|
Name |
Accession |
Description |
Interval |
E-value |
| FadE_coli |
NF038187 |
acyl-CoA dehydrogenase FadE; This HMM describes a narrow clade of medium-chain and long-chain ... |
3-814 |
0e+00 |
|
acyl-CoA dehydrogenase FadE; This HMM describes a narrow clade of medium-chain and long-chain acyl-CoA dehydrogenases that includes YafH from Escherichia coli K-12 and Salmonella enterica LT2 (also called FadF), now called FadE.
Pssm-ID: 439499 [Multi-domain] Cd Length: 816 Bit Score: 1819.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 3 ILSILATVVLLGALFYHRVSLFISSLILLAWTAALGVAGLWSAWVLVPLAIILVPFNFAPMRKSMISAPVFRGFRKVMPP 82
Cdd:NF038187 1 LLSILAMLVLLGALAYHRVSLLTSSLILAAVMAAGTAAGLWSLWLWLPFLIIALPLNVPSIRQSLISAPALKAFRKVMPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 83 MSRTEKEAIDAGTTWWEGDLFQGKPDWKKLHNYPQPRLTAEEQAFLDGPVEEACRMANDFQITHELADLPPELWAYLKEH 162
Cdd:NF038187 81 MSSTEKEAIDAGTTWWEADLFRGNPDWKKLHNYPKPRLTAEEQAFLDGPVEEVCRMVNDFQITHELADLPPEVWQYLKDH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 163 RFFAMIIKKEYGGLEFSAYAQSRVLQKLSGVSGILAITVGVPNSLGPGELLQHYGTDEQKDHYLPRLARGQEIPCFALTS 242
Cdd:NF038187 161 RFFAMIIKKEYGGLEFSAYAQSRVLQKLAGVSSILASTVGVPNSLGPGELLQHYGTEEQKDHYLPRLARGEEIPCFALTS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 243 PEAGSDAGAIPDTGIVCMGEWQGQQVLGMRLTWNKRYITLAPIATVLGLAFKLSDPEKLLGGAEDLGITCALIPTTTPGV 322
Cdd:NF038187 241 PEAGSDAGSIPDFGVVCKGEWQGEEVLGMRLTWNKRYITLAPVATVLGLAFKLRDPDHLLGDKEELGITCALIPTDTPGV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 323 EIGRRHFPLNVPFQNGPTRGKDVFVPIDYIIGGPKMAGQGWRMLVECLSVGRGITLPSNSTGGVKSVALATGAYAHIRRQ 402
Cdd:NF038187 321 EIGRRHFPLNVPFQNGPTRGKDIFVPLDFIIGGPKMAGQGWRMLVECLSVGRGITLPSNSTGGLKSAALATGAYARIRRQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 403 FKISIGKMEGIEEPLARIAGNAYVMDAAASLITYGIMLGEKPAVLSAIVKYHCTHRGQQSIIDAMDITGGKGIMLGQSNF 482
Cdd:NF038187 401 FKLPIGKMEGIEEPLARIAGNAYLMDAAATLTTTGIDLGEKPSVISAIVKYHCTHRGQRSIIDAMDIHGGKGICLGPNNF 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 483 LARAYQGAPIAITVEGANILTRSMMIFGQGAIRCHPYVLEEMEAAKNND----VNAFDKLLFKHIGHVGSNKVRSFWLGL 558
Cdd:NF038187 481 LARGYQGAPIAITVEGANILTRSMIIYGQGAIRCHPYVLAEMEAAQDNDseqaLNDFDKALFGHIGFVGSNLVRSFWLGL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 559 TRGLTSSTPTGDATKRYYQHLNRLSANLALLSDVSMAVLGGSLKRRERISARLGDILSQLYLASAVLKRYDDEGRNEADL 638
Cdd:NF038187 561 TNGRFSSAPYKDATRRYYQQLNRLSANLALLSDVSMAVLGGSLKRRERISARLGDILSQLYLASATLKRYEDEGRQKEDL 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 639 PLVHWGVQDALYQAEQAMDDLLQNFPNRVVAGLLNVVIFPTGRHYLAPSDKLDHKVAKILQVPNATRSRIGRGQYLTPSE 718
Cdd:NF038187 641 PLVHWAVQDSLYQAEQALDDLLRNFPNRLVAGLLRVIIFPFGRPLKAPSDKLDHKVAKILQTPSATRSRLGRGQYLTPSE 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 719 HNPVGLLEEALVDVIAADPIHQRICKELGKNLPFTRLDELAHNALVKGLIDKDEAAILVKAEESRLRSINVDDFDPEELA 798
Cdd:NF038187 721 HNPVGLLEQALKDILAAEPIHDRVCKAAGKRLPFMRLDKLAEEGLALGVITEEEAALLERAEASRLRSINVDDFDPDELA 800
|
810
....*....|....*.
gi 90111100 799 TKPVKLPEKVRKVEAA 814
Cdd:NF038187 801 AKPAKRPAKQKQDEAA 816
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
42-814 |
0e+00 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 1598.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 42 LWSAWVLVPLAIILVPFNFAPMRKSMISAPVFRGFRKVMPPMSRTEKEAIDAGTTWWEGDLFQGKPDWKKLHNYPQPRLT 121
Cdd:PRK09463 1 LWSLWLLVPLAIILLPLNLPPLRRSLISAPLLKWFRKVLPPMSQTEREALEAGTVWWEGELFSGKPDWKKLLNYPKPTLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 122 AEEQAFLDGPVEEACRMANDFQITHELADLPPELWAYLKEHRFFAMIIKKEYGGLEFSAYAQSRVLQKLSGVSGILAITV 201
Cdd:PRK09463 81 AEEQAFLDGPVEELCRMVNDWQITHELADLPPEVWQFIKEHGFFGMIIPKEYGGLEFSAYAHSRVLQKLASRSGTLAVTV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 202 GVPNSLGPGELLQHYGTDEQKDHYLPRLARGQEIPCFALTSPEAGSDAGAIPDTGIVCMGEWQGQQVLGMRLTWNKRYIT 281
Cdd:PRK09463 161 MVPNSLGPGELLLHYGTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGSIPDTGVVCKGEWQGEEVLGMRLTWNKRYIT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 282 LAPIATVLGLAFKLSDPEKLLGGAEDLGITCALIPTTTPGVEIGRRHFPLNVPFQNGPTRGKDVFVPIDYIIGGPKMAGQ 361
Cdd:PRK09463 241 LAPIATVLGLAFKLYDPDGLLGDKEDLGITCALIPTDTPGVEIGRRHFPLNVPFQNGPTRGKDVFIPLDYIIGGPKMAGQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 362 GWRMLVECLSVGRGITLPSNSTGGVKSVALATGAYAHIRRQFKISIGKMEGIEEPLARIAGNAYVMDAAASLITYGIMLG 441
Cdd:PRK09463 321 GWRMLMECLSVGRGISLPSNSTGGAKLAALATGAYARIRRQFKLPIGKFEGIEEPLARIAGNAYLMDAARTLTTAAVDLG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 442 EKPAVLSAIVKYHCTHRGQQSIIDAMDITGGKGIMLGQSNFLARAYQGAPIAITVEGANILTRSMMIFGQGAIRCHPYVL 521
Cdd:PRK09463 401 EKPSVLSAIAKYHLTERGRQVINDAMDIHGGKGICLGPNNFLARAYQAAPIAITVEGANILTRSLMIFGQGAIRCHPYVL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 522 EEMEAAKNND---VNAFDKLLFKHIGHVGSNKVRSFWLGLTRGLTSSTPTGDATKRYYQHLNRLSANLALLSDVSMAVLG 598
Cdd:PRK09463 481 KEMEAAQNNDkqaLKAFDKALFGHIGFVVSNAVRSFWLGLTGGRLSAAPVDDATKRYYRQLNRLSANLALLADVSMLVLG 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 599 GSLKRRERISARLGDILSQLYLASAVLKRYDDEGRNEADLPLVHWGVQDALYQAEQAMDDLLQNFPNRVVAGLLNVVIFP 678
Cdd:PRK09463 561 GSLKRRERLSARLGDILSQLYLASAVLKRYEDEGRPEADLPLVHWAVQDALYQAEQALDGLLRNFPNRVVAGLLRVLVFP 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 679 TGRHYLAPSDKLDHKVAKILQVPNATRSRIGRGQYLTPSEHNPVGLLEEALVDVIAADPIHQRICKELGKN-LPFTRLDE 757
Cdd:PRK09463 641 LGRRYRAPSDKLDHQVAKLLQTPSATRDRLTRGQYLPPSENNPVGRLEEALLDVIAAEPIEKKICKALKKGkLPFLRLDE 720
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 90111100 758 LAHNALVKGLIDKDEAAILVKAEESRLRSINVDDFDPEELATKPVKLPEKVRKVEAA 814
Cdd:PRK09463 721 LADEALAAGVISEEEAALLREAEEARLRVINVDDFDPEELAAKPVKLPEKVQKVEAA 777
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
45-797 |
0e+00 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 1210.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 45 AWVLVPLAIILVPFNFAPMRKSMISAPVFRGFRKVMPPMSRTEKEAIDAGTTWWEGDLFQGKPDWKKLHNYPQPRLTAEE 124
Cdd:PRK13026 3 TLIILLLIAIVLVFAVKPLRRQFITRPVFKFFKKVLPPLSDTEREAMEAGDVWWEGELFSGKPDWQKLHSYPKPTLTAEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 125 QAFLDGPVEEACRMANDFQITHELADLPPELWAYLKEHRFFAMIIKKEYGGLEFSAYAQSRVLQKLSGVSGILAITVGVP 204
Cdd:PRK13026 83 QAFIDNEVETLLTMLDDWDIVQNRKDLPPEVWDYLKKEGFFALIIPKEYGGKGFSAYANSTIVSKIATRSVSAAVTVMVP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 205 NSLGPGELLQHYGTDEQKDHYLPRLARGQEIPCFALTSPEAGSDAGAIPDTGIVCMGEWQGQQVLGMRLTWNKRYITLAP 284
Cdd:PRK13026 163 NSLGPGELLTHYGTQEQKDYWLPRLADGTEIPCFALTGPEAGSDAGAIPDTGIVCRGEFEGEEVLGLRLTWDKRYITLAP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 285 IATVLGLAFKLSDPEKLLGGAEDLGITCALIPTTTPGVEIGRRHFPLNVPFQNGPTRGKDVFVPIDYIIGGPKMAGQGWR 364
Cdd:PRK13026 243 VATVLGLAFKLRDPDGLLGDKKELGITCALIPTDHPGVEIGRRHNPLGMAFMNGTTRGKDVFIPLDWIIGGPDYAGRGWR 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 365 MLVECLSVGRGITLPSNSTGGVKSVALATGAYAHIRRQFKISIGKMEGIEEPLARIAGNAYVMDAAASLITYGIMLGEKP 444
Cdd:PRK13026 323 MLVECLSAGRGISLPALGTASGHMATRTTGAYAYVRRQFGMPIGQFEGVQEALARIAGNTYLLEAARRLTTTGLDLGVKP 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 445 AVLSAIVKYHCTHRGQQSIIDAMDITGGKGIMLGQSNFLARAYQGAPIAITVEGANILTRSMMIFGQGAIRCHPYVLEEM 524
Cdd:PRK13026 403 SVVTAIAKYHMTELARDVVNDAMDIHAGKGIQLGPKNYLGHAYMAVPIAITVEGANILTRNLMIFGQGATRCHPYVLAEM 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 525 EAAKNND----VNAFDKLLFKHIGHVGSNKVRSFWLGLTRGLTSSTPTGDATKRYYQHLNRLSANLALLSDVSMAVLGGS 600
Cdd:PRK13026 483 EAAAMEDehegLEAFDSLLFKHIGYAARNAFRALFSALTGSRFISAPVSGETAQYYKDMSRLSAALALLADLSMLILGGD 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 601 LKRRERISARLGDILSQLYLASAVLKRYDDEGRNEADLPLVHWGVQDALYQAEQAMDDLLQNFPNRVVAGLLNVVIFPTG 680
Cdd:PRK13026 563 LKRKEMLSARLGDVLSQLYLASATLKRFEDNGRQQDDLPAVHYAMQDCLHLAAKALDEFLRNFPNRPVAWLLRALIFPLG 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 681 RHYLAPSDKLDHKVAKILQVPNATRSRIGRGQYLTPSEHNPVGLLEEALVDVIAADPIHQRICKEL--GKNLPFTRLDEL 758
Cdd:PRK13026 643 NHFRAPSDKLARQLAELMMTPGPARDRLTALCYIFEGDKDGVARVEQAFLAQYAVKPLYKKLKKAQreGKLPRKVPLLEL 722
|
730 740 750
....*....|....*....|....*....|....*....
gi 90111100 759 AHNALVKGLIDKDEAAILVKAEESRLRSINVDDFDPEEL 797
Cdd:PRK13026 723 FAKALEKGVITADEAEKLLAADKLRLDAIQVDDFTPDFM 761
|
|
| ACDH_C |
pfam09317 |
Acyl-CoA dehydrogenase, C-terminal, bacterial type; This C-terminal domain is functionally ... |
514-792 |
3.28e-160 |
|
Acyl-CoA dehydrogenase, C-terminal, bacterial type; This C-terminal domain is functionally uncharacterized and is predominantly found in various prokaryotic acyl-coenzyme A dehydrogenases and seems to be essential for its function.
Pssm-ID: 430522 [Multi-domain] Cd Length: 284 Bit Score: 466.97 E-value: 3.28e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 514 IRCHPYVLEEMEAAKNND----VNAFDKLLFKHIGHVGSNKVRSFWLGLTRGLTSSTPTGDATKRYYQHLNRLSANLALL 589
Cdd:pfam09317 1 IRCHPYVLKEMEAAQNEDkeqaLKAFDRALFGHIGFALSNAARSLVLGLTGGRFASAPVAGETARYYRQLNRLSAAFALL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 590 SDVSMAVLGGSLKRRERISARLGDILSQLYLASAVLKRYDDEGRNEADLPLVHWGVQDALYQAEQAMDDLLQNFPNRVVA 669
Cdd:pfam09317 81 ADLAMLVLGGSLKRRERLSARLGDVLSQLYLASAVLKRFEDEGRPEADLPLVHWAMQDALYQAQQALDGVLRNFPNRPVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 670 GLLNVVIFPTGRHYLAPSDKLDHKVAKILQVPNATRSRIGRGQYLTPSEHNPVGLLEEALVDVIAADPIHQRICKELGK- 748
Cdd:pfam09317 161 WLLRVLVFPLGRRYRKPSDKLGHEVAQLLQEPGEARDRLTAGVYLPDDPDDPVGRLEAAFQAVLAAEPLEKKLKKAIKAg 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 90111100 749 NLPFTRLDELAHNALVKGLIDKDEAAILVKAEESRLRSINVDDF 792
Cdd:pfam09317 241 KLPKLTLEELIEEALEKGVITEEEAELLREAEALRLDVIQVDDF 284
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
119-508 |
4.51e-89 |
|
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and metabolism]; Acyl-CoA dehydrogenase related to the alkylation response protein AidB is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 441563 [Multi-domain] Cd Length: 381 Bit Score: 286.35 E-value: 4.51e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 119 RLTAEEQAFLDgPVEEAC--RMANDFQITHELADLPPELWAYLKEHRFFAMIIKKEYGGLEFSAYAQSRVLQKLSGVSGI 196
Cdd:COG1960 4 ELTEEQRALRD-EVREFAeeEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 197 LAITVGVPNslGPGELLQHYGTDEQKDHYLPRLARGQEIPCFALTSPEAGSDAGAIPDTgivcmGEWQGQqvlGMRLTWN 276
Cdd:COG1960 83 LALPVGVHN--GAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTT-----AVRDGD---GYVLNGQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 277 KRYITLAPIATVLGLAFKLsDPEKllgGAEdlGITCALIPTTTPGVEIGRRHFPLNV-PFQNGPTRGKDVFVPIDYIIGG 355
Cdd:COG1960 153 KTFITNAPVADVILVLART-DPAA---GHR--GISLFLVPKDTPGVTVGRIEDKMGLrGSDTGELFFDDVRVPAENLLGE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 356 PkmaGQGWRMLVECLSVGRgITLPSNSTGGVKSVALATGAYAHIRRQFKISIGKMEGIEEPLARIAGNAYVMDAAASLIT 435
Cdd:COG1960 227 E---GKGFKIAMSTLNAGR-LGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAA 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90111100 436 YGIMLGEKPAVLSAIVKYHCTHRGQQSIIDAMDITGGKGIMlgQSNFLARAYQGAPIAITVEGANILTRSMMI 508
Cdd:COG1960 303 WLLDAGEDAALEAAMAKLFATEAALEVADEALQIHGGYGYT--REYPLERLYRDARILTIYEGTNEIQRLIIA 373
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
152-500 |
1.58e-37 |
|
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA dehydrogenases; Short chain acyl-CoA dehydrogenase (SCAD). SCAD is a mitochondrial beta-oxidation enzyme. It catalyzes the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of SCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. This subgroup also contains the eukaryotic short/branched chain acyl-CoA dehydrogenase(SBCAD), the bacterial butyryl-CoA dehydorgenase(BCAD) and 2-methylbutyryl-CoA dehydrogenase, which is involved in isoleucine catabolism. These enzymes are homotetramers.
Pssm-ID: 173847 [Multi-domain] Cd Length: 373 Bit Score: 144.72 E-value: 1.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 152 PPELWAYLKEHRFFAMIIKKEYGGLEFSAYAQSRVLQKLSGVSGILAITVGVPNSLGPGELLQhYGTDEQKDHYLPRLAR 231
Cdd:cd01158 32 PREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVIVSVHNSLGANPIIK-FGTEEQKKKYLPPLAT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 232 GQEIPCFALTSPEAGSDAGAIPDTGIVCMGEWqgqqvlgmRLTWNKRYITLAPIATVLgLAFKLSDPEKllgGAEdlGIT 311
Cdd:cd01158 111 GEKIGAFALSEPGAGSDAAALKTTAKKDGDDY--------VLNGSKMWITNGGEADFY-IVFAVTDPSK---GYR--GIT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 312 CALIPTTTPGVEIGRRHFPLNVpfQNGPT---RGKDVFVPIDYIIGGPkmaGQGWRMLVECLSVGRgITLPSNSTGGVKS 388
Cdd:cd01158 177 AFIVERDTPGLSVGKKEDKLGI--RGSSTtelIFEDVRVPKENILGEE---GEGFKIAMQTLDGGR-IGIAAQALGIAQA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 389 VALATGAYAHIRRQFKISIGKMEGIEEPLARIAgnayVMDAAASLITYG-IML---GEKPAVLSAIVKYHCTHRGQQSII 464
Cdd:cd01158 251 ALDAAVDYAKERKQFGKPIADFQGIQFKLADMA----TEIEAARLLTYKaARLkdnGEPFIKEAAMAKLFASEVAMRVTT 326
|
330 340 350
....*....|....*....|....*....|....*..
gi 90111100 465 DAMDITGGKGIMlgqSNFLA-RAYQGAPIAITVEGAN 500
Cdd:cd01158 327 DAVQIFGGYGYT---KDYPVeRYYRDAKITEIYEGTS 360
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
207-511 |
2.21e-35 |
|
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal acyl-CoA oxidases (AXO) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. In contrast, AXO catalyzes a different oxidative half-reaction, in which the reduced FAD is reoxidized by molecular oxygen. The ACAD family includes the eukaryotic beta-oxidation enzymes, short (SCAD), medium (MCAD), long (LCAD) and very-long (VLCAD) chain acyl-CoA dehydrogenases. These enzymes all share high sequence similarity, but differ in their substrate specificities. The ACAD family also includes amino acid catabolism enzymes such as Isovaleryl-CoA dehydrogenase (IVD), short/branched chain acyl-CoA dehydrogenases(SBCAD), Isobutyryl-CoA dehydrogenase (IBDH), glutaryl-CoA deydrogenase (GCD) and Crotonobetainyl-CoA dehydrogenase. The mitochondrial ACAD's are generally homotetramers, except for VLCAD, which is a homodimer. Related enzymes include the SOS adaptive reponse proten aidB, Naphthocyclinone hydroxylase (NcnH), and and Dibenzothiophene (DBT) desulfurization enzyme C (DszC)
Pssm-ID: 173838 [Multi-domain] Cd Length: 327 Bit Score: 137.03 E-value: 2.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 207 LGPGELLQHYGTDEQKDHYLPRLARGQEIPCFALTSPEAGSDAGAI-----PDTgivcmGEWqgqqvlgmRLTWNKRYIT 281
Cdd:cd00567 42 LLGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIrttarKDG-----DGY--------VLNGRKIFIS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 282 LAPIATVLGLAFKLSDPekllgGAEDLGITCALIPTTTPGVEIGRrhfPLNVPFQNG-PTRG---KDVFVPIDYIIGGPk 357
Cdd:cd00567 109 NGGDADLFIVLARTDEE-----GPGHRGISAFLVPADTPGVTVGR---IWDKMGMRGsGTGElvfDDVRVPEDNLLGEE- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 358 maGQGWRMLVECLSVGRgITLPSNSTGGVKSVALATGAYAHIRRQFKISIGKMEGIEEPLARIAGNAYVMDA----AASL 433
Cdd:cd00567 180 --GGGFELAMKGLNVGR-LLLAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLllyrAAWL 256
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90111100 434 ITYGImlgEKPAVLSAIVKYHCTHRGQQSIIDAMDITGGKGimLGQSNFLARAYQGAPIAITVEGANilTRSMMIFGQ 511
Cdd:cd00567 257 LDQGP---DEARLEAAMAKLFATEAAREVADLAMQIHGGRG--YSREYPVERYLRDARAARIAEGTA--EIQRLIIAR 327
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
101-513 |
2.19e-34 |
|
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is found in the mitochondria of eukaryotes and in some bacteria. It catalyzes the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. VLCAD acts as a homodimer.
Pssm-ID: 173850 [Multi-domain] Cd Length: 409 Bit Score: 136.44 E-value: 2.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 101 DLFQGKPDWKKLhnYPQPR-LTAEEQAFLD---GPVEEACRMANDFQITHELADLPPELWAYLKEHRFFAMIIKKEYGGL 176
Cdd:cd01161 5 NMFLGDIVTKQV--FPYPSvLTEEQTEELNmlvGPVEKFFEEVNDPAKNDQLEKIPRKTLTQLKELGLFGLQVPEEYGGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 177 EFSAYAQSRVLQKLsGVSGILAITVGVPNSLG-PGELLqhYGTDEQKDHYLPRLARGQEIPCFALTSPEAGSDAGAIPDT 255
Cdd:cd01161 83 GLNNTQYARLAEIV-GMDLGFSVTLGAHQSIGfKGILL--FGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 256 givcmGEWQGQqvlGMRLTWN--KRYITLAPIATVLGLAFKLsdPEKLLGGAEDLGITCALIPTTTPGVEIGRRHFPLNV 333
Cdd:cd01161 160 -----AVLSED---GKHYVLNgsKIWITNGGIADIFTVFAKT--EVKDATGSVKDKITAFIVERSFGGVTNGPPEKKMGI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 334 PFQNGPT-RGKDVFVPIDYIIGgpkMAGQGWRMLVECLSVGRgITLPSNSTGGVKSVALATGAYAHIRRQFKISIGKMEG 412
Cdd:cd01161 230 KGSNTAEvYFEDVKIPVENVLG---EVGDGFKVAMNILNNGR-FGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 413 IEEPLARIAGNAYVMDAAASLITyGIM---LGEKPAVLSAIVKYHCTHRGQQSIIDAMDITGGKGIMlgQSNFLARAYQG 489
Cdd:cd01161 306 IQEKLANMAILQYATESMAYMTS-GNMdrgLKAEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFM--REYGVERVLRD 382
|
410 420
....*....|....*....|....
gi 90111100 490 APIAITVEGANILTRsMMIFGQGA 513
Cdd:cd01161 383 LRIFRIFEGTNEILR-LFIALTGL 405
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
152-474 |
2.41e-22 |
|
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA dehydrogenase, which catalyzes the third step in leucine catabolism, the conversion of isovaleryl-CoA (3-methylbutyryl-CoA) into 3-methylcrotonyl-CoA. IVD is a homotetramer and has the greatest affinity for small branched chain substrates.
Pssm-ID: 173845 [Multi-domain] Cd Length: 376 Bit Score: 99.79 E-value: 2.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 152 PPELWAYLKEHRFFAMIIKKEYGGLEFSAYAQSRVLQKLSGVSGILAITVGVPNSLGPGELLQHyGTDEQKDHYLPRLAR 231
Cdd:cd01156 35 PRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVALSYGAHSNLCINQIYRN-GSAAQKEKYLPKLIS 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 232 GQEIPCFALTSPEAGSDAgaipdTGIVCMGEWQGQQVLgmrLTWNKRYITLAPIATVLgLAFKLSDPEKllgGAEdlGIT 311
Cdd:cd01156 114 GEHIGALAMSEPNAGSDV-----VSMKLRAEKKGDRYV---LNGSKMWITNGPDADTL-VVYAKTDPSA---GAH--GIT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 312 CALIPTTTPGVEIGRRHFPLNVpfqngptRG--------KDVFVPIDYIIGGpkmAGQGWRMLVECLSVGRGItLPSNST 383
Cdd:cd01156 180 AFIVEKGMPGFSRAQKLDKLGM-------RGsntcelvfEDCEVPEENILGG---ENKGVYVLMSGLDYERLV-LAGGPI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 384 GGVKSVALATGAYAHIRRQFKISIGKMEGIEEPLARI-----AGNAYVMDAAASLITygimlGEKPAVLSAIVKYHCTHR 458
Cdd:cd01156 249 GIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMytrlnASRSYLYTVAKACDR-----GNMDPKDAAGVILYAAEK 323
|
330
....*....|....*.
gi 90111100 459 GQQSIIDAMDITGGKG 474
Cdd:cd01156 324 ATQVALDAIQILGGNG 339
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
120-423 |
2.57e-21 |
|
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, which catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and carbon dioxide in the catabolism of lysine, hydroxylysine, and tryptophan. It uses electron transfer flavoprotein (ETF) as an electron acceptor. GCD is a homotetramer. GCD deficiency leads to a severe neurological disorder in humans.
Pssm-ID: 173840 [Multi-domain] Cd Length: 386 Bit Score: 97.04 E-value: 2.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 120 LTAEEQAFLDGpVEEAC------RMANDFqithELADLPPELWAYLKEHRFFAMIIKkEYGGLEFSAYAQSRVLQKLSGV 193
Cdd:cd01151 13 LTEEERAIRDT-AREFCqeelapRVLEAY----REEKFDRKIIEEMGELGLLGATIK-GYGCAGLSSVAYGLIAREVERV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 194 SGILAITVGVPNSLGPGELlQHYGTDEQKDHYLPRLARGQEIPCFALTSPEAGSDAGaipdtGIVCMGEWQGQqvlGMRL 273
Cdd:cd01151 87 DSGYRSFMSVQSSLVMLPI-YDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPG-----GMETRARKDGG---GYKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 274 TWNKRYITLAPIATVLGLAFKLSDPEKLLGgaedlgitcALIPTTTPGVEIGRRH--FPLNVPfQNGPTRGKDVFVPIDY 351
Cdd:cd01151 158 NGSKTWITNSPIADVFVVWARNDETGKIRG---------FILERGMKGLSAPKIQgkFSLRAS-ITGEIVMDNVFVPEEN 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90111100 352 IIGGPKmagqGWRMLVECLSVGR-GItlpsnSTG--GVKSVALATG-AYAHIRRQFKISIGKMEGIEEPLARIAGN 423
Cdd:cd01151 228 LLPGAE----GLRGPFKCLNNARyGI-----AWGalGAAEDCYHTArQYVLDRKQFGRPLAAFQLVQKKLADMLTE 294
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
121-232 |
6.88e-20 |
|
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is an all-alpha domain.
Pssm-ID: 460686 [Multi-domain] Cd Length: 113 Bit Score: 85.59 E-value: 6.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 121 TAEEQAFLDG----------PVEEACRMANDFqitheladlPPELWAYLKEHRFFAMIIKKEYGGLEFSAYAQSRVLQKL 190
Cdd:pfam02771 1 TEEQEALRDTvrefaeeeiaPHAAEWDEEGEF---------PRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEEL 71
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 90111100 191 SGVSGILAITVGVPNSLGpGELLQHYGTDEQKDHYLPRLARG 232
Cdd:pfam02771 72 ARADASVALALSVHSSLG-APPILRFGTEEQKERYLPKLASG 112
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
120-474 |
1.84e-17 |
|
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- dehydrogenation of short branched chain acyl-CoA intermediates in valine catabolism. It is predicted to be a homotetramer.
Pssm-ID: 173851 [Multi-domain] Cd Length: 375 Bit Score: 85.19 E-value: 1.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 120 LTAEEQAFLDgpveeacrMANDFQiTHELA----------DLPPELWAYLKEHRFFAMIIKKEYGGLEFSAYAQSRVLQK 189
Cdd:cd01162 1 LNEEQRAIQE--------VARAFA-AKEMAphaadwdqkkHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 190 LSGVSGILAITVGVPNSLGpgELLQHYGTDEQKDHYLPRLARGQEIPCFALTSPEAGSDAGAIPDTGIVcmgewQGQQVL 269
Cdd:cd01162 72 LSTGCVSTAAYISIHNMCA--WMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVR-----EGDHYV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 270 gmrLTWNKRYITLAPIATVLGLAFKLsdpekllGGAEDLGITCALIPTTTPGVEIGRRHFPLNVPFQngPTRG---KDVF 346
Cdd:cd01162 145 ---LNGSKAFISGAGDSDVYVVMART-------GGEGPKGISCFVVEKGTPGLSFGANEKKMGWNAQ--PTRAvifEDCR 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 347 VPIDYIIGGpkmAGQGWRMLVECLSVGRgITLPSNSTGGVKSVALATGAYAHIRRQFKISIGKMEGIEEPLAriagnayv 426
Cdd:cd01162 213 VPVENRLGG---EGQGFGIAMAGLNGGR-LNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLA-------- 280
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 90111100 427 mDAAASLITYGIML---------GEKPAV-LSAIVKYHCTHRGQQSIIDAMDITGGKG 474
Cdd:cd01162 281 -DMATELVASRLMVrraasaldrGDPDAVkLCAMAKRFATDECFDVANQALQLHGGYG 337
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
152-506 |
8.19e-15 |
|
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found in the mitochondria of eukaryotes and in some prokaryotes. It catalyzes the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of LCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. LCAD acts as a homodimer.
Pssm-ID: 173849 [Multi-domain] Cd Length: 372 Bit Score: 77.16 E-value: 8.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 152 PPELWAYLKEHRFFAMIIKKEYGGLEFSAYAQSRVLQKLsGVSGILAITVGVPNSLGpGELLQHYGTDEQKDHYLPRLAR 231
Cdd:cd01160 32 PREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEEL-ARAGGSGPGLSLHTDIV-SPYITRAGSPEQKERVLPQMVA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 232 GQEIPCFALTSPEAGSDAGAIPDTGIVCMGEWQgqqvlgmrLTWNKRYITLAPIATVLGLAFKlSDPEKllGGAEdlGIT 311
Cdd:cd01160 110 GKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYV--------LNGSKTFITNGMLADVVIVVAR-TGGEA--RGAG--GIS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 312 CALIPTTTPGVEIGRRHFPLNVPFQNGPTRG-KDVFVPIDYIIGgpkMAGQGWRMLVECLSVGRgITLPSNSTGGVKSVA 390
Cdd:cd01160 177 LFLVERGTPGFSRGRKLKKMGWKAQDTAELFfDDCRVPAENLLG---EENKGFYYLMQNLPQER-LLIAAGALAAAEFML 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 391 LATGAYAHIRRQFKISIGKMEGIEEPLARIAGNAYVMDAAASLITYGIMLGEKPAVLSAIVKYHCTHRGQQSIIDAMDIT 470
Cdd:cd01160 253 EETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKYWATELQNRVAYECVQLH 332
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 90111100 471 GGKGIMLGQSnfLARAYQGAPIAITVEGAN-----ILTRSM 506
Cdd:cd01160 333 GGWGYMREYP--IARAYRDARVQPIYGGTTeimkeLISRQM 371
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
155-474 |
7.94e-13 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 71.06 E-value: 7.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 155 LWAYLKEHRFFAMIIKKEYGGLEFSAYAQSRVLQKLSGVSGILAITVGVPNSLGPGELLQHyGTDEQKDHYLPRLARGQE 234
Cdd:PLN02519 64 LWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGSVGLSYGAHSNLCINQLVRN-GTPAQKEKYLPKLISGEH 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 235 IPCFALTSPEAGSDagaipdtgIVCMGEWQGQQVLGMRLTWNKRYITLAPIATVLgLAFKLSDPEkllggAEDLGITCAL 314
Cdd:PLN02519 143 VGALAMSEPNSGSD--------VVSMKCKAERVDGGYVLNGNKMWCTNGPVAQTL-VVYAKTDVA-----AGSKGITAFI 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 315 IPTTTPGVEIGRRHFPLNVpfqngptRGKDV--------FVPIDYIIGGpkmAGQGWRMLVECLSVGRgITLPSNSTGGV 386
Cdd:PLN02519 209 IEKGMPGFSTAQKLDKLGM-------RGSDTcelvfencFVPEENVLGQ---EGKGVYVMMSGLDLER-LVLAAGPLGLM 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 387 KSVALATGAYAHIRRQFKISIGKMEGIEEPLARI-----AGNAYVMDAAASLITygimlGEKPAVLSAIVKYHCTHRGQQ 461
Cdd:PLN02519 278 QACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMytslqSSRSYVYSVARDCDN-----GKVDRKDCAGVILCAAERATQ 352
|
330
....*....|...
gi 90111100 462 SIIDAMDITGGKG 474
Cdd:PLN02519 353 VALQAIQCLGGNG 365
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
169-474 |
4.01e-12 |
|
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which catalyze the alpha,beta dehydrogenation of the corresponding medium chain acyl-CoA by FAD, which becomes reduced. The reduced form of MCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. MCAD is a homotetramer.
Pssm-ID: 173846 [Multi-domain] Cd Length: 378 Bit Score: 68.77 E-value: 4.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 169 IKKEYGGLEFSAYAQSRVLQKLS-GVSGILAITVGvpNSLGPGELLQHyGTDEQKDHYLPRLARGQEIPCFALTSPEAGS 247
Cdd:cd01157 51 IPEDCGGLGLGTFDTCLITEELAyGCTGVQTAIEA--NSLGQMPVIIS-GNDEQKKKYLGRMTEEPLMCAYCVTEPGAGS 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 248 DAgaipdTGIVCMGEWQGQQVLgmrLTWNKRYITLAPIAT-VLGLAFKLSDPEKLLGGAedlgITCALIPTTTPGVEIGR 326
Cdd:cd01157 128 DV-----AGIKTKAEKKGDEYI---INGQKMWITNGGKANwYFLLARSDPDPKCPASKA----FTGFIVEADTPGIQPGR 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 327 RHfpLNVPFQNGPTRG---KDVFVPIDYIIGGPkmaGQGWRMLVECLSVGRgitlPSNSTG--GVKSVALATGA-YAHIR 400
Cdd:cd01157 196 KE--LNMGQRCSDTRGitfEDVRVPKENVLIGE---GAGFKIAMGAFDKTR----PPVAAGavGLAQRALDEATkYALER 266
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90111100 401 RQFKISIGKMEGIEEPLARIAGNAYVMDAAASLITYGIMLGEKPAVLSAIVKYHCTHRGQQSIIDAMDITGGKG 474
Cdd:cd01157 267 KTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAKAFAADIANQLATDAVQIFGGNG 340
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
237-335 |
4.29e-12 |
|
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a beta-barrel fold.
Pssm-ID: 460685 [Multi-domain] Cd Length: 95 Bit Score: 62.68 E-value: 4.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 237 CFALTSPEAGSDAGAIPDTGIVCMGEwqgqqvlGMRLTWNKRYITLAPIATVLGLAFKLSDPEKllggaeDLGITCALIP 316
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAADGDGG-------GWVLNGTKWWITNAGIADLFLVLARTGGDDR------HGGISLFLVP 67
|
90
....*....|....*....
gi 90111100 317 TTTPGVEIGRRHFPLNVPF 335
Cdd:pfam02770 68 KDAPGVSVRRIETKLGVRG 86
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
171-375 |
1.07e-10 |
|
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA dehydrogenases (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173841 [Multi-domain] Cd Length: 380 Bit Score: 64.29 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 171 KEYGGLEFSAYAQSRVLQKL--SGVSGILAItVGVpNSLGPgeLLQHYGTDEQKDHYLPRLARGQEIPCFALTSPEAGSD 248
Cdd:cd01152 56 KEYGGRGASLMEQLIFREEMaaAGAPVPFNQ-IGI-DLAGP--TILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSD 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 249 AGAIPDTGIVCMGEWQ--GQQVlgmrltWNkryiTLAPIATVLGLAFKlSDPEkllgGAEDLGITCALIPTTTPGVEI-- 324
Cdd:cd01152 132 LAGLRTRAVRDGDDWVvnGQKI------WT----SGAHYADWAWLLVR-TDPE----APKHRGISILLVDMDSPGVTVrp 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 90111100 325 -----GRRHFplNVPFQNgptrgkDVFVPIDYIIGGPkmaGQGWRMLVECLSVGRG 375
Cdd:cd01152 197 irsinGGEFF--NEVFLD------DVRVPDANRVGEV---NDGWKVAMTTLNFERV 241
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
120-427 |
1.24e-10 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 64.49 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 120 LTAEEQAFldgpveeacRMANDFQITHELADLPPELWAylKEHRFFAMIIK-----------KEYG--GLEFSAYAQSrv 186
Cdd:PLN02526 29 LTPEEQAL---------RKRVRECMEKEVAPIMTEYWE--KAEFPFHIIPKlgslgiaggtiKGYGcpGLSITASAIA-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 187 LQKLSGVSGILAITVGVPNSLGPGELLQhYGTDEQKDHYLPRLARGQEIPCFALTSPEAGSDAGAIPDTGIVCMGEW--Q 264
Cdd:PLN02526 96 TAEVARVDASCSTFILVHSSLAMLTIAL-CGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWilN 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 265 GQqvlgmrltwnKRYITLAPIATVLGLAFKLSDPEKLLG-----GAEdlGITCALIPTttpgvEIGRRHfplnvpFQNGP 339
Cdd:PLN02526 175 GQ----------KRWIGNSTFADVLVIFARNTTTNQINGfivkkGAP--GLKATKIEN-----KIGLRM------VQNGD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 340 TRGKDVFVPIDYIIGGPkmagQGWRMLVECLSVGRgITLPSNSTGGVKSVALATGAYAHIRRQFKISIGKMEGIEEPLAR 419
Cdd:PLN02526 232 IVLKDVFVPDEDRLPGV----NSFQDTNKVLAVSR-VMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVR 306
|
....*...
gi 90111100 420 IAGNAYVM 427
Cdd:PLN02526 307 MLGNIQAM 314
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
119-474 |
1.46e-09 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 60.90 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 119 RLTAEEQAFLDGPVEEACRMA--NDFQITHELADLPPELWAYLKEHRFFAMIIKKEYGGLEFSAYAQSRVLQKLSgvsgi 196
Cdd:PRK12341 4 SLTEEQELLLASIRELITRNFpeEYFRTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEVS----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 197 laiTVGVP-NSLGPGELL---QHYGTDEQK----DHYLprlARGQEIPCFALTSPEAGSDAGAIPDTGIVCMGEwqgqqv 268
Cdd:PRK12341 79 ---KCGAPaFLITNGQCIhsmRRFGSAEQLrktaESTL---ETGDPAYALALTEPGAGSDNNSATTTYTRKNGK------ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 269 lgMRLTWNKRYITLA---PIATVLGLAFKLSDPEKllggaedlGITCALIPTTTPGVEIGRRHfplNVPFQNGPTRG--- 342
Cdd:PRK12341 147 --VYLNGQKTFITGAkeyPYMLVLARDPQPKDPKK--------AFTLWWVDSSKPGIKINPLH---KIGWHMLSTCEvyl 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 343 KDVFVPIDYIIGgpkMAGQGWRMLVECLSVGRgITLPSNSTGGVKSVALATGAYAHIRRQFKISIGKMEGIEEPLARIAG 422
Cdd:PRK12341 214 DNVEVEESDLVG---EEGMGFLNVMYNFEMER-LINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAI 289
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 90111100 423 NAYVMDAAASLITYGIMLGEKPAVLSAIVKYHCTHRGQQSIIDAMDITGGKG 474
Cdd:PRK12341 290 KIENMRNMVYKVAWQADNGQSLRTSAALAKLYCARTAMEVIDDAIQIMGGLG 341
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
360-500 |
3.14e-09 |
|
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an all-alpha, four helical up-and-down bundle.
Pssm-ID: 395354 [Multi-domain] Cd Length: 149 Bit Score: 56.11 E-value: 3.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 360 GQGWRMLVECLSVGRgITLPSNSTGGVKSVALATGAYAHIRRQFKISIGKMEGIEEPLARIAGNAYVMDAAASLITYGIM 439
Cdd:pfam00441 1 GRGFRVAMETLNHER-LAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALD 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 90111100 440 LGEKPAVLSAIVKYHCTHRGQQSIIDAMDITGGKGIMLGQSnfLARAYQGAPIAITVEGAN 500
Cdd:pfam00441 80 AGGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYP--VERLYRDARVLRIGEGTS 138
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
119-475 |
1.35e-07 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 54.45 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 119 RLTAEEQAFLDGPVEeacRMAND-----FQITHELADLPPELWAYLKEHRFFAMIIKKEYGGLEFSAYAQSRVLQKLSGV 193
Cdd:PRK03354 4 NLNDEQELFVAGIRE---LMASEnweayFAECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 194 SGILAITVGVPNslGPGELLQHyGTDEQKDHYLPRLARGQEIPCFALTSPEAGSDAGAIPDTGIVCMGEwqgqqvlgMRL 273
Cdd:PRK03354 81 GAPTYVLYQLPG--GFNTFLRE-GTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGK--------VYL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 274 TWNKRYIT-LAPIATVLGLAFKLSDPEKLLggaedlgITCALIPTTTPGVEIG-------RRHFPLNVPFQNGPTRGKDV 345
Cdd:PRK03354 150 NGSKCFITsSAYTPYIVVMARDGASPDKPV-------YTEWFVDMSKPGIKVTkleklglRMDSCCEITFDDVELDEKDM 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 346 FvpidyiiggpKMAGQGWRMLVECLSVGRGITLPSNStgGVKSVALATGA-YAHIRRQFKISIGKMEGIEEPLARIAGNA 424
Cdd:PRK03354 223 F----------GREGNGFNRVKEEFDHERFLVALTNY--GTAMCAFEDAArYANQRVQFGEAIGRFQLIQEKFAHMAIKL 290
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 90111100 425 YVMDAAASLITYGIMLGEKPAVLSAIVKYHCTHRGQQSIIDAMDITGGKGI 475
Cdd:PRK03354 291 NSMKNMLYEAAWKADNGTITSGDAAMCKYFCANAAFEVVDSAMQVLGGVGI 341
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
166-500 |
3.60e-07 |
|
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173842 [Multi-domain] Cd Length: 407 Bit Score: 53.16 E-value: 3.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 166 AMIIKKEYGGLEFSAYAQSRVLQKLSGVSGILAITVGvpnSLGPGELLQHYGTDEQKDHYLPRLARGQEIPCFALTSPEA 245
Cdd:cd01153 52 ALGVPEEYGGQGLPITVYSALAEIFSRGDAPLMYASG---TQGAAATLLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 246 GSDAG-----AIPDTGivcmGEWqgqqvlgmRLTWNKRYIT--------------LA----PIATVLGLAFKLSDpeKLL 302
Cdd:cd01153 129 GSDLGalrtkAVYQAD----GSW--------RINGVKRFISagehdmsenivhlvLArsegAPPGVKGLSLFLVP--KFL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 303 GGAEDLGITCAliptttpGVE--IGRRHFP-LNVPFQNGPTrgkdvfvpidYIIGGPkmaGQGWRMLVECLSVGR-GItl 378
Cdd:cd01153 195 DDGERNGVTVA-------RIEekMGLHGSPtCELVFDNAKG----------ELIGEE---GMGLAQMFAMMNGARlGV-- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 379 psnstgGVKSVALATGA------YAHIRRQFkisiGKMeGIEEPLARIAGNAYV--MDAAASLITYG-----------IM 439
Cdd:cd01153 253 ------GTQGTGLAEAAylnalaYAKERKQG----GDL-IKAAPAVTIIHHPDVrrSLMTQKAYAEGsraldlytatvQD 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90111100 440 LGEKPAV--------------LSAIVKYHCTHRGQQSIIDAMDITGGKGIMlgQSNFLARAYQGAPIAITVEGAN 500
Cdd:cd01153 322 LAERKATegedrkalsaladlLTPVVKGFGSEAALEAVSDAIQVHGGSGYT--REYPIEQYYRDARITTIYEGTT 394
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
133-259 |
6.15e-05 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 46.40 E-value: 6.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 133 EEACRMANDFQITheladLPP---ELWAYLKEHRFFAMIIKKEYGG--LEFSAYAQSRVLQKLSGVSgiLAITVGVpnSL 207
Cdd:PTZ00456 84 SEGCVLLKDGNVT-----TPKgfkEAYQALKAGGWTGISEPEEYGGqaLPLSVGFITRELMATANWG--FSMYPGL--SI 154
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 90111100 208 GPGELLQHYGTDEQKDHYLPRLARGQEIPCFALTSPEAGSDAGAIPDTGIVC 259
Cdd:PTZ00456 155 GAANTLMAWGSEEQKEQYLTKLVSGEWSGTMCLTEPQCGTDLGQVKTKAEPS 206
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
211-355 |
1.59e-04 |
|
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA dehydrogenases (ACAD) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACAD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. ACAD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173844 [Multi-domain] Cd Length: 394 Bit Score: 44.69 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 211 ELLQHYGTDEQKDHYLPRLARGQEIPCFALTSPE-AGSDAgaipdTGIVCMGEWQGQQVLgmrLTWNKRYITLA--P--- 284
Cdd:cd01155 102 EVLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDA-----TNIECSIERDGDDYV---INGRKWWSSGAgdPrck 173
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90111100 285 IATVLGlafkLSDPEKLlggAEDLGITCALIPTTTPGVEIGRrhfPLNV------PFQNGPTRGKDVFVPIDYIIGG 355
Cdd:cd01155 174 IAIVMG----RTDPDGA---PRHRQQSMILVPMDTPGVTIIR---PLSVfgyddaPHGHAEITFDNVRVPASNLILG 240
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
188-502 |
2.19e-03 |
|
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of several genes involved in the SOS adaptive response to DNA alkylation damage, whose expression is activated by the Ada protein. Its function has not been entirely elucidated; however, it is similar in sequence and function to acyl-CoA dehydrogenases. It has been proposed that aidB directly destroys DNA alkylating agents such as nitrosoguanidines (nitrosated amides) or their reaction intermediates.
Pssm-ID: 173843 [Multi-domain] Cd Length: 418 Bit Score: 41.20 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 188 QKLSGVSGILAITVG-VPnslgpgeLLQHYGTDEQKDHYLPRLARGQEIPCFA---LTSPEAGSDAGAIPDTGIVCMGE- 262
Cdd:cd01154 104 DAAAGLLCPLTMTDAaVY-------ALRKYGPEELKQYLPGLLSDRYKTGLLGgtwMTEKQGGSDLGANETTAERSGGGv 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 263 WqgqqvlgmRLTWNKrYITLAPIATVlglAFKLSDPEKLLGGAEdlGITCALIPTTTP-----GVEIGRRHFPLNVpfQN 337
Cdd:cd01154 177 Y--------RLNGHK-WFASAPLADA---ALVLARPEGAPAGAR--GLSLFLVPRLLEdgtrnGYRIRRLKDKLGT--RS 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 338 GPTrGKDVFV-PIDYIIGGPkmaGQGWRMLVECLSVGRgITLPSNSTGGVKSVALATGAYAHIRRQFKISIgkmegIEEP 416
Cdd:cd01154 241 VAT-GEVEFDdAEAYLIGDE---GKGIYYILEMLNISR-LDNAVAALGIMRRALSEAYHYARHRRAFGKPL-----IDHP 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111100 417 LAR--IAGNAYVMDAAASLITYGIMLGEKPA-----------VLSAIVKYHCTHRGQQSIIDAMDITGGKGIMlgQSNFL 483
Cdd:cd01154 311 LMRrdLAEMEVDVEAATALTFRAARAFDRAAadkpveahmarLATPVAKLIACKRAAPVTSEAMEVFGGNGYL--EEWPV 388
|
330 340
....*....|....*....|
gi 90111100 484 ARAYQGAPIAITVEG-ANIL 502
Cdd:cd01154 389 ARLHREAQVTPIWEGtGNIQ 408
|
|
| |
