLRNDLGRIAEVGSVKVPELFVVETYPTVHQLVSTITARLRE 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 605 PITAWDVLSKSFPPGSMTGAPKLRSVRMLEPLEQHGRGIYSGTLGYWDVTGSAEFNVIIRSAfkyKADD-YWRIGAGGAV 683
Cdd:TIGR00553 232 DLTLSDLFRALFPGGSITGAPKVRAMEIIDELEPQPRGVYCGAIGYLSPEGDMDFNVAIRTL---TLDGgRAVYGVGGGI 308
|
250 260
....*....|....*....|
gi 19113328 684 TILSSPEGEYEEMVLKANSI 703
Cdd:TIGR00553 309 VADSDPEAEYRECLLKAAPL 328
|
|
| PabA |
COG0512 |
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ... |
10-197 |
9.18e-56 |
|
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440278 [Multi-domain] Cd Length: 189 Bit Score: 188.71 E-value: 9.18e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 10 ILLIDCYDSYTFNLYDLLYKASENacVIVVHWDKMSpdlWEDI--LQFDAIVVGPGPGHPAEYSSILNRIWQL--NIPVM 85
Cdd:COG0512 1 ILLIDNYDSFTYNLVQYLGELGAE--VVVVRNDEIT---LEEIeaLAPDGIVLSPGPGTPEEAGISLEVIRAFagKIPIL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 86 GICLGFQSLALYHGATIERMPNlPWHGRVSSVTTSKTFIFDGI-SAVKGMRYHSLYANKIPI-DSLQILAQSdEDNIVMS 163
Cdd:COG0512 76 GVCLGHQAIGEAFGGKVVRAPE-PMHGKTSPITHDGSGLFAGLpNPFTATRYHSLVVDRETLpDELEVTAWT-EDGEIMG 153
|
170 180 190
....*....|....*....|....*....|....
gi 19113328 164 IKATKFPHFGILYHPESVGSSKSLKIFKNFLSLA 197
Cdd:COG0512 154 IRHRELPIEGVQFHPESILTEHGHQLLANFLELA 187
|
|
| PabB-clade2 |
TIGR01824 |
aminodeoxychorismate synthase, component I, clade 2; This clade of sequences is more closely ... |
447-700 |
1.86e-53 |
|
aminodeoxychorismate synthase, component I, clade 2; This clade of sequences is more closely related to TrpE (anthranilate synthase, TIGR00564/TIGR01820/TIGR00565) than to the better characterized group of PabB enzymes (TIGR00553/TIGR01823). This clade includes one characterized enzyme from Lactococcus and the conserved function across the clade is supported by these pieces of evidence: 1) all genomes with a member in this clade also have a separate TrpE gene, 2) none of these genomes contain an aparrent PabB from any of the other PabB clades, 3) none of these sequences are found in a region of the genome in association with other Trp biosynthesis genes, 4) all of these genomes aparrently contain most if not all of the steps of the folate biosynthetic pathway (for which PABA is a precursor). Many of the sequences hit by this model are annotated as TrpE enzymes, however, we believe that all members of this clade are, in fact, PabB. The sequences from Bacillus halodurans and subtilus which score below the trusted cutoff for this model are also likely to be PabB enzymes, but are too closely related to TrpE to be separated at this time.
Pssm-ID: 130883 Cd Length: 355 Bit Score: 188.06 E-value: 1.86e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 447 YCESVKACQEHLLAGDSYEMCLTDTTFVSAPPELSDFEMYMRARSLNPATFAGFVRLNHFTLLCCSPERFLQFRDDRCLF 526
Cdd:TIGR01824 99 YETGVRRIKDYIRAGDVFQANLSRRLTAPIAADVDPLQLFLALRAPNPAPYAIYLEEPGVDVASASPELFLAREGRVVQT 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 527 SPIKGTLKREGHMSLEEARKKLL--NEKDMGELNMIIDLIRNDLHQLAKKNSVHVPELYSVEEHSNVYSLLSNIYGRIES 604
Cdd:TIGR01824 179 RPIAGTRPRGATLAEDGALAAELlqHDKDRAEHVMIVDLERNDLGRVCATGTVRVPELCAVESYSHVHHLVSRVTGRLRE 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 605 PITAWDVLSKSFPPGSMTGAPKLRSVRMLEPLEQHGRGIYSGTLGYWDVTGSAEFNVIIRSAFKYKADDYWRIGAGgaVT 684
Cdd:TIGR01824 259 GAGLADLIRALFPGGSITGAPKVRAMEIIDELEPQPRGPYTGSVGWIDADGNADLNILIRTLEGGGAQLHFRTGAG--IV 336
|
250
....*....|....*.
gi 19113328 685 ILSSPEGEYEEMVLKA 700
Cdd:TIGR01824 337 ADSDPAGEWDETEAKA 352
|
|
| PRK05877 |
PRK05877 |
aminodeoxychorismate synthase component I; Provisional |
403-704 |
4.36e-50 |
|
aminodeoxychorismate synthase component I; Provisional
Pssm-ID: 235634 [Multi-domain] Cd Length: 405 Bit Score: 180.28 E-value: 4.36e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 403 TCSEWWGELLASTCNTKLDNLSClhsfdgkqnfglVQSFPKKEVYCESVKACQEHLLAGDSYEMCLT---DTTFVSAPPE 479
Cdd:PRK05877 112 PDPDWLASALATTRARPAPPCRI------------DWTPPDRAAHRDGVLACLEAIAAGEVYQACVCtqfTGTVTGSPLD 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 480 LsdfeMYMRARSLNPATfAGFVRLNHFTLLCCSPERFLQFRDDRCLFSPIKGTLKREGHMSLEEArkkllNEKDMGELNM 559
Cdd:PRK05877 180 F----FADGVARTAPAR-AAYLAGDWGAVASLSPELFLRRRGSVVTSSPIKGTLPLDADPSALRA-----SAKDVAENIM 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 560 IIDLIRNDLHQLAKKNSVHVPELYSVEEHSNVYSLLSNIYGRIESPITAWDVLSKSFPPGSMTGAPKLRSVRMLEPLEQH 639
Cdd:PRK05877 250 IVDLVRNDLGRVARTGTVTVPELLVVRPAPGVWHLVSTVSAQVPDELPMSDLLDATFPPASVTGTPKLRARELISQWEPV 329
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19113328 640 GRGIYSGTLGY-WDVTGsAEFNVIIRSaFKYKADDYWRIGAGGAVTILSSPEGEYEEMVLKANSIL 704
Cdd:PRK05877 330 RRGIYCGTVGLaSPVAG-CELNVAIRT-VEFDADGNAVLGVGGGITADSDPDAEWQECLHKAAPIV 393
|
|
| pabB |
PRK15465 |
aminodeoxychorismate synthase component 1; |
296-704 |
4.79e-47 |
|
aminodeoxychorismate synthase component 1;
Pssm-ID: 185362 [Multi-domain] Cd Length: 453 Bit Score: 173.18 E-value: 4.79e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 296 TNTTEIRICKDNSFVRINND---LWSTVADFMNQHKAikPDTNLPFYGGIMGIIGYecsDLSTKSvsnASFPLDFQQTTV 372
Cdd:PRK15465 59 TFGKETVVSESEKRTTTTDDplqVLQQVLDRADIRPT--HNEDLPFQGGALGLFGY---DLGRRF---ESLPEIAEQDIV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 373 DAELA--FVDRSFVFDLEikklfVQTLTPLNETcsewwgellasTCNTKLDNLSCLHsFDGKQNFGLV---QSFPKKEVY 447
Cdd:PRK15465 131 LPDMAvgIYDWALIVDHQ-----RQTVSLLSHN-----------DVNARRAWLESQQ-FSPQEDFTLTsdwQSNMTREQY 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 448 CESVKACQEHLLAGDSYEMCLTDTtfVSAPPELSDFEMYMRARSLNPATFAGFVRLNHFTLLCCSPERFLQFRDDRCLFS 527
Cdd:PRK15465 194 GEKFRQVQEYLHSGDCYQVNLAQR--FHATYSGDEWQAFLQLNQANRAPFSAFLRLEQGAILSLSPERFILCDNSEIQTR 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 528 PIKGTLKR--EGHMSLEEARKKLLNEKDMGELNMIIDLIRNDLHQLAKKNSVHVPELYSVEEHSNVYSLLSNIYGRIESP 605
Cdd:PRK15465 272 PIKGTLPRlpDPQEDSKQAEKLANSAKDRAENLMIVDLMRNDIGRVAVAGSVKVPELFVVEPFPAVHHLVSTITARLPEQ 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 606 ITAWDVLSKSFPPGSMTGAPKLRSVRMLEPLEQHGRGIYSGTLGYWDVTGSAEFNVIIRSAFKYKADDYwrIGAGGAVTI 685
Cdd:PRK15465 352 LHASDLLRAAFPGGSITGAPKVRAMEIIDELEPQRRNAWCGSIGYLSFCGNMDTSITIRTLTAINGQIY--CSAGGGIVA 429
|
410
....*....|....*....
gi 19113328 686 LSSPEGEYEEMVLKANSIL 704
Cdd:PRK15465 430 DSQEEAEYQETFDKVNRIL 448
|
|
| PRK07508 |
PRK07508 |
aminodeoxychorismate synthase component I; |
447-700 |
3.34e-43 |
|
aminodeoxychorismate synthase component I;
Pssm-ID: 236035 [Multi-domain] Cd Length: 378 Bit Score: 160.56 E-value: 3.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 447 YCESVKACQEHLLAGDSYEMCLT---DTTFVSAPPELsdfemYMRARSLNPATFAGFVRLNHFTLLCCSPERFLQfRDDR 523
Cdd:PRK07508 114 YAQRFERLHRHIRAGDCYQANLTfplDARWGGDPLAL-----FWALAARQPVGYGALVDLGGPVILSRSPELFFR-VDGE 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 524 CLFS--PIKGTLKReGHMSLEEARKK--LLN-EKDMGELNMIIDLIRNDLHQLAKKNSVHVPELYSVEEHSNVYSLLSNI 598
Cdd:PRK07508 188 GWIEthPMKGTAPR-GATPAEDARLRaaLLNdEKNQAENRMIVDLLRNDISRISEVGSLDVPELFDIETYPTVHQMVSRV 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 599 YGRIESPITAWDVLSKSFPPGSMTGAPKLRSVRMLEPLEQHGRGIYSGTLGYWDVTGSAEFNVIIRSAFKYkADDYWRIG 678
Cdd:PRK07508 267 RARLLPGLGLADIFAALFPCGSITGAPKIRAMEILRELEPGPRDLYCGAIGWIAPDGRMRFNVAIRTLSLF-PGGRAVFN 345
|
250 260
....*....|....*....|..
gi 19113328 679 AGGAVTILSSPEGEYEEMVLKA 700
Cdd:PRK07508 346 VGGGIVFDSTAEAEYEECLLKA 367
|
|
| PRK05670 |
PRK05670 |
anthranilate synthase component II; Provisional |
10-197 |
8.14e-43 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 235552 [Multi-domain] Cd Length: 189 Bit Score: 153.36 E-value: 8.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 10 ILLIDCYDSYTFNLYDllYKASENACVIVVHWDKMSPDLWEDILQfDAIVVGPGPGHPAEYSSILNRIWQL--NIPVMGI 87
Cdd:PRK05670 2 ILLIDNYDSFTYNLVQ--YLGELGAEVVVYRNDEITLEEIEALNP-DAIVLSPGPGTPAEAGISLELIREFagKVPILGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 88 CLGFQSLALYHGATIERMPNlPWHGRVSSVTTSKTFIFDGI-SAVKGMRYHSLYANKIPI-DSLQILAQSDeDNIVMSIK 165
Cdd:PRK05670 79 CLGHQAIGEAFGGKVVRAKE-IMHGKTSPIEHDGSGIFAGLpNPFTVTRYHSLVVDRESLpDCLEVTAWTD-DGEIMGVR 156
|
170 180 190
....*....|....*....|....*....|..
gi 19113328 166 ATKFPHFGILYHPESVGSSKSLKIFKNFLSLA 197
Cdd:PRK05670 157 HKELPIYGVQFHPESILTEHGHKLLENFLELA 188
|
|
| PRK09070 |
PRK09070 |
aminodeoxychorismate synthase component I; |
442-707 |
2.13e-42 |
|
aminodeoxychorismate synthase component I;
Pssm-ID: 236371 [Multi-domain] Cd Length: 447 Bit Score: 159.87 E-value: 2.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 442 PKKevYCESVKACQEHLLAGDSYEMCLT---DTTFVS--APPELsdfemYMRARSLNPATFAGFVRLNHFTLLCCSPERF 516
Cdd:PRK09070 182 PER--FTDGVERVLDYIRAGDVFQVNLSrawQAQFANavDPAAL-----YARLRAANPAPFSGLFVAAGRAIVSSSPERL 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 517 LQFRDDRCLFSPIKGTLKREGHMSLEEARKKLLNE-KDMGELNMIIDLIRNDLHQLAKKNSVHVPELYSVEEHSNVYSLL 595
Cdd:PRK09070 255 VSVQGGVVQTRPIAGTRPRFAGDDDAALIRELVGHpKERAEHVMLIDLERNDLGRICAPGSVEVDELMTVESYAHVHHIV 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 596 SNIYGRIESPITAWDVLSKSFPPGSMTGAPKLRSVRMLEPLEQHGRGIYSGTLGYWDVTGSAEFNVIIRSAFKYKADDYW 675
Cdd:PRK09070 335 SNVRGRLRDGVTPGEVIRAVFPGGTITGCPKVRCMQIIAELEQTPRGAYTGSFGYLNRDGDMDLNILIRTAEVQGNQVRF 414
|
250 260 270
....*....|....*....|....*....|..
gi 19113328 676 RIGAGgaVTILSSPEGEYEEMVLKANSILPAF 707
Cdd:PRK09070 415 RTGAG--IVVDSDPERELDETRAKARGLLRAL 444
|
|
| PRK13574 |
PRK13574 |
anthranilate synthase component I; Provisional |
249-695 |
1.57e-41 |
|
anthranilate synthase component I; Provisional
Pssm-ID: 184155 [Multi-domain] Cd Length: 420 Bit Score: 156.90 E-value: 1.57e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 249 EPLALADCIQKSGNPICFLDSAKKP---GRYSILGILTgplariihyekatntteirickdNSFVRINNDLWSTVADFMN 325
Cdd:PRK13574 11 SPFEVFKCIERDFKVAGLLESIGGPqykARYSVIAWGT-----------------------NGYLKIHDDPVNILNSYLK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 326 QhkaiKPDTNLP--FYGGIMGIIGYECSDLSTKSVSNASFPLDFQqttvDAELAFVDRSFVFDLEIKKLFVQTLTPLNET 403
Cdd:PRK13574 68 D----LKLVDIPglFKGGMIGYISYDAVRFWEKIRDLKPAAEDWP----YAEFFIPDNIIIYDHNEGKVYVNGDLSSVGG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 404 CSEwwgellastcntkldnlsclhsfDGKQNFGLVQSFPKKEVYCESVKACQEHLLAGDSYEMCLTdtTFVSAPPELSDF 483
Cdd:PRK13574 140 CGD-----------------------MGEFKISFYDESLNKNNYEKIVSESLEYIRSGYIFQVVLS--RFYRYLFSGDPL 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 484 EMYMRARSLNPATFAGFVRLNHFTLLCCSPERFLQFRDDRCLFSPIKGTLKR----EGHMSLEEarkKLLN-EKDMGELN 558
Cdd:PRK13574 195 RIYYNLRRINPSPYMFYLKFDERYLIGSSPELLFRVQDNIVETYPIAGTRPRgsdqEEDLKLEL---ELMNsEKDKAEHL 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 559 MIIDLIRNDLHQLAKKNSVHVPELYSVEEHSNVYSLLSNIYGRIESPITAWDVLSKSFPPGSMTGAPKLRSVRMLEPLEQ 638
Cdd:PRK13574 272 MLVDLARNDLGKVCVPGTVRVPELMYVEKYSHVQHIVSKVIGTLKKKYNALDVLKATFPAGTVSGAPKPMAMNIIETLEE 351
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 19113328 639 HGRGIYSGTLGYWDVTGSAEFNVIIRSAFKYKadDYWRIGAGGAVTILSSPEGEYEE 695
Cdd:PRK13574 352 YKRGPYAGAVGFISADGNAEFAIAIRTAFLNK--DLLRIQAGAGIVYDSNPESEYFE 406
|
|
| PRK13572 |
PRK13572 |
anthranilate synthase component I; Provisional |
240-707 |
5.05e-41 |
|
anthranilate synthase component I; Provisional
Pssm-ID: 237432 [Multi-domain] Cd Length: 435 Bit Score: 155.67 E-value: 5.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 240 IHSVEIPWVEPLALADCIQKSGNPIcFLDSAKKPG---RYSILGILTGPLARIihyekaTNTTEIrickDNSFV-RINND 315
Cdd:PRK13572 1 MLMKKLDYVNPLKLYSVLRDEGYPF-ILESAEKGQrkaRYTYISANPEFMVRI------GNKTKV----DGETIsKESNP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 316 LWSTVADFMNQHKAIKpdtnlpFYGGIMGIIGYEC------SDLSTKSVsnasfpldfqqttvdaeLAFVDRSFVFDLEI 389
Cdd:PRK13572 70 FKALKENFKITQSGDR------FTGGFVGYIAYDAvhnyigGKIEEPSV-----------------FGYYDHVFVYDHVT 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 390 KKLFVQTLT--PLNETCSEwwgELLASTCNTKLDNLsclhsfDGkqNFGLVQSFPKKEVYCESVKACQEHLLAGDSYEMC 467
Cdd:PRK13572 127 RKFYFHSLNnnPEELFNAE---KIVEKAKRFEIEEE------DG--GSEVLGCDADREEFVEMVEKAKEYIYSGDVFQVV 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 468 LTDTTFVSAppELSDFEMYMRARSLNPATFAGFVRLNHfTLLCCSPERFLQFRDDRCLFSPIKGTLK--REGHMSLEEAR 545
Cdd:PRK13572 196 LSREYRLKT--DLSPFQLYRNLREINPSPYMFLLEFDK-DVVGASPETMASVENNILKINPIAGTAPrgKTEEEDKKLAE 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 546 KKLLNEKDMGELNMIIDLIRNDLHQLAKKNSVHVPELYSVEEHSNVYSLLSNIYGRIESPITAWDVLSKSFPPGSMTGAP 625
Cdd:PRK13572 273 ALLSDEKERAEHVMLVDLARNDVRKVSKSGSVRLERFFDVVKYSHVQHIESEVVGELKEDSTMFDAIEAAFPAGTLTGAP 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 626 KLRSVRMLEPLEQHGRGIYSGTLGYWDVTGSAEFNVIIRSAfkyKADDYWRIGAGGAVTILSSPEGEYEEMVLKANSILP 705
Cdd:PRK13572 353 KFRAMEIIDELEKSRRKVYGGAVGYFSNSGNADLAIAIRMA---EIDKVCRVRAGAGIVADSVPEKEFYETERKMAAVLK 429
|
..
gi 19113328 706 AF 707
Cdd:PRK13572 430 AL 431
|
|
| PRK07093 |
PRK07093 |
para-aminobenzoate synthase component I; Validated |
419-699 |
4.97e-38 |
|
para-aminobenzoate synthase component I; Validated
Pssm-ID: 235932 [Multi-domain] Cd Length: 323 Bit Score: 144.24 E-value: 4.97e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 419 KLDNLSCLHSFDGKQNFGLVQSFPKK----------EVYCESVKACQEHLLAGDSYEMCLTDTTFVSAPpeLSDFEMYMR 488
Cdd:PRK07093 38 ELAESGILFDFNGKTNVPSQVRPHKPfelqkepisfEEYQQGFELVQEEIQAGNSYLLNLTYPTPIETN--LSLEEIFQA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 489 ARslnpatfAGFVRLNHFTLLCCSPERFLQFRDDRCLFSPIKGTLKreghMSLEEARKKLLN-EKDMGELNMIIDLIRND 567
Cdd:PRK07093 116 SK-------AKYKLLFKDQFVCFSPEPFVRIEDNKISTYPMKGTID----ASLPNAEEKLLNdEKEFAEHATIVDLLRND 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 568 LHQLAKKnsVHVPELYSVEE-HSNVYSLL---SNIYGRIESPitaW-----DVLSKSFPPGSMTGAPKLRSVRMLEPLEQ 638
Cdd:PRK07093 185 LSMVAKN--VRVTRFRYIDKiKTNKGEILqtsSEISGTLPEN---WqenigDILAKLLPAGSITGAPKEKTVEIIEQAEG 259
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19113328 639 HGRGIYSGTLGYWDvtG----SAefnVIIRsaFKYKADD--YWRigAGGAVTILSSPEGEYEEMVLK 699
Cdd:PRK07093 260 YERGFYTGVFGYFD--GesldSA---VMIR--FIEQENDglYFK--SGGGITIDSDLKDEYNELIQK 317
|
|
| PRK05940 |
PRK05940 |
anthranilate synthase component I; |
447-714 |
9.90e-37 |
|
anthranilate synthase component I;
Pssm-ID: 235651 [Multi-domain] Cd Length: 463 Bit Score: 143.72 E-value: 9.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 447 YCESVKACQEHLLAGDSYEMCLTdTTFvSAPPELSDFEMYMRARSLNPATFAGFVRLNHFTLLCCSPERFLQFRDDRCLF 526
Cdd:PRK05940 192 YEAAVRQAKKYIQAGDIFQANLS-LRF-QTTTSADSWQIYRRLQQINPSPFASYWRTPWGDVVSCSPERLVQLQGNQAQT 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 527 SPIKGTLKREGHMSLEE--ARKKLLNEKDMGELNMIIDLIRNDLHQLAKKNSVHVPELYSVEEHSNVYSLLSNIYGRIES 604
Cdd:PRK05940 270 RPIAGTRPRGKTPAEDQqlAEELLSNIKERAEHIMLVDLERNDLGRVCQWGSVEVDELLTIERYSHVIHLVSNVVGTLQP 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 605 PITAWDVLSKSFPPGSMTGAPKLRSVRMLEPLEQHGRGIYSGTLGYWDVTGSAEFNVIIRSAFKYKADD-----YWRIGA 679
Cdd:PRK05940 350 NRDAIDLIRALFPGGTITGCPKVRCMEIIEELEPVRRNLFYGSCGYLDQRGNLDLNILIRTLLYTPLSRglstiWGQVGA 429
|
250 260 270
....*....|....*....|....*....|....*
gi 19113328 680 GgaVTILSSPEGEYEEMVLKANSILPAFVNLKNKK 714
Cdd:PRK05940 430 G--IVADSDPEKEWLESLQKAKAQLAALNLVRSQN 462
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
11-194 |
8.97e-36 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 133.52 E-value: 8.97e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 11 LLIDCYDSYTFNLYDLLYKAseNACVIVVHWDkmSPDLWEDILQFDAIVVGPGPGHPAEY---SSILNRIWQLNIPVMGI 87
Cdd:pfam00117 1 LLIDNGDSFTYNLARALREL--GVEVTVVPND--TPAEEILEENPDGIILSGGPGSPGAAggaIEAIREARELKIPILGI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 88 CLGFQSLALYHGATIERMPNLPWHGRVSSVTTSKTFIFDGI-SAVKGMRYHSLYANKIPI-DSLQILAQSDEDNIVMSIK 165
Cdd:pfam00117 77 CLGHQLLALAFGGKVVKAKKFGHHGKNSPVGDDGCGLFYGLpNVFIVRRYHSYAVDPDTLpDGLEVTATSENDGTIMGIR 156
|
170 180
....*....|....*....|....*....
gi 19113328 166 ATKFPHFGILYHPESVGSSKSLKIFKNFL 194
Cdd:pfam00117 157 HKKLPIFGVQFHPESILTPHGPEILFNFF 185
|
|
| PRK13571 |
PRK13571 |
anthranilate synthase component I; Provisional |
444-706 |
3.36e-35 |
|
anthranilate synthase component I; Provisional
Pssm-ID: 184152 [Multi-domain] Cd Length: 506 Bit Score: 140.16 E-value: 3.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 444 KEVYCESVKACQEHLLAGDSYEMCL-----TDTTfvsAPPelsdFEMYMRARSLNPATFAGFVRLNH------FTLLCCS 512
Cdd:PRK13571 229 VEEFGAAVEKLVEEIRAGEAFQVVPsqrfeMDTT---ADP----LDVYRVLRVTNPSPYMYLLRVPNsdggtdFSIVGSS 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 513 PERFLQFRDDRCLFSPIKGTLKReGHMSLEEAR--KKLL-NEKDMGELNMIIDLIRNDLHQLAKKNSVHVPELYSVEEHS 589
Cdd:PRK13571 302 PEALVTVTDGRATTHPIAGTRWR-GATPEEDALleKELLaDPKERAEHLMLVDLGRNDLGRVCRPGTVRVVDFSHIERYS 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 590 NVYSLLSNIYGRIESPITAWDVLSKSFPPGSMTGAPKLRSVRMLEPLEQHGRGIYSGTLGYWDVTGSAEFNVIIRSAFKY 669
Cdd:PRK13571 381 HVMHLVSTVTGELAEGRTALDAVTACFPAGTLSGAPKVRAMELIEELEPTRRGLYGGVVGYLDFAGDADTAIAIRTALMR 460
|
250 260 270
....*....|....*....|....*....|....*..
gi 19113328 670 KADDYwrIGAGGAVTILSSPEGEYEEMVLKANSILPA 706
Cdd:PRK13571 461 DGTAY--VQAGGGVVADSDPDYEDNEARNKAAAVLRA 495
|
|
| PRK13567 |
PRK13567 |
anthranilate synthase component I; Provisional |
248-704 |
3.40e-32 |
|
anthranilate synthase component I; Provisional
Pssm-ID: 184148 [Multi-domain] Cd Length: 468 Bit Score: 130.65 E-value: 3.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 248 VEPLALAdciQKSGNPICF--LDSAKKPGRYSILGIltgplariIHYEKAT-NTTEIRICKDNSFVRINNDLWSTVADFM 324
Cdd:PRK13567 12 VTPEVLA---QLHSKKIILesTNQQQTKGRYSVVIF--------DIYGTLTlDNDVLSVSTLKESYQITERPYHYLTTKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 325 NQHKAIKPDT---NLPFYGGIMGiigyECS-DLSTKSvsnasFPL-------DFQQTtvDAELAFVDRSFVFDLEIKKLF 393
Cdd:PRK13567 81 NEDYHNIQDEqlkSLPFISGYVG----TCSfDLVRHE-----FPKlqsiqleDHKQH--DVRLYMVEQVYVFDHYKDELY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 394 VqtlTPLNETCSEWWGELLASTCNtKLDNLSCLHSFDGKQNFGL----VQSFPKKEVYCESVKACQEHLLAGDSYEMCLT 469
Cdd:PRK13567 150 I---IATNQFSNSTKSDLENRVNK-SIEDLTKIQPFMPTQDFDFktkeIQSNISEERFIEMIQYFKEKITEGDMFQVVPS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 470 -----DTTFVSAPPELSdFEMYMRARSLNPATFAGFVRLNHFTLLCCSPERFLQFRDDRCLFSPIKGTLKREGHMSLEEA 544
Cdd:PRK13567 226 riykyAHHASQHLNQLS-FQLYQNLKRQNPSPYMYYLNIDQPYIVGSSPESFVSVKDQIVTTNPIAGTIQRGETTQIDNE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 545 R-KKLLN-EKDMGELNMIIDLIRNDLHQLAKKNSVHVPELYSVEEHSNVYSLLSNIYGRIESPITAWDVLSKSFPPGSMT 622
Cdd:PRK13567 305 NmKQLLNdPKECSEHRMLVDLGRNDIHRVSKIGTSKITKLMVIEKYEHVMHIVSEVTGKINQNLSPMTVIANLLPTGTVS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 623 GAPKLRSVRMLEPLEQHGRGIYSGTLGYWDVTGSAEFNVIIRSAFkyKADDYWRIGAGGAVTILSSPEGEYEEMVLKANS 702
Cdd:PRK13567 385 GAPKLRAIERIYEQYPHKRGVYSGGVGYINCNHNLDFALAIRTMM--IDEQYINVEAGCGVVYDSIPEKELNETKLKAKS 462
|
..
gi 19113328 703 IL 704
Cdd:PRK13567 463 LL 464
|
|
| trpG |
CHL00101 |
anthranilate synthase component 2 |
10-198 |
3.82e-32 |
|
anthranilate synthase component 2
Pssm-ID: 214365 [Multi-domain] Cd Length: 190 Bit Score: 123.30 E-value: 3.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 10 ILLIDCYDSYTFNLYDLLykASENACVIVVHWDKMspDLWE-DILQFDAIVVGPGPGHPAEYSSILNRIWQL--NIPVMG 86
Cdd:CHL00101 2 ILIIDNYDSFTYNLVQSL--GELNSDVLVCRNDEI--DLSKiKNLNIRHIIISPGPGHPRDSGISLDVISSYapYIPILG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 87 ICLGFQSLALYHGATIERMPNlPWHGRVSSVTTSKTFIFDGISA-VKGMRYHSLYANKI-PIDSLQILAQSdEDNIVMSI 164
Cdd:CHL00101 78 VCLGHQSIGYLFGGKIIKAPK-PMHGKTSKIYHNHDDLFQGLPNpFTATRYHSLIIDPLnLPSPLEITAWT-EDGLIMAC 155
|
170 180 190
....*....|....*....|....*....|....*
gi 19113328 165 KATKFPH-FGILYHPESVGSSKSLKIFKNFLSLAD 198
Cdd:CHL00101 156 RHKKYKMlRGIQFHPESLLTTHGQQILRNFLSLSS 190
|
|
| PLN02445 |
PLN02445 |
anthranilate synthase component I |
274-700 |
4.76e-31 |
|
anthranilate synthase component I
Pssm-ID: 215244 [Multi-domain] Cd Length: 523 Bit Score: 127.87 E-value: 4.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 274 GRYSILGiltgplariihyekATNTTEIrICKDNSFVRINNDLWS----TVADFMNQHKAIKPDTN------LP--FYGG 341
Cdd:PLN02445 57 GRYSVVG--------------AQPAMEI-VAKENKVTIMDHEKGTrteeIVEDPMEIPRRISEKWNpqlidgLPdvFCGG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 342 IMGIIGYECSDLSTKS---VSNAsfPLDfQQTTVDAELAFVDRSFVFDLEIKKLFVqtLTPLNETCSEWWGELLASTCNt 418
Cdd:PLN02445 122 WVGYFSYDTVRYVEKKklpFSGA--PED-DRNLPDIHLGLYDDVIVFDHVEKKAYV--IHWVRLDRYSSVEEAYEDGMK- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 419 KLDNL-SCLHSFDG-KQNFGLV----QSFPK--------KEVYCESVKACQEHLLAGDSYEMCLTD----TTFvsAPPel 480
Cdd:PLN02445 196 RLEALvSRLQDINPpKLSPGSVklstNQFGPsleksnmtSEEYKNAVLQAKEHILAGDIFQIVLSQrferRTF--ADP-- 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 481 sdFEMYMRARSLNPATFAGFVRLNHFTLLCCSPERFLQFRDDRCLFSPIKGTLKR-----EGHMsLEEArkkLLN-EKDM 554
Cdd:PLN02445 272 --FEVYRALRIVNPSPYMIYLQARGCILVASSPEILTRVKKNKIVNRPLAGTRRRgktpeEDKA-LEKD---LLAdEKQC 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 555 GELNMIIDLIRNDLHQLAKKNSVHVPELYSVEEHSNVYSLLSNIYGRIESPITAWDVLSKSFPPGSMTGAPKLRSVRMLE 634
Cdd:PLN02445 346 AEHIMLVDLGRNDVGKVSKAGSVKVEKLMNIERYSHVMHISSTVTGELLDHLTSWDALRAALPVGTVSGAPKVRAMELID 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 635 PLEQHGRGIYSGTLGYWDVTGSAEFNVIIRS-----------AFKYKADDYWR-----IGAGGAVTILSSPEGEYEEMVL 698
Cdd:PLN02445 426 ELEVTRRGPYSGGFGGVSFTGDMDIALALRTmvfptaarydtMYSYKDTNSRRewvahLQAGAGIVADSDPEDEYRECVN 505
|
..
gi 19113328 699 KA 700
Cdd:PLN02445 506 KA 507
|
|
| PRK14607 |
PRK14607 |
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase; |
10-197 |
5.32e-31 |
|
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
Pssm-ID: 237764 [Multi-domain] Cd Length: 534 Bit Score: 127.91 E-value: 5.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 10 ILLIDCYDSYTFNLYDLLYKASENaCVIVVHWDKMSpdlWEDI--LQFDAIVVGPGPGHPAEYSSILNRIWQL--NIPVM 85
Cdd:PRK14607 2 IILIDNYDSFTYNIYQYIGELGPE-EIEVVRNDEIT---IEEIeaLNPSHIVISPGPGRPEEAGISVEVIRHFsgKVPIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 86 GICLGFQSLALYHGATIERMPNlPWHGRVSSVTTSKTFIFDGI-SAVKGMRYHSLY--ANKIPiDSLQILAQSDeDNIVM 162
Cdd:PRK14607 78 GVCLGHQAIGYAFGGKIVHAKR-ILHGKTSPIDHNGKGLFRGIpNPTVATRYHSLVveEASLP-ECLEVTAKSD-DGEIM 154
|
170 180 190
....*....|....*....|....*....|....*
gi 19113328 163 SIKATKFPHFGILYHPESVGSSKSLKIFKNFLSLA 197
Cdd:PRK14607 155 GIRHKEHPIFGVQFHPESILTEEGKRILKNFLNYQ 189
|
|
| Anth_synII_Halo |
NF041322 |
anthranilate synthase component II; |
13-197 |
3.73e-26 |
|
anthranilate synthase component II;
Pssm-ID: 469219 [Multi-domain] Cd Length: 190 Bit Score: 105.88 E-value: 3.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 13 IDCYDSYTFNLYDLLYKASENACVIVVhwdKMSPDLwEDILQF--DAIVVGPGPGHPA-------------EYSSilnri 77
Cdd:NF041322 2 VDNFDSFTYNLVEYVSEQREHAETTVL---KNTASL-AEVRAVdpDAIVISPGPGHPKndrdvgvtadvlrELSP----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 78 wqlNIPVMGICLGFQSLALYHGATIERMPNlPWHGRVSSVTTSKTFIFDGI-SAVKGMRYHSLYANKIPiDSLQILAQSD 156
Cdd:NF041322 73 ---EVPTLGVCLGLEAAVYAYGGTVGRAPE-PVHGKAFPVDHDGEGVFAGLeQGFQAGRYHSLVATEVP-DCFEVTATTD 147
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 19113328 157 ED--NIVMSIKATKFPHFGILYHPESVGSSKSLKIFKNFLSLA 197
Cdd:NF041322 148 HDgeELVMGIRHREHPIECVQFHPESVLTGVGHDVIENFLAAA 190
|
|
| PRK07765 |
PRK07765 |
aminodeoxychorismate/anthranilate synthase component II; |
8-181 |
8.10e-26 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181107 [Multi-domain] Cd Length: 214 Bit Score: 105.90 E-value: 8.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 8 LQILLIDCYDSYTFNLYDLLYKASENAcvIVVHWDKMSP-DLWEDILQFDAIVVGPGPGHPAEYSSILNRI---WQLNIP 83
Cdd:PRK07765 1 MRILVVDNYDSFVFNLVQYLGQLGVEA--EVWRNDDPRLaDEAAVAAQFDGVLLSPGPGTPERAGASIDMVracAAAGTP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 84 VMGICLGFQSLALYHGATIERMPNLpWHGRVSSVTTSKTFIFDGI-SAVKGMRYHSLYA--NKIPiDSLQILAQSDeDNI 160
Cdd:PRK07765 79 LLGVCLGHQAIGVAFGATVDRAPEL-LHGKTSSVHHTGVGVLAGLpDPFTATRYHSLTIlpETLP-AELEVTARTD-SGV 155
|
170 180
....*....|....*....|.
gi 19113328 161 VMSIKATKFPHFGILYHPESV 181
Cdd:PRK07765 156 IMAVRHRELPIHGVQFHPESV 176
|
|
| PRK13566 |
PRK13566 |
anthranilate synthase component I; |
10-197 |
1.35e-24 |
|
anthranilate synthase component I;
Pssm-ID: 237429 [Multi-domain] Cd Length: 720 Bit Score: 109.62 E-value: 1.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 10 ILLIDCYDSYTFNLYDllYKASENACVIVVHWDKMSPDLweDILQFDAIVVGPGPGHPAEY--SSILNRIWQLNIPVMGI 87
Cdd:PRK13566 529 VLLVDHEDSFVHTLAN--YFRQTGAEVTTVRYGFAEEML--DRVNPDLVVLSPGPGRPSDFdcKATIDAALARNLPIFGV 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 88 CLGFQSLALYHGATIERMPNlPWHGRVSSVT-TSKTFIFDGI-SAVKGMRYHSLYA--NKIPiDSLQILAQSdEDNIVMS 163
Cdd:PRK13566 605 CLGLQAIVEAFGGELGQLAY-PMHGKPSRIRvRGPGRLFSGLpEEFTVGRYHSLFAdpETLP-DELLVTAET-EDGVIMA 681
|
170 180 190
....*....|....*....|....*....|....*..
gi 19113328 164 IKATKFPHFGILYHPESV---GSSKSLKIFKNFLSLA 197
Cdd:PRK13566 682 IEHKTLPVAAVQFHPESImtlGGDVGLRIIENVVRLL 718
|
|
| PRK07649 |
PRK07649 |
aminodeoxychorismate/anthranilate synthase component II; |
10-194 |
1.43e-24 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181066 [Multi-domain] Cd Length: 195 Bit Score: 101.80 E-value: 1.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 10 ILLIDCYDSYTFNLYDLLYKASE------NACVIVVHWDKMSPDLwedilqfdaIVVGPGPGHPAEYSSILNRIWQL--N 81
Cdd:PRK07649 2 ILMIDNYDSFTFNLVQFLGELGQelvvkrNDEVTISDIENMKPDF---------LMISPGPCSPNEAGISMEVIRYFagK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 82 IPVMGICLGFQSLALYHGATIERMPNLpWHGRVSSVTTSKTFIFDGI-SAVKGMRYHSLYANK--IPiDSLQILAQSDED 158
Cdd:PRK07649 73 IPIFGVCLGHQSIAQVFGGEVVRAERL-MHGKTSLMHHDGKTIFSDIpNPFTATRYHSLIVKKetLP-DCLEVTSWTEEG 150
|
170 180 190
....*....|....*....|....*....|....*.
gi 19113328 159 NIvMSIKATKFPHFGILYHPESVGSSKSLKIFKNFL 194
Cdd:PRK07649 151 EI-MAIRHKTLPIEGVQFHPESIMTSHGKELLQNFI 185
|
|
| PLN02335 |
PLN02335 |
anthranilate synthase |
10-198 |
7.21e-24 |
|
anthranilate synthase
Pssm-ID: 177969 [Multi-domain] Cd Length: 222 Bit Score: 100.64 E-value: 7.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 10 ILLIDCYDSYTFNLYDLL------YKASENACVIVVHWDKMSPDlwedilqfdAIVVGPGPGHPAEYSSILNRIWQLN-- 81
Cdd:PLN02335 21 IIVIDNYDSFTYNLCQYMgelgchFEVYRNDELTVEELKRKNPR---------GVLISPGPGTPQDSGISLQTVLELGpl 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 82 IPVMGICLGFQSLALYHGATIERMPNLPWHGRVSSVTTSKTF---IFDGISA-VKGMRYHSLYANK--IPIDSLQILAQS 155
Cdd:PLN02335 92 VPLFGVCMGLQCIGEAFGGKIVRSPFGVMHGKSSPVHYDEKGeegLFSGLPNpFTAGRYHSLVIEKdtFPSDELEVTAWT 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 19113328 156 dEDNIVMSIKATKFPHF-GILYHPESVGSSKSLKIFKNFLSLAD 198
Cdd:PLN02335 172 -EDGLIMAARHRKYKHIqGVQFHPESIITTEGKTIVRNFIKIIE 214
|
|
| PRK08007 |
PRK08007 |
aminodeoxychorismate synthase component 2; |
10-195 |
1.15e-23 |
|
aminodeoxychorismate synthase component 2;
Pssm-ID: 181194 [Multi-domain] Cd Length: 187 Bit Score: 98.84 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 10 ILLIDCYDSYTFNLYDllYKASENACVIVVHWDKMSpdLWE-DILQFDAIVVGPGPGHPAEYSSILN--RIWQLNIPVMG 86
Cdd:PRK08007 2 ILLIDNYDSFTWNLYQ--YFCELGADVLVKRNDALT--LADiDALKPQKIVISPGPCTPDEAGISLDviRHYAGRLPILG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 87 ICLGFQSLALYHGATIERMPNLpWHGRVSSVTTSKTFIFDGIS-AVKGMRYHSLYANKIPI-DSLQILAQSDEDNIvMSI 164
Cdd:PRK08007 78 VCLGHQAMAQAFGGKVVRAAKV-MHGKTSPITHNGEGVFRGLAnPLTVTRYHSLVVEPDSLpACFEVTAWSETREI-MGI 155
|
170 180 190
....*....|....*....|....*....|.
gi 19113328 165 KATKFPHFGILYHPESVGSSKSLKIFKNFLS 195
Cdd:PRK08007 156 RHRQWDLEGVQFHPESILSEQGHQLLANFLH 186
|
|
| PRK06404 |
PRK06404 |
anthranilate synthase component I; Reviewed |
500-704 |
5.04e-22 |
|
anthranilate synthase component I; Reviewed
Pssm-ID: 102361 [Multi-domain] Cd Length: 351 Bit Score: 98.40 E-value: 5.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 500 FVRLNHFTLLCCSPERFLQFRDDRCLFSPIKGTLKregHMSLEEARkkLLNEKDMGELNMIIDLIRNDLHQLAKKNSVHV 579
Cdd:PRK06404 156 YYRFGKYRVVGSSPENVFTVNGNIINVDPIAGTYD---DKILSNEL--LNSEKDKLEHRMLLDLARNDLSKFADIGTLNV 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 580 PELYSVEEHSNVYSLLSNIYGRIeSPITAWDVLSKSFPPGSMTGAPKLRSVRMLEPLEQHGRGIYSGTLGywdVTGSAEF 659
Cdd:PRK06404 231 DKVMKIEEFSSVKHLVSQVTAKF-SNASYRDILASMFPAGTVSGSPKERAIEIINKYEETPRGPYGGAIG---IISKGYT 306
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 19113328 660 N--VIIRSAfkYKADDYWRIGAGGAVTILSSPEGEYEEMVLKANSIL 704
Cdd:PRK06404 307 DmaLVIRTA--YSHGNGFRVRAGAGIVKDSDPEDEVNEIYSKARSVM 351
|
|
| Anth_synt_I_N |
pfam04715 |
Anthranilate synthase component I, N terminal region; Anthranilate synthase (EC:4.1.3.27) ... |
246-394 |
1.44e-21 |
|
Anthranilate synthase component I, N terminal region; Anthranilate synthase (EC:4.1.3.27) catalyzes the first step in the biosynthesis of tryptophan. Component I catalyzes the formation of anthranilate using ammonia and chorismate. The catalytic site lies in the adjacent region, described in the chorismate binding enzyme family (pfam00425). This region is involved in feedback inhibition by tryptophan. This family also contains a region of Para-aminobenzoate synthase component I (EC 4.1.3.-).
Pssm-ID: 428082 [Multi-domain] Cd Length: 140 Bit Score: 91.22 E-value: 1.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 246 PWVEPLALADCIQKSGNPIcFLDSAK-KPGRYSILGIltGPLARIIhyekaTNTTEIRICKDNSFVRINND-LWSTVADF 323
Cdd:pfam04715 1 DLLTPLSVYLKLAGEPHSF-LLESAEgGEGRYSFIGI--NPLLTIK-----SKNGEVSVSGPDGQELEQEDgPLDALRAL 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19113328 324 MNQHKAIKP-DTNLPFYGGIMGIIGYECSDLSTKSVSNASFPLDfqqtTVDAELAFVDRSFVFDLEIKKLFV 394
Cdd:pfam04715 73 LARFRIEDSpPTLPPFSGGLVGYLGYDLVRYIEKLPRTAPDDLN----LPDARLILYEDLIVFDHQENKLYL 140
|
|
| PRK06774 |
PRK06774 |
aminodeoxychorismate synthase component II; |
10-194 |
2.63e-21 |
|
aminodeoxychorismate synthase component II;
Pssm-ID: 180689 [Multi-domain] Cd Length: 191 Bit Score: 92.23 E-value: 2.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 10 ILLIDCYDSYTFNLYDllYKASENACVIVVHWDKMSpdlWEDILQF--DAIVVGPGPGHPAEYSSILNRIWQL--NIPVM 85
Cdd:PRK06774 2 LLLIDNYDSFTYNLYQ--YFCELGTEVMVKRNDELQ---LTDIEQLapSHLVISPGPCTPNEAGISLAVIRHFadKLPIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 86 GICLGFQSLALYHGATIERMPNLpWHGRVSSVTTSKTFIFDGIS-AVKGMRYHSLY--ANKIPiDSLQILAQSDEDNIV- 161
Cdd:PRK06774 77 GVCLGHQALGQAFGARVVRARQV-MHGKTSAICHSGQGVFRGLNqPLTVTRYHSLViaADSLP-GCFELTAWSERGGEMd 154
|
170 180 190
....*....|....*....|....*....|....*
gi 19113328 162 --MSIKATKFPHFGILYHPESVGSSKSLKIFKNFL 194
Cdd:PRK06774 155 eiMGIRHRTLPLEGVQFHPESILSEQGHQLLDNFL 189
|
|
| PRK05637 |
PRK05637 |
anthranilate synthase component II; Provisional |
10-183 |
8.40e-20 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 180178 [Multi-domain] Cd Length: 208 Bit Score: 88.36 E-value: 8.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 10 ILLIDCYDSYTFNLYDLLYKASENACVIvvhwdKMSPDLwEDIL--QFDAIVVGPGPGHPAEYSSILNRIWQL--NIPVM 85
Cdd:PRK05637 4 VVLIDNHDSFVYNLVDAFAVAGYKCTVF-----RNTVPV-EEILaaNPDLICLSPGPGHPRDAGNMMALIDRTlgQIPLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 86 GICLGFQSLALYHGATIErmPNLPWHGRVSSVTTSKTF----IFDGISA-------------VKGMRYHSLYANKIPiDS 148
Cdd:PRK05637 78 GICLGFQALLEHHGGKVE--PCGPVHGTTDNMILTDAGvqspVFAGLATdvepdhpeipgrkVPIARYHSLGCVVAP-DG 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 19113328 149 LQILAQSDED--NIVMSIKATKFPHFGILYHPESVGS 183
Cdd:PRK05637 155 MESLGTCSSEigPVIMAAETTDGKAIGLQFHPESVLS 191
|
|
| PRK06895 |
PRK06895 |
anthranilate synthase component II; |
10-198 |
6.95e-18 |
|
anthranilate synthase component II;
Pssm-ID: 235882 [Multi-domain] Cd Length: 190 Bit Score: 82.09 E-value: 6.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 10 ILLIDCYDSYTFNLYDLLYKASENACVIVVhwDKMSPDlweDILQFDAIVVGPGPGHPAEYS---SILNRIWQLNiPVMG 86
Cdd:PRK06895 4 LLIINNHDSFTFNLVDLIRKLGVPMQVVNV--EDLDLD---EVENFSHILISPGPDVPRAYPqlfAMLERYHQHK-SILG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 87 ICLGFQSLALYHGATIERMPNlPWHGRVSSV-TTSKTFIFDGI-SAVKGMRYHSLYANKIP-IDSLQILAQSDeDNIVMS 163
Cdd:PRK06895 78 VCLGHQTLCEFFGGELYNLNN-VRHGQQRPLkVRSNSPLFDGLpEEFNIGLYHSWAVSEENfPTPLEITAVCD-ENVVMA 155
|
170 180 190
....*....|....*....|....*....|....*
gi 19113328 164 IKATKFPHFGILYHPESVGSSKSLKIFKNFLSLAD 198
Cdd:PRK06895 156 MQHKTLPIYGVQFHPESYISEFGEQILRNWLAISP 190
|
|
| salicyl_syn |
TIGR03494 |
salicylate synthase; Members of this protein family are salicylate synthases, bifunctional ... |
512-705 |
1.43e-17 |
|
salicylate synthase; Members of this protein family are salicylate synthases, bifunctional enzymes that make salicylate, in two steps, from chorismate. Members are homologous to anthranilate synthase component I from Trp biosynthesis. Members typically are found in gene regions associated with siderophore or other secondary metabolite biosynthesis.
Pssm-ID: 132533 [Multi-domain] Cd Length: 425 Bit Score: 85.60 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 512 SPERFLQFRDDRCLFS-PIKGTLKRE-GHMSLEEARKKLLNE-KDMGELNMIIDLIRNDLHQLAKKNSVHVPELYSVEEH 588
Cdd:TIGR03494 227 SPELVMSVRADGKVVTePLAGTRALGgGPEHDKQLRDELLSDsKEIVEHAISVKEAIEELEQVCEPGTVVVEDFMTVRER 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 589 SNVYSLLSNIYGRIESPITAWDVLSKSFPPGSMTGAPKLRSVRMLEPLEQHGRGIYSGTLGYWDVTGSAEFNVIIRSAfk 668
Cdd:TIGR03494 307 GSVQHLGSTVSGQLAPSKDAWDAFEVLFPAITASGIPKAAALEAIMRLEKTPRGLYSGAVLLLDADGTLDAALVLRAA-- 384
|
170 180 190
....*....|....*....|....*....|....*..
gi 19113328 669 YKADDYWRIGAGGAVTILSSPEGEYEEMVLKANSILP 705
Cdd:TIGR03494 385 YQDSGRTWLQAGAGIIAQSTPERELTETCEKLASIAP 421
|
|
| PRK13564 |
PRK13564 |
anthranilate synthase component 1; |
445-706 |
1.60e-17 |
|
anthranilate synthase component 1;
Pssm-ID: 237428 [Multi-domain] Cd Length: 520 Bit Score: 86.43 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 445 EVYCESVKACQEHLLAGDSYEMCLTDTTFVSAPpelSDFEMYMRARSLNPATFAGFVRLNHFTLLCCSPERFLQFR-DDR 523
Cdd:PRK13564 243 EEFCAVVRKLKEHIRAGDIFQVVPSRRFSLPCP---SPLAAYRVLKKSNPSPYMFYMQDEDFTLFGASPESALKYDaSSR 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 524 CL-FSPIKGTLKR----EGHMSLE-EARKKL---LNEKDMGELNMIIDLIRNDLHQLAKKNSVHVPELYSVEEHSNVYSL 594
Cdd:PRK13564 320 QVeIYPIAGTRPRgrraDGSIDRDlDSRIELelrTDHKELAEHLMLVDLARNDLARICQPGSRYVADLLKVDRYSHVMHL 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 595 LSNIYGRIESPITAWDVLSKSFPPGSMTGAPKLRSVRMLEPLEQHGRGIYSGTLGYWDVTGSAEFNVIIRSAFkyKADDY 674
Cdd:PRK13564 400 VSRVVGELRHDLDALHAYRACMNMGTLTGAPKVRAMQLIREVEGQRRGSYGGAVGYLTGHGDLDTCIVIRSAF--VENGI 477
|
250 260 270
....*....|....*....|....*....|..
gi 19113328 675 WRIGAGGAVTILSSPEGEYEEMVLKANSILPA 706
Cdd:PRK13564 478 ATVQAGAGVVLDSDPQSEADETRNKAQAVLRA 509
|
|
| PRK08857 |
PRK08857 |
aminodeoxychorismate/anthranilate synthase component II; |
10-195 |
1.19e-16 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181566 [Multi-domain] Cd Length: 193 Bit Score: 78.77 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 10 ILLIDCYDSYTFNLYDllYKASENACVIVVHWDKMspdlweDILQFDA-----IVVGPGPGHPAEYSSILNRIWQL--NI 82
Cdd:PRK08857 2 LLMIDNYDSFTYNLYQ--YFCELGAQVKVVRNDEI------DIDGIEAlnpthLVISPGPCTPNEAGISLQAIEHFagKL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 83 PVMGICLGFQSLALYHGATIERMPNLpWHGRVSSVTTSKTFIFDGI-SAVKGMRYHSLY--ANKIPiDSLQILAQSDED- 158
Cdd:PRK08857 74 PILGVCLGHQAIAQVFGGQVVRARQV-MHGKTSPIRHTGRSVFKGLnNPLTVTRYHSLVvkNDTLP-ECFELTAWTELEd 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 19113328 159 ---NIVMSIKATKFPHFGILYHPESVGSSKSLKIFKNFLS 195
Cdd:PRK08857 152 gsmDEIMGFQHKTLPIEAVQFHPESIKTEQGHQLLANFLA 191
|
|
| PRK13566 |
PRK13566 |
anthranilate synthase component I; |
442-706 |
2.03e-16 |
|
anthranilate synthase component I;
Pssm-ID: 237429 [Multi-domain] Cd Length: 720 Bit Score: 83.43 E-value: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 442 PKKEVYCESVKACQEHLLAGDSYEMCLTDTTFvsAPPELSDFEMYMRARSLNPATFAGFVRL--NHFtLLCCSPERFLQF 519
Cdd:PRK13566 241 HAPGEYAALVEKAKESFRRGDLFEVVPGQTFY--EPCERSPSEIFRRLKEINPSPYGFFINLgdGEY-LVGASPEMFVRV 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 520 RDDRCLFSPIKGTLKReGHMSLEEAR--KKLLN-EKDMGELNMIIDLIRNDlhqlakKNSVHVP-----------ELYSV 585
Cdd:PRK13566 318 EGRRVETCPISGTIKR-GADAIGDAEqiRKLLNsKKDESELTMCTDVDRND------KSRVCEPgsvkvigrrqiEMYSR 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 586 EEHSnvyslLSNIYGRIESPITA--------WDVlsksfppgSMTGAPKLRSVRMLEPLEQHGRGIYSGTLGYWDVTGSA 657
Cdd:PRK13566 391 LIHT-----VDHVEGRLRPGFDAldaflthaWAV--------TVTGAPKLWAMQFIEDHERSPRRWYGGAVGMVGFDGDM 457
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 19113328 658 EFNVIIRSAfkykaddywRIGAG------GAvTIL--SSPEGEYEEMVLKANSILPA 706
Cdd:PRK13566 458 NTGLTLRTI---------RIKDGvaevrvGA-TLLfdSDPEAEEAETELKASALLQA 504
|
|
| PRK09522 |
PRK09522 |
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ... |
10-197 |
3.73e-16 |
|
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate phosphoribosyltransferase TrpD;
Pssm-ID: 181927 [Multi-domain] Cd Length: 531 Bit Score: 82.00 E-value: 3.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 10 ILLIDCYDSYTFNLYDLLYKASENacvIVVHWDKMSPDLWEDIL---QFDAIVVGPGPGHPAE---YSSILNRIwQLNIP 83
Cdd:PRK09522 4 ILLLDNIDSFTYNLADQLRSNGHN---VVIYRNHIPAQTLIERLatmSNPVLMLSPGPGVPSEagcMPELLTRL-RGKLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 84 VMGICLGFQSLALYHGATIERMPNLpWHGRVSSVTTSKTFIFDGIS-AVKGMRYHSLYANKIPiDSLQILAQSdeDNIVM 162
Cdd:PRK09522 80 IIGICLGHQAIVEAYGGYVGQAGEI-LHGKASSIEHDGQAMFAGLTnPLPVARYHSLVGSNIP-AGLTINAHF--NGMVM 155
|
170 180 190
....*....|....*....|....*....|....*
gi 19113328 163 SIKATKFPHFGILYHPESVGSSKSLKIFKNFLSLA 197
Cdd:PRK09522 156 AVRHDADRVCGFQFHPESILTTQGARLLEQTLAWA 190
|
|
| GATase1_CPSase |
cd01744 |
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
10-194 |
6.22e-16 |
|
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This group of sequences represents the small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II. CPSase II catalyzes the production of carbomyl phosphate (CP) from bicarbonate, glutamine and two molecules of MgATP. The reaction is believed to proceed by a series of four biochemical reactions involving a minimum of three discrete highly reactive intermediates. The synthesis of CP is critical for the initiation of two separate biosynthetic pathways. In one CP is coupled to aspartate, its carbon and nitrogen nuclei ultimately incorporated into the aromatic moieties of pyrimidine nucleotides. In the second pathway CP is condensed with ornithine at the start of the urea cycle and is utilized for the detoxification of ammonia and biosynthesis of arginine. CPSases may be encoded by one or by several genes, depending on the species. The E.coli enzyme is a heterodimer consisting of two polypeptide chains referred to as the small and large subunit. Ammonia an intermediate during the biosynthesis of carbomyl phosphate produced by the hydrolysis of glutamine in the small subunit of the enzyme is delivered via a molecular tunnel between the remotely located carboxyphosphate active site in the large subunit. CPSase IIs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. This group also contains the sequence from the mammalian urea cycle form which has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I.
Pssm-ID: 153215 [Multi-domain] Cd Length: 178 Bit Score: 76.38 E-value: 6.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 10 ILLIDCYDSYtfNLYDLLykaSENAC-VIVVHWDkmSPDLWEDILQFDAIVVGPGPGHPAEYSSILNRIWQL---NIPVM 85
Cdd:cd01744 1 VVVIDFGVKH--NILREL---LKRGCeVTVVPYN--TDAEEILKLDPDGIFLSNGPGDPALLDEAIKTVRKLlgkKIPIF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 86 GICLGFQSLALYHGATIERMP------NLPwhgrVSSVTTSKTFIfdgISAVKGmryhslYAnkIPIDSLQ----ILAQS 155
Cdd:cd01744 74 GICLGHQLLALALGAKTYKMKfghrgsNHP----VKDLITGRVYI---TSQNHG------YA--VDPDSLPggleVTHVN 138
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 19113328 156 DEDNIVMSIKATKFPHFGILYHPE-SVGSSKSLKIFKNFL 194
Cdd:cd01744 139 LNDGTVEGIRHKDLPVFSVQFHPEaSPGPHDTEYLFDEFL 178
|
|
| MenF |
COG1169 |
Isochorismate synthase EntC [Coenzyme transport and metabolism, Secondary metabolites ... |
438-707 |
1.07e-15 |
|
Isochorismate synthase EntC [Coenzyme transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; Isochorismate synthase EntC is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440783 [Multi-domain] Cd Length: 353 Bit Score: 79.04 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 438 VQSFPKKEVYCESVKACQEHLLAGDSYEMCLTDTTFVSAPPELSDFEMYMRARSLNPA--TFAgfVRLNHF-TLLCCSPE 514
Cdd:COG1169 82 RRGVPDPAEWREAVAQALEAIRAGELDKVVLARALDLTLDEPIDPRALLARLRRRNPDcyTFA--VELGAGdGFVGASPE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 515 RFLQfRDDRCLFS-PIKGTLKREGhmSLEEARK---KLLN-EKDMGELNMIIDLIRNDLHQLAKknSVHVPELYSVEEHS 589
Cdd:COG1169 160 RLVR-RRGGQLTTeALAGTAPRGA--DPEEDAAlaaALLAsEKDRREHALVVDSIREALAPLCS--SLDVPEEPELLRLR 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 590 NVYSLLSNIYGRIESPITAWDVLSKSFPPGSMTGAPKLRSVRMLEPLEQHGRGIYSGTLGYWDVTGSAEFNVIIRSAfky 669
Cdd:COG1169 235 NVQHLATPITGTLDPGVSALDLAAALHPTPAVGGTPREAALALIRELEPFDRGWYAGPVGWVDADGDGEFAVAIRSA--- 311
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 19113328 670 kaddywRI---------GAGgavtIL--SSPEGEYEEMVLKANSILPAF 707
Cdd:COG1169 312 ------LIdgnrarlfaGAG----IVagSDPEAEWAETEAKLRTMLRAL 350
|
|
| PRK07912 |
PRK07912 |
salicylate synthase; |
486-708 |
1.09e-14 |
|
salicylate synthase;
Pssm-ID: 169151 [Multi-domain] Cd Length: 449 Bit Score: 77.14 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 486 YMRARSLNPATFAGFVRLNHFTLLCCSPERFLQFRDDRCLFS-PIKGT--LKReGHMSLEEARKKLL-NEKDMGELNMII 561
Cdd:PRK07912 223 YRLGRRHNTPVRSFLLRLGGIRALGYSPELVTAVRADGVVITePLAGTraFGR-GAAIDRLARDDLEsNSKEIVEHAISV 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 562 DLIRNDLHQLAKKNSVHVPELYSVEEHSNVYSLLSNIYGRIESPITAWDVLSKSFPPGSMTGAPKLRSVRMLEPLEQHGR 641
Cdd:PRK07912 302 RSSLAEITEIAEPGSAAVIDFMTVRERGSVQHLGSTVRGRLDASSDRMDALEALFPAVTASGIPKAAGVDAIFRLDEAPR 381
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19113328 642 GIYSGTLGYWDVTGSAEFNVIIRSAFKYKADDYWRIGAGgaVTILSSPEGEYEEMVLKANSILPAFV 708
Cdd:PRK07912 382 GLYSGAVVMLSADGGLDAALTLRAAYQVGGRTWLRAGAG--IIEESEPEREFEETCEKLSTLAPYLV 446
|
|
| PRK06772 |
PRK06772 |
salicylate synthase; |
512-705 |
1.79e-12 |
|
salicylate synthase;
Pssm-ID: 102546 [Multi-domain] Cd Length: 434 Bit Score: 70.15 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 512 SPERFLQFRDDRCLFSPIKGTLKREGHMSLEEARKK--LLNEKDMGELNMIIDLIRNDLHQLAKKNSVHVPELYSVEEHS 589
Cdd:PRK06772 238 SPELVMSVTGNKVVTEPLAGTRDRMGNPEHNKAKEAelLHDSKEVLEHILSVKEAIAELEAVCQPGSVVVEDLMSVRQRG 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 590 NVYSLLSNIYGRIESPITAWDVLSKSFPPGSMTGAPKLRSVRMLEPLEQHGRGIYSGTLGYWDVTgSAEFNVIIRSAFKy 669
Cdd:PRK06772 318 SVQHLGSGVSGQLAENKDAWDAFTVLFPSITASGIPKNAALNAIMQIEKTPRELYSGAILLLDDT-RFDAALVLRSVFQ- 395
|
170 180 190
....*....|....*....|....*....|....*.
gi 19113328 670 KADDYWrIGAGGAVTILSSPEGEYEEMVLKANSILP 705
Cdd:PRK06772 396 DSQRCW-IQAGAGIIAQSTPERELTETREKLASIAP 430
|
|
| GATase1_GMP_Synthase |
cd01742 |
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ... |
77-194 |
2.41e-12 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase. GMP synthetase is a glutamine amidotransferase from the de novo purine biosynthetic pathway. Glutamine amidotransferase (GATase) activity catalyse the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. GMP synthetase catalyses the amination of the nucleotide precursor xanthosine 5'-monophosphate to form GMP. GMP synthetase belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.
Pssm-ID: 153213 [Multi-domain] Cd Length: 181 Bit Score: 66.02 E-value: 2.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 77 IWQLNIPVMGICLGFQSLALYHGATIERMPNlPWHGRVSSVTTSKTFIFDGISavKGMRY---HSLYANKIPiDSLQILA 153
Cdd:cd01742 66 IFELGVPVLGICYGMQLIAKALGGKVERGDK-REYGKAEIEIDDSSPLFEGLP--DEQTVwmsHGDEVVKLP-EGFKVIA 141
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 19113328 154 QSDeDNIVMSIKATKFPHFGILYHPESVGSSKSLKIFKNFL 194
Cdd:cd01742 142 SSD-NCPVAAIANEEKKIYGVQFHPEVTHTEKGKEILKNFL 181
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
10-106 |
2.51e-12 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.
Pssm-ID: 153210 [Multi-domain] Cd Length: 115 Bit Score: 64.16 E-value: 2.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 10 ILLIDCYDSYT---FNLYDLLYKAseNACVIVVHWDKMSPDLWEDILQFDAIVVGPGPGHP------AEYSSILNRIWQL 80
Cdd:cd01653 1 VAVLLFPGFEElelASPLDALREA--GAEVDVVSPDGGPVESDVDLDDYDGLILPGGPGTPddlardEALLALLREAAAA 78
|
90 100
....*....|....*....|....*.
gi 19113328 81 NIPVMGICLGFQSLALYHGATIERMP 106
Cdd:cd01653 79 GKPILGICLGAQLLVLGVQFHPEAID 104
|
|
| PRK12838 |
PRK12838 |
carbamoyl phosphate synthase small subunit; Reviewed |
23-106 |
4.89e-12 |
|
carbamoyl phosphate synthase small subunit; Reviewed
Pssm-ID: 183784 [Multi-domain] Cd Length: 354 Bit Score: 67.99 E-value: 4.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 23 LYDLLYKAS------ENAC-VIVVHWDKmSPdlwEDI--LQFDAIVVGPGPGHPAEYSSILNRIWQL--NIPVMGICLGF 91
Cdd:PRK12838 172 LIDFGYKKSilrslsKRGCkVTVLPYDT-SL---EEIknLNPDGIVLSNGPGDPKELQPYLPEIKKLisSYPILGICLGH 247
|
90
....*....|....*
gi 19113328 92 QSLALYHGATIERMP 106
Cdd:PRK12838 248 QLIALALGADTEKLP 262
|
|
| PRK07054 |
PRK07054 |
isochorismate synthase; |
487-699 |
1.79e-11 |
|
isochorismate synthase;
Pssm-ID: 235920 [Multi-domain] Cd Length: 475 Bit Score: 67.10 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 487 MRARSLNPATFAgfVRLNHFTLLCCSPERFLQFRDDRCLFSPIKGTLKREGHmSLEEAR---KKLLNEKDMGELNMIIDL 563
Cdd:PRK07054 239 LRLRDPHAHLFA--FRRGNACFLGATPERLVRVAAGDLHTHALAGTIARGAD-PAEDARlgaALMASAKDRLEHALVVDA 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 564 IRNDLHQLAKKnsVHVPELYSVEEHSNVYSLLSNIYGRIESPITAWDVLSKSFPPGSMTGAPKLRSVRMLEPLEQHGRGI 643
Cdd:PRK07054 316 IRAALAPLSRA--LDIPDQPSLHRLPRLQHLSTPIRATLAPDATLLQVVAALHPTPAVGGHPRAAALDYIRAHEGFDRGW 393
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 19113328 644 YSGTLGYWDVTGSAEFNVIIRSAFkyKADDYWRIGAGGAVTILSSPEGEYEEMVLK 699
Cdd:PRK07054 394 YAAPIGWLDAHGNGDFAVALRSAL--ITGGACRLFAGCGIVADSEPASEYRETCLK 447
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
10-94 |
5.27e-11 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain.
Pssm-ID: 153222 [Multi-domain] Cd Length: 92 Bit Score: 59.52 E-value: 5.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 10 ILLIDCYDSYT---FNLYDLLYKAseNACVIVVHWDKMSPDLWEDILQFDAIVVGPGPGHP------AEYSSILNRIWQL 80
Cdd:cd03128 1 VAVLLFGGSEElelASPLDALREA--GAEVDVVSPDGGPVESDVDLDDYDGLILPGGPGTPddlawdEALLALLREAAAA 78
|
90
....*....|....
gi 19113328 81 NIPVMGICLGFQSL 94
Cdd:cd03128 79 GKPVLGICLGAQLL 92
|
|
| PRK12564 |
PRK12564 |
carbamoyl-phosphate synthase small subunit; |
50-196 |
1.12e-10 |
|
carbamoyl-phosphate synthase small subunit;
Pssm-ID: 237139 [Multi-domain] Cd Length: 360 Bit Score: 63.94 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 50 EDILQF--DAIVVGPGPGHPAEYSSILNRIWQL---NIPVMGICLGFQSLALYHGATIERMP------NLPwhgrVSSVT 118
Cdd:PRK12564 212 EEILALnpDGVFLSNGPGDPAALDYAIEMIRELlekKIPIFGICLGHQLLALALGAKTYKMKfghrgaNHP----VKDLE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 119 TSKTFI------FdgisAVKgmryhslyANKIPiDSLQILAQSDEDNIVMSIKATKFPHFGILYHPE-SVGSSKSLKIFK 191
Cdd:PRK12564 288 TGKVEItsqnhgF----AVD--------EDSLP-ANLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEaSPGPHDSAYLFD 354
|
....*
gi 19113328 192 NFLSL 196
Cdd:PRK12564 355 EFVEL 359
|
|
| CPSaseIIsmall |
TIGR01368 |
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ... |
6-198 |
2.25e-10 |
|
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small chain of the glutamine-dependent form (EC 6.3.5.5) of carbamoyl phosphate synthase, CPSase II. The C-terminal domain has glutamine amidotransferase activity. Note that the sequence from the mammalian urea cycle form has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I (EC 6.3.4.16). CPSases of pyrimidine biosynthesis, arginine biosynthesis, and the urea cycle may be encoded by one or by several genes, depending on the species. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273580 [Multi-domain] Cd Length: 357 Bit Score: 63.03 E-value: 2.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 6 NRLQILLIDCydSYTFNLYDLLykASENACVIVVHWDkmSPdlWEDILQF--DAIVVGPGPGHPAEYSSILNRIWQL--N 81
Cdd:TIGR01368 171 KGKRVVVIDF--GVKRNILRRL--VKRGCEVTVVPYD--TD--AEEIKKYnpDGIFLSNGPGDPAAVEPAIETIRKLleK 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 82 IPVMGICLGFQSLALYHGATIERMP------NLPwhgrVSSVTTSKTFI------FdgisAVKGmryhslyaNKIPIDSL 149
Cdd:TIGR01368 243 IPIFGICLGHQLLALAFGAKTYKMKfghrggNHP----VKDLITGRVEItsqnhgY----AVDP--------DSLPAGDL 306
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 19113328 150 QILAQSDEDNIVMSIKATKFPHFGILYHPE-SVGSSKSLKIFKNFLSLAD 198
Cdd:TIGR01368 307 EVTHVNLNDGTVEGIRHKDLPVFSVQYHPEaSPGPHDTEYLFDEFIDLMK 356
|
|
| CarA |
COG0505 |
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
50-196 |
3.63e-10 |
|
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase small subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440271 [Multi-domain] Cd Length: 361 Bit Score: 62.35 E-value: 3.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 50 EDILQF--DAIVVGPGPGHPAEYSSILNRIWQL---NIPVMGICLGFQSLALYHGATIERMP------NLPwhgrVSSVT 118
Cdd:COG0505 211 EEILALnpDGVFLSNGPGDPAALDYAIETIRELlgkGIPIFGICLGHQLLALALGAKTYKLKfghrgaNHP----VKDLE 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 119 TSKTFI------FdgisAVKGmryhslyankipiDSLqilaqsDEDNIVMS-----------IKATKFPHFGILYHPE-S 180
Cdd:COG0505 287 TGRVEItsqnhgF----AVDE-------------DSL------PATDLEVThvnlndgtvegLRHKDLPAFSVQYHPEaS 343
|
170
....*....|....*.
gi 19113328 181 VGSSKSLKIFKNFLSL 196
Cdd:COG0505 344 PGPHDSAYLFDRFIEL 359
|
|
| carA |
CHL00197 |
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional |
4-197 |
4.47e-10 |
|
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
Pssm-ID: 214392 [Multi-domain] Cd Length: 382 Bit Score: 62.12 E-value: 4.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 4 ISNRLQILLIDcydsYTFNLYDLLYKASENACVIVVhwDKMSPdlWEDILQF--DAIVVGPGPGHPAEYSSILNRIWQL- 80
Cdd:CHL00197 189 SSYQLKIIVID----FGVKYNILRRLKSFGCSITVV--PATSP--YQDILSYqpDGILLSNGPGDPSAIHYGIKTVKKLl 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 81 --NIPVMGICLGFQSLALYHGATI------ERMPNLP--WHGRVSsvTTSKTFIFdgisAVKgmrYHSLYANKIPIDSLQ 150
Cdd:CHL00197 261 kyNIPIFGICMGHQILSLALEAKTfklkfgHRGLNHPsgLNQQVE--ITSQNHGF----AVN---LESLAKNKFYITHFN 331
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 19113328 151 IlaqsdEDNIVMSIKATKFPHFGILYHPE-SVGSSKSLKIFKNFLSLA 197
Cdd:CHL00197 332 L-----NDGTVAGISHSPKPYFSVQYHPEaSPGPHDADYLFEYFIEII 374
|
|
| PRK15016 |
PRK15016 |
isochorismate synthase EntC; Provisional |
493-707 |
1.61e-09 |
|
isochorismate synthase EntC; Provisional
Pssm-ID: 184977 [Multi-domain] Cd Length: 391 Bit Score: 60.27 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 493 NPATFAGFVRL-NHFTLLCCSPErfLQFRDDRCLFS--PIKGTLKREGHMSLE-EARKKLL-NEKDMGELNMII----DL 563
Cdd:PRK15016 175 NPVSYNFHVPLaDGGVLLGASPE--LLLRKDGERFSslPLAGSARRQPDEVLDrEAGNRLLaSEKDRHEHELVTqamkEV 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 564 IRNDLHQLAKKNSvhvPELYSVeehSNVYSLLSNIYGRIESPITAWDVLSKSFPPGSMTGAPKLRSVRMLEPLEQHGRGI 643
Cdd:PRK15016 253 LRERSSELHVPSS---PQLITT---PTLWHLATPFEGKANAQENALTLACLLHPTPALSGFPHQAAKQVIAELEPFDREL 326
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19113328 644 YSGTLGYWDVTGSAEFNVIIRSAFKYKadDYWRIGAGGAVTILSSPEGEYEEMVLKANSILPAF 707
Cdd:PRK15016 327 FGGIVGWCDSEGNGEWVVTIRCAKLRE--NQVRLFAGAGIVPASSPLGEWRETGVKLSTMLNVF 388
|
|
| GuaA1 |
COG0518 |
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ... |
10-106 |
2.50e-08 |
|
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP synthase, glutamine amidotransferase domain is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 440284 [Multi-domain] Cd Length: 225 Bit Score: 54.95 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 10 ILLIDC---YDSYTFNLYDLLYKASENACVIVVHWDKMSPDLWeDILQFDAIVV--GP-----GPGHPAEYSSILNRIWQ 79
Cdd:COG0518 2 ILILDHdpfGGQYPGLIARRLREAGIELDVLRVYAGEILPYDP-DLEDPDGLILsgGPmsvydEDPWLEDEPALIREAFE 80
|
90 100
....*....|....*....|....*..
gi 19113328 80 LNIPVMGICLGFQSLALYHGATIERMP 106
Cdd:COG0518 81 LGKPVLGICYGAQLLAHALGGKVEPGP 107
|
|
| PRK00758 |
PRK00758 |
GMP synthase subunit A; Validated |
50-196 |
5.04e-08 |
|
GMP synthase subunit A; Validated
Pssm-ID: 179112 [Multi-domain] Cd Length: 184 Bit Score: 53.32 E-value: 5.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 50 EDILQF-DAIVVGPGP-----GHPAEYssilnrIWQLNIPVMGICLGFQSLALYHGATIERmPNLPWHGRVSSVTTSKTF 123
Cdd:PRK00758 36 EEIKAFeDGLILSGGPdieraGNCPEY------LKELDVPILGICLGHQLIAKAFGGEVGR-GEYGEYALVEVEILDEDD 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19113328 124 IFDGISavKGMRYHSLYAN--KIPIDSLQILAQSDednI--VMSIKATKFPHFGILYHPESVGSSKSLKIFKNFLSL 196
Cdd:PRK00758 109 ILKGLP--PEIRVWASHADevKELPDGFEILARSD---IceVEAMKHKEKPIYGVQFHPEVAHTEYGEEIFKNFLEI 180
|
|
| PLN02786 |
PLN02786 |
isochorismate synthase |
512-700 |
9.46e-08 |
|
isochorismate synthase
Pssm-ID: 178383 [Multi-domain] Cd Length: 533 Bit Score: 55.17 E-value: 9.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 512 SPERFLQfRDDRCLFS-PIKGTLKREGHMS--LEEARKKLLNEKDMGELNMIIDLIRNDLHQLAKKnsVHVPELYSVEEH 588
Cdd:PLN02786 330 TPEQLFH-RKGLGVCSeALAATRPRGGSSArdLQIELDLLTSPKDDLEFSIVRENIREKLEAICDR--VVVEPHKAIRKL 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 589 SNVYSLLSNIYGRIESPITAWDVLSKSFPPGSMTGAPKLRSVRMLEPLEQHGRGIYSGTLGyWDVTGSAEFNVIIRSAFK 668
Cdd:PLN02786 407 ARVQHLYAQLAGRLRSEDDEFDILAALHPTPAVCGHPTEEARLLIAETESFDRGMYAGPVG-WFGGGESEFAVGIRSALV 485
|
170 180 190
....*....|....*....|....*....|..
gi 19113328 669 YKADDYWrIGAGGAVTILSSPEGEYEEMVLKA 700
Cdd:PLN02786 486 EKGLGAL-IYAGTGIVEGSNPSSEWNELELKI 516
|
|
| guaA |
PRK00074 |
GMP synthase; Reviewed |
76-194 |
1.15e-07 |
|
GMP synthase; Reviewed
Pssm-ID: 234614 [Multi-domain] Cd Length: 511 Bit Score: 55.05 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 76 RIWQLNIPVMGICLGFQSLALYHGATIERMPNlPWHGRVSSVTTSKTFIFDGISAVKG--MRyHSLYANKIPiDSLQILA 153
Cdd:PRK00074 70 EIFELGVPVLGICYGMQLMAHQLGGKVERAGK-REYGRAELEVDNDSPLFKGLPEEQDvwMS-HGDKVTELP-EGFKVIA 146
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 19113328 154 QSDEDNI-VMSIKATKFphFGILYHPESVGSSKSLKIFKNFL 194
Cdd:PRK00074 147 STENCPIaAIANEERKF--YGVQFHPEVTHTPQGKKLLENFV 186
|
|
| IMP_synth_hisH |
TIGR01855 |
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ... |
50-196 |
2.15e-07 |
|
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model represents the glutamine amidotransferase subunit (or domain, in eukaryotic systems) of imidazole glycerol phosphate synthase. This subunit catalyzes step 5 of histidine biosynthesis from PRPP. The other subunit, the cyclase, catalyzes step 6. [Amino acid biosynthesis, Histidine family]
Pssm-ID: 273836 [Multi-domain] Cd Length: 196 Bit Score: 51.94 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 50 EDILQFDAIVVgPGPGH-PAEYSSILNRIWQLNI--------PVMGICLGFQ-------------SLALYHGATI----E 103
Cdd:TIGR01855 32 KEAELADKLIL-PGVGAfGAAMARLRENGLDLFVelvvrlgkPVLGICLGMQllferseegggvpGLGLIKGNVVkleaR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 104 RMPNLPWHgRVSSVTTSKtfIFDGISavKGMRY---HSLYankipidslqilAQSDEDNIVMSIK-ATKFPH-------F 172
Cdd:TIGR01855 111 KVPHMGWN-EVHPVKESP--LLNGID--EGAYFyfvHSYY------------AVCEEEAVLAYADyGEKFPAavqkgniF 173
|
170 180
....*....|....*....|....
gi 19113328 173 GILYHPESVGsSKSLKIFKNFLSL 196
Cdd:TIGR01855 174 GTQFHPEKSG-KTGLKLLENFLEL 196
|
|
| GATase1_2 |
cd01745 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
73-193 |
2.82e-07 |
|
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.
Pssm-ID: 153216 [Multi-domain] Cd Length: 189 Bit Score: 51.42 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 73 ILNRIWQLNIPVMGICLGFQSLALYHGATIERmpnlpwHGRVSSvttsktfifdgisavkgmrYHSlYANKIPIDSLQIL 152
Cdd:cd01745 92 LLRAALERGKPILGICRGMQLLNVALGGTLYQ------DIRVNS-------------------LHH-QAIKRLADGLRVE 145
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 19113328 153 AQSdEDNIVMSIKATKFP-HFGILYHPES--VGSSKSLKIFKNF 193
Cdd:cd01745 146 ARA-PDGVIEAIESPDRPfVLGVQWHPEWlaDTDPDSLKLFEAF 188
|
|
| GATase1_1 |
cd01741 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
10-194 |
8.35e-07 |
|
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.
Pssm-ID: 153212 [Multi-domain] Cd Length: 188 Bit Score: 49.94 E-value: 8.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 10 ILLIDCYDSYTF-NLYDLLYKASENACVIVVhWDKMSPDLWEDILQFDAIVVGPGPGHP--AEYSSI------LNRIWQL 80
Cdd:cd01741 2 ILILQHDTPEGPgLFEDLLREAGAETIEIDV-VDVYAGELLPDLDDYDGLVILGGPMSVdeDDYPWLkklkelIRQALAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 81 NIPVMGICLGFQSLALYHGATIERMPNlPWHGRVSSVTTSKTFIFDGISAVKGMRYHSLYANK-----IPIDSlQILAQS 155
Cdd:cd01741 81 GKPVLGICLGHQLLARALGGKVGRNPK-GWEIGWFPVTLTEAGKADPLFAGLPDEFPVFHWHGdtvveLPPGA-VLLASS 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 19113328 156 DEDNI-VMSIKATkfpHFGILYHPESvgsskslKIFKNFL 194
Cdd:cd01741 159 EACPNqAFRYGDR---ALGLQFHPEE-------RLLRNFL 188
|
|
| GATase1_IGP_Synthase |
cd01748 |
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ... |
50-194 |
1.64e-06 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS); Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS). IGPS incorporates ammonia derived from glutamine into N1-[(5'-phosphoribulosyl)-formimino]-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to form 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR) and imidazole glycerol phosphate (IGP). The glutamine amidotransferase domain generates the ammonia nucleophile which is channeled from the glutaminase active site to the PRFAR active site. IGPS belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.
Pssm-ID: 153219 [Multi-domain] Cd Length: 198 Bit Score: 49.42 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 50 EDILQFDAIVVgPGPGH--PA-------EYSSILNRIWQLNIPVMGICLGFQSLA-------------LYHGaTIERMPN 107
Cdd:cd01748 32 EEILSADKLIL-PGVGAfgDAmanlrerGLIEALKEAIASGKPFLGICLGMQLLFesseegggtkglgLIPG-KVVRFPA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 108 LP--------WHgRVSSVTTSKtfIFDGISavKGMRY---HSLYAnkIPIDSLQILAQSD----------EDNIVmsikA 166
Cdd:cd01748 110 SEglkvphmgWN-QLEITKESP--LFKGIP--DGSYFyfvHSYYA--PPDDPDYILATTDyggkfpaaveKDNIF----G 178
|
170 180 190
....*....|....*....|....*....|..
gi 19113328 167 TKFphfgilyHPEsvgssKS----LKIFKNFL 194
Cdd:cd01748 179 TQF-------HPE-----KSgkagLKLLKNFL 198
|
|
| PLN02347 |
PLN02347 |
GMP synthetase |
81-194 |
2.85e-04 |
|
GMP synthetase
Pssm-ID: 215197 [Multi-domain] Cd Length: 536 Bit Score: 43.90 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 81 NIPVMGICLGFQSLALYHGATIE--------RMPnlpwhgrVSSVTTSKTFIFDGISAVKGM-RYHSLYANKIPiDSLQI 151
Cdd:PLN02347 86 GVPVLGICYGMQLIVQKLGGEVKpgekqeygRME-------IRVVCGSQLFGDLPSGETQTVwMSHGDEAVKLP-EGFEV 157
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 19113328 152 LAQSDEDNIVmSIKATKFPHFGILYHPESVGSSKSLKIFKNFL 194
Cdd:PLN02347 158 VAKSVQGAVV-AIENRERRIYGLQYHPEVTHSPKGMETLRHFL 199
|
|
| HisH |
COG0118 |
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ... |
50-191 |
2.36e-03 |
|
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid transport and metabolism]; Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH is part of the Pathway/BioSystem: Histidine biosynthesis
Pssm-ID: 439888 [Multi-domain] Cd Length: 196 Bit Score: 39.64 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 50 EDILQFDAIVVgPGPGH---------PAEYSSILNRIWQLNIPVMGICLGFQSLALY---HGAT---------IERMPN- 107
Cdd:COG0118 34 DEIRAADRLVL-PGVGAfgdamenlrERGLDEAIREAVAGGKPVLGICLGMQLLFERseeNGDTeglglipgeVVRFPAs 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 108 ---LP---WhGRVSSVTTSKtfIFDGISA------VkgmryHSLYAnkIPIDSLQILAQSD----------EDNIVmsik 165
Cdd:COG0118 113 dlkVPhmgW-NTVEIAKDHP--LFAGIPDgeyfyfV-----HSYYV--PPDDPEDVVATTDygvpftaaveRGNVF---- 178
|
170 180 190
....*....|....*....|....*....|
gi 19113328 166 ATKFphfgilyHPEsvgssKS----LKIFK 191
Cdd:COG0118 179 GTQF-------HPE-----KSgaagLRLLK 196
|
|
| hisH |
PRK13170 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
77-196 |
3.94e-03 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 183877 [Multi-domain] Cd Length: 196 Bit Score: 39.07 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113328 77 IWQLNIPVMGICLGFQSLALY---HGAT---------IERMP--NLP-----WhgrvSSVTTSKT-FIFDGISAvkGMRY 136
Cdd:PRK13170 66 IKACTQPVLGICLGMQLLGERseeSGGVdclgiidgpVKKMTdfGLPlphmgW----NQVTPQAGhPLFQGIED--GSYF 139
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19113328 137 ---HSlYAnkIPIDSLQIlAQSDEDNIVMS-IKATKFphFGILYHPESVGSSKSlKIFKNFLSL 196
Cdd:PRK13170 140 yfvHS-YA--MPVNEYTI-AQCNYGEPFSAaIQKDNF--FGVQFHPERSGAAGA-QLLKNFLEM 196
|
|
| |
