|
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: 1792.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 3 ILSIVATLVLIGALFYHRVSLPLSSLILLAWTAALGAAGLWSLWLLVPLAIILVPLNVTPVRKSLISAPVFRGFRKVMPP 82
Cdd:NF038187 1 LLSILAMLVLLGALAYHRVSLLTSSLILAAVMAAGTAAGLWSLWLWLPFLIIALPLNVPSIRQSLISAPALKAFRKVMPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 83 MSRTEKEAIDAGTTWWEGDLFRGNPDWQKLHNYPQPKLTAEEQAFLDGPVEEACRMANDFQITHEMADLPPELWAFLKEH 162
Cdd:NF038187 81 MSSTEKEAIDAGTTWWEADLFRGNPDWKKLHNYPKPRLTAEEQAFLDGPVEEVCRMVNDFQITHELADLPPEVWQYLKDH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 163 RFFAMIIKKEYGGLEFSAYAQSRVLQKLAGVSGILAITVGVPNSLGPGELLQHYGTDAQKNHYLPRLARGQEIPCFALTS 242
Cdd:NF038187 161 RFFAMIIKKEYGGLEFSAYAQSRVLQKLAGVSSILASTVGVPNSLGPGELLQHYGTEEQKDHYLPRLARGEEIPCFALTS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 243 PEAGSDAGAIPDTGVVCMGEWQGEQVLGMRLTWNKRYITLAPIATVLGLAFKLSDPDRLLGGEQELGITCALIPTNTPGV 322
Cdd:NF038187 241 PEAGSDAGSIPDFGVVCKGEWQGEEVLGMRLTWNKRYITLAPVATVLGLAFKLRDPDHLLGDKEELGITCALIPTDTPGV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 323 EIGRRHFPLNVPFQNGPTRGKDIFVPIDYIIGGPKMAGQGWRMLVECLSVGRGITLPSNSTGSLKSIALATGAYAHIRRQ 402
Cdd:NF038187 321 EIGRRHFPLNVPFQNGPTRGKDIFVPLDFIIGGPKMAGQGWRMLVECLSVGRGITLPSNSTGGLKSAALATGAYARIRRQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 403 FKVSIGKMEGIEEPLARIAGNAYVMDAAASLITYGIMLGEKPAVLSAIVKYHCTHRGQQSIIDAMDIAGGKGIMLGEGNF 482
Cdd:NF038187 401 FKLPIGKMEGIEEPLARIAGNAYLMDAAATLTTTGIDLGEKPSVISAIVKYHCTHRGQRSIIDAMDIHGGKGICLGPNNF 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 483 LARAYQGAPIAITVEGANILTRTMMIFGQGAIRCHPYVLEEMAAAQNND----VNAFDKLLFRHIGHVGSNLVRSFWLGL 558
Cdd:NF038187 481 LARGYQGAPIAITVEGANILTRSMIIYGQGAIRCHPYVLAEMEAAQDNDseqaLNDFDKALFGHIGFVGSNLVRSFWLGL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 559 TNGLTSRSPTRDATRRYYQHINRLSASLALLSDVSMAVLGGSLKRRERISARLGDVLSQLYLASAVLKRYDDEGRQEADL 638
Cdd:NF038187 561 TNGRFSSAPYKDATRRYYQQLNRLSANLALLSDVSMAVLGGSLKRRERISARLGDILSQLYLASATLKRYEDEGRQKEDL 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 639 PLVHWGVQDALHQAEQAISDLLRNFPNGAVAGLLSLAIFPAGRRYDAPSDKLDHKLAKILQTPSATRSRIGRGQYLTPSE 718
Cdd:NF038187 641 PLVHWAVQDSLYQAEQALDDLLRNFPNRLVAGLLRVIIFPFGRPLKAPSDKLDHKVAKILQTPSATRSRLGRGQYLTPSE 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 719 HNPVGLLEQALLEVMAADPIHQRICKEMGKNLPFTRLDELAKRALKEGRINEDEAAILIRAEESRLRSINVDDFEPDALA 798
Cdd:NF038187 721 HNPVGLLEQALKDILAAEPIHDRVCKAAGKRLPFMRLDKLAEEGLALGVITEEEAALLERAEASRLRSINVDDFDPDELA 800
|
810
....*....|....*.
gi 1756880054 799 TQPVKLPEAVRKVEAA 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: 1586.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 42 LWSLWLLVPLAIILVPLNVTPVRKSLISAPVFRGFRKVMPPMSRTEKEAIDAGTTWWEGDLFRGNPDWQKLHNYPQPKLT 121
Cdd:PRK09463 1 LWSLWLLVPLAIILLPLNLPPLRRSLISAPLLKWFRKVLPPMSQTEREALEAGTVWWEGELFSGKPDWKKLLNYPKPTLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 122 AEEQAFLDGPVEEACRMANDFQITHEMADLPPELWAFLKEHRFFAMIIKKEYGGLEFSAYAQSRVLQKLAGVSGILAITV 201
Cdd:PRK09463 81 AEEQAFLDGPVEELCRMVNDWQITHELADLPPEVWQFIKEHGFFGMIIPKEYGGLEFSAYAHSRVLQKLASRSGTLAVTV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 202 GVPNSLGPGELLQHYGTDAQKNHYLPRLARGQEIPCFALTSPEAGSDAGAIPDTGVVCMGEWQGEQVLGMRLTWNKRYIT 281
Cdd:PRK09463 161 MVPNSLGPGELLLHYGTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGSIPDTGVVCKGEWQGEEVLGMRLTWNKRYIT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 282 LAPIATVLGLAFKLSDPDRLLGGEQELGITCALIPTNTPGVEIGRRHFPLNVPFQNGPTRGKDIFVPIDYIIGGPKMAGQ 361
Cdd:PRK09463 241 LAPIATVLGLAFKLYDPDGLLGDKEDLGITCALIPTDTPGVEIGRRHFPLNVPFQNGPTRGKDVFIPLDYIIGGPKMAGQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 362 GWRMLVECLSVGRGITLPSNSTGSLKSIALATGAYAHIRRQFKVSIGKMEGIEEPLARIAGNAYVMDAAASLITYGIMLG 441
Cdd:PRK09463 321 GWRMLMECLSVGRGISLPSNSTGGAKLAALATGAYARIRRQFKLPIGKFEGIEEPLARIAGNAYLMDAARTLTTAAVDLG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 442 EKPAVLSAIVKYHCTHRGQQSIIDAMDIAGGKGIMLGEGNFLARAYQGAPIAITVEGANILTRTMMIFGQGAIRCHPYVL 521
Cdd:PRK09463 401 EKPSVLSAIAKYHLTERGRQVINDAMDIHGGKGICLGPNNFLARAYQAAPIAITVEGANILTRSLMIFGQGAIRCHPYVL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 522 EEMAAAQNND---VNAFDKLLFRHIGHVGSNLVRSFWLGLTNGLTSRSPTRDATRRYYQHINRLSASLALLSDVSMAVLG 598
Cdd:PRK09463 481 KEMEAAQNNDkqaLKAFDKALFGHIGFVVSNAVRSFWLGLTGGRLSAAPVDDATKRYYRQLNRLSANLALLADVSMLVLG 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 599 GSLKRRERISARLGDVLSQLYLASAVLKRYDDEGRQEADLPLVHWGVQDALHQAEQAISDLLRNFPNGAVAGLLSLAIFP 678
Cdd:PRK09463 561 GSLKRRERLSARLGDILSQLYLASAVLKRYEDEGRPEADLPLVHWAVQDALYQAEQALDGLLRNFPNRVVAGLLRVLVFP 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 679 AGRRYDAPSDKLDHKLAKILQTPSATRSRIGRGQYLTPSEHNPVGLLEQALLEVMAADPIHQRICKEMGKN-LPFTRLDE 757
Cdd:PRK09463 641 LGRRYRAPSDKLDHQVAKLLQTPSATRDRLTRGQYLPPSENNPVGRLEEALLDVIAAEPIEKKICKALKKGkLPFLRLDE 720
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 1756880054 758 LAKRALKEGRINEDEAAILIRAEESRLRSINVDDFEPDALATQPVKLPEAVRKVEAA 814
Cdd:PRK09463 721 LADEALAAGVISEEEAALLREAEEARLRVINVDDFDPEELAAKPVKLPEKVQKVEAA 777
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
46-803 |
0e+00 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 1200.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 46 WLLVPLAIILVPLNVTPVRKSLISAPVFRGFRKVMPPMSRTEKEAIDAGTTWWEGDLFRGNPDWQKLHNYPQPKLTAEEQ 125
Cdd:PRK13026 4 LIILLLIAIVLVFAVKPLRRQFITRPVFKFFKKVLPPLSDTEREAMEAGDVWWEGELFSGKPDWQKLHSYPKPTLTAEEQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 126 AFLDGPVEEACRMANDFQITHEMADLPPELWAFLKEHRFFAMIIKKEYGGLEFSAYAQSRVLQKLAGVSGILAITVGVPN 205
Cdd:PRK13026 84 AFIDNEVETLLTMLDDWDIVQNRKDLPPEVWDYLKKEGFFALIIPKEYGGKGFSAYANSTIVSKIATRSVSAAVTVMVPN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 206 SLGPGELLQHYGTDAQKNHYLPRLARGQEIPCFALTSPEAGSDAGAIPDTGVVCMGEWQGEQVLGMRLTWNKRYITLAPI 285
Cdd:PRK13026 164 SLGPGELLTHYGTQEQKDYWLPRLADGTEIPCFALTGPEAGSDAGAIPDTGIVCRGEFEGEEVLGLRLTWDKRYITLAPV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 286 ATVLGLAFKLSDPDRLLGGEQELGITCALIPTNTPGVEIGRRHFPLNVPFQNGPTRGKDIFVPIDYIIGGPKMAGQGWRM 365
Cdd:PRK13026 244 ATVLGLAFKLRDPDGLLGDKKELGITCALIPTDHPGVEIGRRHNPLGMAFMNGTTRGKDVFIPLDWIIGGPDYAGRGWRM 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 366 LVECLSVGRGITLPSNSTGSLKSIALATGAYAHIRRQFKVSIGKMEGIEEPLARIAGNAYVMDAAASLITYGIMLGEKPA 445
Cdd:PRK13026 324 LVECLSAGRGISLPALGTASGHMATRTTGAYAYVRRQFGMPIGQFEGVQEALARIAGNTYLLEAARRLTTTGLDLGVKPS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 446 VLSAIVKYHCTHRGQQSIIDAMDIAGGKGIMLGEGNFLARAYQGAPIAITVEGANILTRTMMIFGQGAIRCHPYVLEEMA 525
Cdd:PRK13026 404 VVTAIAKYHMTELARDVVNDAMDIHAGKGIQLGPKNYLGHAYMAVPIAITVEGANILTRNLMIFGQGATRCHPYVLAEME 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 526 AAQNND----VNAFDKLLFRHIGHVGSNLVRSFWLGLTNGLTSRSPTRDATRRYYQHINRLSASLALLSDVSMAVLGGSL 601
Cdd:PRK13026 484 AAAMEDehegLEAFDSLLFKHIGYAARNAFRALFSALTGSRFISAPVSGETAQYYKDMSRLSAALALLADLSMLILGGDL 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 602 KRRERISARLGDVLSQLYLASAVLKRYDDEGRQEADLPLVHWGVQDALHQAEQAISDLLRNFPNGAVAGLLSLAIFPAGR 681
Cdd:PRK13026 564 KRKEMLSARLGDVLSQLYLASATLKRFEDNGRQQDDLPAVHYAMQDCLHLAAKALDEFLRNFPNRPVAWLLRALIFPLGN 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 682 RYDAPSDKLDHKLAKILQTPSATRSRIGRGQYLTPSEHNPVGLLEQALLEVMAADPIHQRICKEM--GKNLPFTRLDELA 759
Cdd:PRK13026 644 HFRAPSDKLARQLAELMMTPGPARDRLTALCYIFEGDKDGVARVEQAFLAQYAVKPLYKKLKKAQreGKLPRKVPLLELF 723
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 1756880054 760 KRALKEGRINEDEAAILIRAEESRLRSINVDDFEPDAL---ATQPVK 803
Cdd:PRK13026 724 AKALEKGVITADEAEKLLAADKLRLDAIQVDDFTPDFMekkTLQSRK 770
|
|
| ACDH_C |
pfam09317 |
Acyl-CoA dehydrogenase, C-terminal, bacterial type; This C-terminal domain is functionally ... |
514-792 |
3.84e-157 |
|
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: 458.88 E-value: 3.84e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 514 IRCHPYVLEEMAAAQNND----VNAFDKLLFRHIGHVGSNLVRSFWLGLTNGLTSRSPTRDATRRYYQHINRLSASLALL 589
Cdd:pfam09317 1 IRCHPYVLKEMEAAQNEDkeqaLKAFDRALFGHIGFALSNAARSLVLGLTGGRFASAPVAGETARYYRQLNRLSAAFALL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 590 SDVSMAVLGGSLKRRERISARLGDVLSQLYLASAVLKRYDDEGRQEADLPLVHWGVQDALHQAEQAISDLLRNFPNGAVA 669
Cdd:pfam09317 81 ADLAMLVLGGSLKRRERLSARLGDVLSQLYLASAVLKRFEDEGRPEADLPLVHWAMQDALYQAQQALDGVLRNFPNRPVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 670 GLLSLAIFPAGRRYDAPSDKLDHKLAKILQTPSATRSRIGRGQYLTPSEHNPVGLLEQALLEVMAADPIHQRICKEMGK- 748
Cdd:pfam09317 161 WLLRVLVFPLGRRYRKPSDKLGHEVAQLLQEPGEARDRLTAGVYLPDDPDDPVGRLEAAFQAVLAAEPLEKKLKKAIKAg 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1756880054 749 NLPFTRLDELAKRALKEGRINEDEAAILIRAEESRLRSINVDDF 792
Cdd:pfam09317 241 KLPKLTLEELIEEALEKGVITEEEAELLREAEALRLDVIQVDDF 284
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
120-508 |
7.30e-87 |
|
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: 280.57 E-value: 7.30e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 120 LTAEEQAFLDgPVEEAC--RMANDFQITHEMADLPPELWAFLKEHRFFAMIIKKEYGGLEFSAYAQSRVLQKLAGVSGIL 197
Cdd:COG1960 5 LTEEQRALRD-EVREFAeeEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADASL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 198 AITVGVPNslGPGELLQHYGTDAQKNHYLPRLARGQEIPCFALTSPEAGSDAGAIPDTGVvcmgeWQGEqvlGMRLTWNK 277
Cdd:COG1960 84 ALPVGVHN--GAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAV-----RDGD---GYVLNGQK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 278 RYITLAPIATVLGLAFKLSDPDRllggeqELGITCALIPTNTPGVEIGRRHFPLNV-PFQNGPTRGKDIFVPIDYIIGGP 356
Cdd:COG1960 154 TFITNAPVADVILVLARTDPAAG------HRGISLFLVPKDTPGVTVGRIEDKMGLrGSDTGELFFDDVRVPAENLLGEE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 357 kmaGQGWRMLVECLSVGRgITLPSNSTGSLKSIALATGAYAHIRRQFKVSIGKMEGIEEPLARIAGNAYVMDAAASLITY 436
Cdd:COG1960 228 ---GKGFKIAMSTLNAGR-LGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAW 303
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1756880054 437 GIMLGEKPAVLSAIVKYHCTHRGQQSIIDAMDIAGGKGIMLGEGnfLARAYQGAPIAITVEGANILTRTMMI 508
Cdd:COG1960 304 LLDAGEDAALEAAMAKLFATEAALEVADEALQIHGGYGYTREYP--LERLYRDARILTIYEGTNEIQRLIIA 373
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
145-500 |
1.02e-36 |
|
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: 142.41 E-value: 1.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 145 THEMadlPPELWAFLKEHRFFAMIIKKEYGGLEFSAYAQSRVLQKLAGVSGILAITVGVPNSLGPGELLQhYGTDAQKNH 224
Cdd:cd01158 28 KGEF---PREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVIVSVHNSLGANPIIK-FGTEEQKKK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 225 YLPRLARGQEIPCFALTSPEAGSDAGAIPDTGVVCMGEWqgeqvlgmRLTWNKRYITLAPIATVLgLAFKLSDPDRllgg 304
Cdd:cd01158 104 YLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDY--------VLNGSKMWITNGGEADFY-IVFAVTDPSK---- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 305 eQELGITCALIPTNTPGVEIGRRHFPLNVpfQNGPT---RGKDIFVPIDYIIGGPkmaGQGWRMLVECLSVGRgITLPSN 381
Cdd:cd01158 171 -GYRGITAFIVERDTPGLSVGKKEDKLGI--RGSSTtelIFEDVRVPKENILGEE---GEGFKIAMQTLDGGR-IGIAAQ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 382 STGslksIALA----TGAYAHIRRQFKVSIGKMEGIEEPLARIAgnayVMDAAASLITYG-IML---GEKPAVLSAIVKY 453
Cdd:cd01158 244 ALG----IAQAaldaAVDYAKERKQFGKPIADFQGIQFKLADMA----TEIEAARLLTYKaARLkdnGEPFIKEAAMAKL 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1756880054 454 HCTHRGQQSIIDAMDIAGGKGIMlgeGNFLA-RAYQGAPIAITVEGAN 500
Cdd:cd01158 316 FASEVAMRVTTDAVQIFGGYGYT---KDYPVeRYYRDAKITEIYEGTS 360
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
101-513 |
2.11e-33 |
|
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: 133.36 E-value: 2.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 101 DLFRGNPDWQKLHNYPQpKLTAEEQAFLD---GPVEEACRMANDFQITHEMADLPPELWAFLKEHRFFAMIIKKEYGGLE 177
Cdd:cd01161 5 NMFLGDIVTKQVFPYPS-VLTEEQTEELNmlvGPVEKFFEEVNDPAKNDQLEKIPRKTLTQLKELGLFGLQVPEEYGGLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 178 FSAYAQSRVLQKLaGVSGILAITVGVPNSLG-PGELLqhYGTDAQKNHYLPRLARGQEIPCFALTSPEAGSDAGAIPDTG 256
Cdd:cd01161 84 LNNTQYARLAEIV-GMDLGFSVTLGAHQSIGfKGILL--FGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 257 VvcmgeWQGEqvlGMRLTWN--KRYITLAPIATVLGLAFKLSDPDRllGGEQELGITCALIPTNTPGVEIGRRHFPLNVP 334
Cdd:cd01161 161 V-----LSED---GKHYVLNgsKIWITNGGIADIFTVFAKTEVKDA--TGSVKDKITAFIVERSFGGVTNGPPEKKMGIK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 335 FQNGPT-RGKDIFVPIDYIIGgpkMAGQGWRMLVECLSVGRgITLPSNSTGSLKSIALATGAYAHIRRQFKVSIGKMEGI 413
Cdd:cd01161 231 GSNTAEvYFEDVKIPVENVLG---EVGDGFKVAMNILNNGR-FGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 414 EEPLARIAGNAYVMDAAASLITyGIM---LGEKPAVLSAIVKYHCTHRGQQSIIDAMDIAGGKGIMLGEGnfLARAYQGA 490
Cdd:cd01161 307 QEKLANMAILQYATESMAYMTS-GNMdrgLKAEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYG--VERVLRDL 383
|
410 420
....*....|....*....|...
gi 1756880054 491 PIAITVEGANILTRtMMIFGQGA 513
Cdd:cd01161 384 RIFRIFEGTNEILR-LFIALTGL 405
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
207-500 |
1.37e-32 |
|
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: 128.94 E-value: 1.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 207 LGPGELLQHYGTDAQKNHYLPRLARGQEIPCFALTSPEAGSDAGAIPDTGVVCMGEWqgeqvlgmRLTWNKRYITLAPIA 286
Cdd:cd00567 42 LLGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGY--------VLNGRKIFISNGGDA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 287 TVLGLAFKLSDPDRLLGgeqelGITCALIPTNTPGVEIGRrhfPLNVPFQNG-PTRG---KDIFVPIDYIIGGPkmaGQG 362
Cdd:cd00567 114 DLFIVLARTDEEGPGHR-----GISAFLVPADTPGVTVGR---IWDKMGMRGsGTGElvfDDVRVPEDNLLGEE---GGG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 363 WRMLVECLSVGRgITLPSNSTGSLKSIALATGAYAHIRRQFKVSIGKMEGIEEPLARIAGNAYVMDA----AASLITYGI 438
Cdd:cd00567 183 FELAMKGLNVGR-LLLAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLllyrAAWLLDQGP 261
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1756880054 439 mlgEKPAVLSAIVKYHCTHRGQQSIIDAMDIAGGKGimLGEGNFLARAYQGAPIAITVEGAN 500
Cdd:cd00567 262 ---DEARLEAAMAKLFATEAAREVADLAMQIHGGRG--YSREYPVERYLRDARAARIAEGTA 318
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
152-474 |
3.66e-21 |
|
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: 96.33 E-value: 3.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 152 PPELWAFLKEHRFFAMIIKKEYGGLEFSAYAQSRVLQKLAGVSGILAITVGVPNSLGPGELLQHyGTDAQKNHYLPRLAR 231
Cdd:cd01156 35 PRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVALSYGAHSNLCINQIYRN-GSAAQKEKYLPKLIS 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 232 GQEIPCFALTSPEAGSDagaipdtgVVCM---GEWQGEQVLgmrLTWNKRYITLAPIATVLgLAFKLSDPDRllggeQEL 308
Cdd:cd01156 114 GEHIGALAMSEPNAGSD--------VVSMklrAEKKGDRYV---LNGSKMWITNGPDADTL-VVYAKTDPSA-----GAH 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 309 GITCALIPTNTPGVEIGRRHFPLNVpfqngptRG--------KDIFVPIDYIIGGpkmAGQGWRMLVECLSVGRGItLPS 380
Cdd:cd01156 177 GITAFIVEKGMPGFSRAQKLDKLGM-------RGsntcelvfEDCEVPEENILGG---ENKGVYVLMSGLDYERLV-LAG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 381 NSTGSLKSIALATGAYAHIRRQFKVSIGKMEGIEEPLARI-----AGNAYVMDAAASLITygimlGEKPAVLSAIVKYHC 455
Cdd:cd01156 246 GPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMytrlnASRSYLYTVAKACDR-----GNMDPKDAAGVILYA 320
|
330
....*....|....*....
gi 1756880054 456 THRGQQSIIDAMDIAGGKG 474
Cdd:cd01156 321 AEKATQVALDAIQILGGNG 339
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
107-423 |
5.50e-20 |
|
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: 92.81 E-value: 5.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 107 PDWQKLHNYPQpKLTAEEQAFLDGpVEEAC------RMANDFqithEMADLPPELWAFLKEHRFFAMIIKkEYGGLEFSA 180
Cdd:cd01151 1 FNWEDPLNLDD-LLTEEERAIRDT-AREFCqeelapRVLEAY----REEKFDRKIIEEMGELGLLGATIK-GYGCAGLSS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 181 YAQSRVLQKLAGVSGILAITVGVPNSLGPGELlQHYGTDAQKNHYLPRLARGQEIPCFALTSPEAGSDAGaipdtGVVCM 260
Cdd:cd01151 74 VAYGLIAREVERVDSGYRSFMSVQSSLVMLPI-YDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPG-----GMETR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 261 GEWQGEqvlGMRLTWNKRYITLAPIATVLGLAFKLSDPDRLLGgeqelgitcALIPTNTPGVEIGRRH--FPLNVPfQNG 338
Cdd:cd01151 148 ARKDGG---GYKLNGSKTWITNSPIADVFVVWARNDETGKIRG---------FILERGMKGLSAPKIQgkFSLRAS-ITG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 339 PTRGKDIFVPIDYIIGGPKmagqGWRMLVECLSVGR-GItlpsnstgSLKSIALATGA------YAHIRRQFKVSIGKME 411
Cdd:cd01151 215 EIVMDNVFVPEENLLPGAE----GLRGPFKCLNNARyGI--------AWGALGAAEDCyhtarqYVLDRKQFGRPLAAFQ 282
|
330
....*....|..
gi 1756880054 412 GIEEPLARIAGN 423
Cdd:cd01151 283 LVQKKLADMLTE 294
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
121-232 |
3.07e-18 |
|
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: 80.97 E-value: 3.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 121 TAEEQAFLDG----------PVEEACRMANDFqithemadlPPELWAFLKEHRFFAMIIKKEYGGLEFSAYAQSRVLQKL 190
Cdd:pfam02771 1 TEEQEALRDTvrefaeeeiaPHAAEWDEEGEF---------PRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEEL 71
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1756880054 191 AGVSGILAITVGVPNSLGpGELLQHYGTDAQKNHYLPRLARG 232
Cdd:pfam02771 72 ARADASVALALSVHSSLG-APPILRFGTEEQKERYLPKLASG 112
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
120-474 |
5.02e-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: 83.65 E-value: 5.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 120 LTAEEQAFLDgpveeacrMANDF---QITHEMAD------LPPELWAFLKEHRFFAMIIKKEYGGLEFSAYAQSRVLQKL 190
Cdd:cd01162 1 LNEEQRAIQE--------VARAFaakEMAPHAADwdqkkhFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEAL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 191 AGVSGILAITVGVPNSLGpgELLQHYGTDAQKNHYLPRLARGQEIPCFALTSPEAGSDAGAIPDTGVVcmgewQGEQVLg 270
Cdd:cd01162 73 STGCVSTAAYISIHNMCA--WMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVR-----EGDHYV- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 271 mrLTWNKRYITLAPIATVLGLAFKLsdpdrllGGEQELGITCALIPTNTPGVEIGRRHFPLNVPFQngPTRG---KDIFV 347
Cdd:cd01162 145 --LNGSKAFISGAGDSDVYVVMART-------GGEGPKGISCFVVEKGTPGLSFGANEKKMGWNAQ--PTRAvifEDCRV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 348 PIDYIIGGpkmAGQGWRMLVECLSVGRgITLPSNSTGSLKSIALATGAYAHIRRQFKVSIGKMEGIEEPLAriagnayvm 427
Cdd:cd01162 214 PVENRLGG---EGQGFGIAMAGLNGGR-LNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLA--------- 280
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1756880054 428 DAAASLITYGIML---------GEKPAV-LSAIVKYHCTHRGQQSIIDAMDIAGGKG 474
Cdd:cd01162 281 DMATELVASRLMVrraasaldrGDPDAVkLCAMAKRFATDECFDVANQALQLHGGYG 337
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
152-500 |
1.49e-14 |
|
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: 76.00 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 152 PPELWAFLKEHRFFAMIIKKEYGGLEFSAYAQSRVLQKLAgVSGILAITVGVPNSLGpGELLQHYGTDAQKNHYLPRLAR 231
Cdd:cd01160 32 PREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELA-RAGGSGPGLSLHTDIV-SPYITRAGSPEQKERVLPQMVA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 232 GQEIPCFALTSPEAGSDAGAIPDTGVVCMGEWQgeqvlgmrLTWNKRYITLAPIATVLGLAFKLSDPDRLLGgeqelGIT 311
Cdd:cd01160 110 GKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYV--------LNGSKTFITNGMLADVVIVVARTGGEARGAG-----GIS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 312 CALIPTNTPGVEIGRRHFPLNVPFQNGPTRG-KDIFVPIDYIIGgpkMAGQGWRMLVECLSVGRgITLPSNSTGSLKSIA 390
Cdd:cd01160 177 LFLVERGTPGFSRGRKLKKMGWKAQDTAELFfDDCRVPAENLLG---EENKGFYYLMQNLPQER-LLIAAGALAAAEFML 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 391 LATGAYAHIRRQFKVSIGKMEGIEEPLARIAGNAYVMDAAASLITYGIMLGEKPAVLSAIVKYHCTHRGQQSIIDAMDIA 470
Cdd:cd01160 253 EETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKYWATELQNRVAYECVQLH 332
|
330 340 350
....*....|....*....|....*....|
gi 1756880054 471 GGKGIMLGEGnfLARAYQGAPIAITVEGAN 500
Cdd:cd01160 333 GGWGYMREYP--IARAYRDARVQPIYGGTT 360
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
155-474 |
9.48e-13 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 71.06 E-value: 9.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 155 LWAFLKEHRFFAMIIKKEYGGLEFSAYAQSRVLQKLAGVSGILAITVGVPNSLGPGELLQHyGTDAQKNHYLPRLARGQE 234
Cdd:PLN02519 64 LWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGSVGLSYGAHSNLCINQLVRN-GTPAQKEKYLPKLISGEH 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 235 IPCFALTSPEAGSDagaipdtgVVCMgEWQGEQV-LGMRLTWNKRYITLAPIATVLgLAFKLSDPDrllGGEQelGITCA 313
Cdd:PLN02519 143 VGALAMSEPNSGSD--------VVSM-KCKAERVdGGYVLNGNKMWCTNGPVAQTL-VVYAKTDVA---AGSK--GITAF 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 314 LIPTNTPGVEIGRRHFPLNVpfqngptRGKDI--------FVPIDYIIGGpkmAGQGWRMLVECLSVGRgITLPSNSTGS 385
Cdd:PLN02519 208 IIEKGMPGFSTAQKLDKLGM-------RGSDTcelvfencFVPEENVLGQ---EGKGVYVMMSGLDLER-LVLAAGPLGL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 386 LKSIALATGAYAHIRRQFKVSIGKMEGIEEPLARI-----AGNAYVMDAAASLITygimlGEKPAVLSAIVKYHCTHRGQ 460
Cdd:PLN02519 277 MQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMytslqSSRSYVYSVARDCDN-----GKVDRKDCAGVILCAAERAT 351
|
330
....*....|....
gi 1756880054 461 QSIIDAMDIAGGKG 474
Cdd:PLN02519 352 QVALQAIQCLGGNG 365
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
237-335 |
1.22e-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: 64.22 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 237 CFALTSPEAGSDAGAIPDTGVVcmgewqgEQVLGMRLTWNKRYITLAPIATVLGLAFKLSDPDRllggeqELGITCALIP 316
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAAD-------GDGGGWVLNGTKWWITNAGIADLFLVLARTGGDDR------HGGISLFLVP 67
|
90
....*....|....*....
gi 1756880054 317 TNTPGVEIGRRHFPLNVPF 335
Cdd:pfam02770 68 KDAPGVSVRRIETKLGVRG 86
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
169-474 |
1.89e-11 |
|
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: 66.84 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 169 IKKEYGGLEFSAYAQSRVLQKLA-GVSGILAITVGvpNSLGPGELLQHyGTDAQKNHYLPRLARGQEIPCFALTSPEAGS 247
Cdd:cd01157 51 IPEDCGGLGLGTFDTCLITEELAyGCTGVQTAIEA--NSLGQMPVIIS-GNDEQKKKYLGRMTEEPLMCAYCVTEPGAGS 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 248 DAgaipdTGVVCMGEWQGEQVLgmrLTWNKRYITLAPIATVLGLAFKlSDPDRLLGGEQelGITCALIPTNTPGVEIGRR 327
Cdd:cd01157 128 DV-----AGIKTKAEKKGDEYI---INGQKMWITNGGKANWYFLLAR-SDPDPKCPASK--AFTGFIVEADTPGIQPGRK 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 328 HfpLNVPFQNGPTRG---KDIFVPIDYIIGGPkmaGQGWRMLVECLSVGRgitlPSNSTGS--LKSIALATGA-YAHIRR 401
Cdd:cd01157 197 E--LNMGQRCSDTRGitfEDVRVPKENVLIGE---GAGFKIAMGAFDKTR----PPVAAGAvgLAQRALDEATkYALERK 267
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1756880054 402 QFKVSIGKMEGIEEPLARIAGNAYVMDAAASLITYGIMLGEKPAVLSAIVKYHCTHRGQQSIIDAMDIAGGKG 474
Cdd:cd01157 268 TFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAKAFAADIANQLATDAVQIFGGNG 340
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
120-427 |
7.72e-11 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 64.87 E-value: 7.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 120 LTAEEQAFldgpveeacRMANDFQITHEMADLPPELWAflKEHRFFAMIIK-----------KEYG--GLEFSAYAQSrv 186
Cdd:PLN02526 29 LTPEEQAL---------RKRVRECMEKEVAPIMTEYWE--KAEFPFHIIPKlgslgiaggtiKGYGcpGLSITASAIA-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 187 LQKLAGVSGILAITVGVPNSLGPGELLQhYGTDAQKNHYLPRLARGQEIPCFALTSPEAGSDAGAIPDTGVVCMGEWQge 266
Cdd:PLN02526 96 TAEVARVDASCSTFILVHSSLAMLTIAL-CGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWI-- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 267 qvlgmrLTWNKRYITLAPIATVLGLAFKLSDPDRLLG---GEQELGITCALIPTntpgvEIGRRHfplnvpFQNGPTRGK 343
Cdd:PLN02526 173 ------LNGQKRWIGNSTFADVLVIFARNTTTNQINGfivKKGAPGLKATKIEN-----KIGLRM------VQNGDIVLK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 344 DIFVPIDYIIGGPkmagQGWRMLVECLSVGRGITlpsnstgSLKSIALATGAY--AHI----RRQFKVSIGKMEGIEEPL 417
Cdd:PLN02526 236 DVFVPDEDRLPGV----NSFQDTNKVLAVSRVMV-------AWQPIGISMGVYdmCHRylkeRKQFGAPLAAFQINQEKL 304
|
330
....*....|
gi 1756880054 418 ARIAGNAYVM 427
Cdd:PLN02526 305 VRMLGNIQAM 314
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
360-500 |
1.09e-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: 57.65 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 360 GQGWRMLVECLSVGRgITLPSNSTGSLKSIALATGAYAHIRRQFKVSIGKMEGIEEPLARIAGNAYVMDAAASLITYGIM 439
Cdd:pfam00441 1 GRGFRVAMETLNHER-LAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALD 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1756880054 440 LGEKPAVLSAIVKYHCTHRGQQSIIDAMDIAGGKGIMLGEGnfLARAYQGAPIAITVEGAN 500
Cdd:pfam00441 80 AGGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYP--VERLYRDARVLRIGEGTS 138
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
171-375 |
7.41e-09 |
|
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: 58.51 E-value: 7.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 171 KEYGGLEFSAYAQSRVLQKLA-----GVSGILAItvgvpNSLGPgeLLQHYGTDAQKNHYLPRLARGQEIPCFALTSPEA 245
Cdd:cd01152 56 KEYGGRGASLMEQLIFREEMAaagapVPFNQIGI-----DLAGP--TILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 246 GSDAGAIPDTGVVCMGEWQgeqvlgmrLTWNKRYITLAPIATVLGLAFKlSDPDrllgGEQELGITCALIPTNTPGVEI- 324
Cdd:cd01152 129 GSDLAGLRTRAVRDGDDWV--------VNGQKIWTSGAHYADWAWLLVR-TDPE----APKHRGISILLVDMDSPGVTVr 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1756880054 325 ------GRRHFplNVPFQNgptrgkDIFVPIDYIIGGPkmaGQGWRMLVECLSVGRG 375
Cdd:cd01152 196 pirsinGGEFF--NEVFLD------DVRVPDANRVGEV---NDGWKVAMTTLNFERV 241
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
166-500 |
1.81e-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: 54.32 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 166 AMIIKKEYGGLEFSAYAQSRVLQKLAGVSGILAITVGvpnSLGPGELLQHYGTDAQKNHYLPRLARGQEIPCFALTSPEA 245
Cdd:cd01153 52 ALGVPEEYGGQGLPITVYSALAEIFSRGDAPLMYASG---TQGAAATLLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 246 GSDAG-----AIPDTGvvcmGEWqgeqvlgmRLTWNKRYIT--------------LA----PIATVLGLAFKLSdPDRLL 302
Cdd:cd01153 129 GSDLGalrtkAVYQAD----GSW--------RINGVKRFISagehdmsenivhlvLArsegAPPGVKGLSLFLV-PKFLD 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 303 GG----------EQELGI----TCALIPTNTPGVEIGRRHFPLnvpfqngptrgKDIFVPIDyiiggpkmagqGWRMLVE 368
Cdd:cd01153 196 DGerngvtvariEEKMGLhgspTCELVFDNAKGELIGEEGMGL-----------AQMFAMMN-----------GARLGVG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 369 CLSVGRGitlpsnSTGSLKSIalatgAYAHIRRQFkvsiGKMeGIEEPLARIAGNAYV--MDAAASLITYG--------- 437
Cdd:cd01153 254 TQGTGLA------EAAYLNAL-----AYAKERKQG----GDL-IKAAPAVTIIHHPDVrrSLMTQKAYAEGsraldlyta 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1756880054 438 --IMLGEKPAV--------------LSAIVKYHCTHRGQQSIIDAMDIAGGKGIMlgEGNFLARAYQGAPIAITVEGAN 500
Cdd:cd01153 318 tvQDLAERKATegedrkalsaladlLTPVVKGFGSEAALEAVSDAIQVHGGSGYT--REYPIEQYYRDARITTIYEGTT 394
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
119-475 |
1.93e-06 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 50.99 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 119 KLTAEEQAFLDGPVEeacRMAND-----FQITHEMADLPPELWAFLKEHRFFAMIIKKEYGGLEFSAYAQSRVLQKLAGV 193
Cdd:PRK03354 4 NLNDEQELFVAGIRE---LMASEnweayFAECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 194 SGILAITVGVPNslGPGELLQHyGTDAQKNHYLPRLARGQEIPCFALTSPEAGSDAGAIPDTGVVCMGEwqgeqvlgMRL 273
Cdd:PRK03354 81 GAPTYVLYQLPG--GFNTFLRE-GTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGK--------VYL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 274 TWNKRYIT-LAPIATVLGLAFKLSDPDRLLGGEQELGITCALIpTNTPGVEIGRRHFPL-NVPFQNGPTRGKDIFvpidy 351
Cdd:PRK03354 150 NGSKCFITsSAYTPYIVVMARDGASPDKPVYTEWFVDMSKPGI-KVTKLEKLGLRMDSCcEITFDDVELDEKDMF----- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 352 iiggpKMAGQGWRMLVECLSVGRGITLPSNSTGSLKSIALATgAYAHIRRQFKVSIGKMEGIEEPLARIAGNAYVMDAAA 431
Cdd:PRK03354 224 -----GREGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAA-RYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNML 297
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1756880054 432 SLITYGIMLGEKPAVLSAIVKYHCTHRGQQSIIDAMDIAGGKGI 475
Cdd:PRK03354 298 YEAAWKADNGTITSGDAAMCKYFCANAAFEVVDSAMQVLGGVGI 341
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
211-333 |
5.97e-05 |
|
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: 46.23 E-value: 5.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 211 ELLQHYGTDAQKNHYLPRLARGQEIPCFALTSPE-AGSDAgaipdTGVVCMGEWQG-EQVLGMRLTW-----NKRyitlA 283
Cdd:cd01155 102 EVLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDA-----TNIECSIERDGdDYVINGRKWWssgagDPR----C 172
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1756880054 284 PIATVLGlafkLSDPDRLLGGEQELGItcaLIPTNTPGVEIGRrhfPLNV 333
Cdd:cd01155 173 KIAIVMG----RTDPDGAPRHRQQSMI---LVPMDTPGVTIIR---PLSV 212
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
133-259 |
2.15e-04 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 44.86 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756880054 133 EEACRMANDFQIThemadLPP---ELWAFLKEHRFFAMIIKKEYGG--LEFSAYAQSRVLQKLAGVSgiLAITVGVpnSL 207
Cdd:PTZ00456 84 SEGCVLLKDGNVT-----TPKgfkEAYQALKAGGWTGISEPEEYGGqaLPLSVGFITRELMATANWG--FSMYPGL--SI 154
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1756880054 208 GPGELLQHYGTDAQKNHYLPRLARGQEIPCFALTSPEAGSDAGAIPDTGVVC 259
Cdd:PTZ00456 155 GAANTLMAWGSEEQKEQYLTKLVSGEWSGTMCLTEPQCGTDLGQVKTKAEPS 206
|
|
| |
