|
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: 1791.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 3 ILSIIATVVLLGALFYHRVSLFLSSLILLAWTAALGVAGLWSIWLLVPLAIILVPFNLTPMRKSMISAPVFRGFRKVMPP 82
Cdd:NF038187 1 LLSILAMLVLLGALAYHRVSLLTSSLILAAVMAAGTAAGLWSLWLWLPFLIIALPLNVPSIRQSLISAPALKAFRKVMPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 83 MSRTEKEAIDAGTTWWEGDLFQGKPDWKKLHNYPQPQLTAEEQAFLDGPVEEACRMANDFQITHELADLPPELWAYLKEH 162
Cdd:NF038187 81 MSSTEKEAIDAGTTWWEADLFRGNPDWKKLHNYPKPRLTAEEQAFLDGPVEEVCRMVNDFQITHELADLPPEVWQYLKDH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 163 RFFAMIIKKEYGGLEFSAYAQSRVLQKLSGVSGILAITVGVPNSLGPGELLQHYGTEEQKNHYLPRLARGQEIPCFALTS 242
Cdd:NF038187 161 RFFAMIIKKEYGGLEFSAYAQSRVLQKLAGVSSILASTVGVPNSLGPGELLQHYGTEEQKDHYLPRLARGEEIPCFALTS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 243 PEAGSDAGAIPDTGVVCMGEWQGQQVLGMRLTWNKRYITLAPIATVLGLAFKLSDPDRLLGGEEELGITCALIPTSTPGV 322
Cdd:NF038187 241 PEAGSDAGSIPDFGVVCKGEWQGEEVLGMRLTWNKRYITLAPVATVLGLAFKLRDPDHLLGDKEELGITCALIPTDTPGV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 323 EIGRRHFPLNVPFQNGPTRGNDIFVPIDYIIGGPKMAGQGWRMLVECLSVGRGITLPSNSTGGVKSVALATGAYAHIRRQ 402
Cdd:NF038187 321 EIGRRHFPLNVPFQNGPTRGKDIFVPLDFIIGGPKMAGQGWRMLVECLSVGRGITLPSNSTGGLKSAALATGAYARIRRQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 403 FKISIGKMEGIEEPLARIAGNAYVMDAAASLITYGIMLGEKPAVLSAIVKYHCTHRGQQSIIDAMDITGGKGIMLGESNF 482
Cdd:NF038187 401 FKLPIGKMEGIEEPLARIAGNAYLMDAAATLTTTGIDLGEKPSVISAIVKYHCTHRGQRSIIDAMDIHGGKGICLGPNNF 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 483 LARAYQGAPIAITVEGANILTRSMMIFGQGAIRCHPYVLEEMAAAQNND----VNAFDKLLFKHIGHVGSNTVRSFWLGL 558
Cdd:NF038187 481 LARGYQGAPIAITVEGANILTRSMIIYGQGAIRCHPYVLAEMEAAQDNDseqaLNDFDKALFGHIGFVGSNLVRSFWLGL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 559 TRGLTSHTPTGDATKRYYQHLNRLSANLALLSDVSMAVLGGSLKRRERISARLGDVLSQLYLASAVLKRYDDEGRHEADL 638
Cdd:NF038187 561 TNGRFSSAPYKDATRRYYQQLNRLSANLALLSDVSMAVLGGSLKRRERISARLGDILSQLYLASATLKRYEDEGRQKEDL 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 639 PLVHWGVQDALYRAEQAMDDLLQNFPNRVVAGLLTAMIFPTGRHYLAPSDKLDHAVAKILQVPNATRSRIGRGQYLTPAK 718
Cdd:NF038187 641 PLVHWAVQDSLYQAEQALDDLLRNFPNRLVAGLLRVIIFPFGRPLKAPSDKLDHKVAKILQTPSATRSRLGRGQYLTPSE 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 719 HNPVGLLEEALRDVIAADPIHQRICKELGKNLPFTRLDELARNALAKGLIDKDEAAILAKAEESRLRSINVDDFEPEALA 798
Cdd:NF038187 721 HNPVGLLEQALKDILAAEPIHDRVCKAAGKRLPFMRLDKLAEEGLALGVITEEEAALLERAEASRLRSINVDDFDPDELA 800
|
810
....*....|....*.
gi 446895789 799 TRPVKLPEKVRKVEAA 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: 1597.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 42 LWSIWLLVPLAIILVPFNLTPMRKSMISAPVFRGFRKVMPPMSRTEKEAIDAGTTWWEGDLFQGKPDWKKLHNYPQPQLT 121
Cdd:PRK09463 1 LWSLWLLVPLAIILLPLNLPPLRRSLISAPLLKWFRKVLPPMSQTEREALEAGTVWWEGELFSGKPDWKKLLNYPKPTLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 122 AEEQAFLDGPVEEACRMANDFQITHELADLPPELWAYLKEHRFFAMIIKKEYGGLEFSAYAQSRVLQKLSGVSGILAITV 201
Cdd:PRK09463 81 AEEQAFLDGPVEELCRMVNDWQITHELADLPPEVWQFIKEHGFFGMIIPKEYGGLEFSAYAHSRVLQKLASRSGTLAVTV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 202 GVPNSLGPGELLQHYGTEEQKNHYLPRLARGQEIPCFALTSPEAGSDAGAIPDTGVVCMGEWQGQQVLGMRLTWNKRYIT 281
Cdd:PRK09463 161 MVPNSLGPGELLLHYGTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGSIPDTGVVCKGEWQGEEVLGMRLTWNKRYIT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 282 LAPIATVLGLAFKLSDPDRLLGGEEELGITCALIPTSTPGVEIGRRHFPLNVPFQNGPTRGNDIFVPIDYIIGGPKMAGQ 361
Cdd:PRK09463 241 LAPIATVLGLAFKLYDPDGLLGDKEDLGITCALIPTDTPGVEIGRRHFPLNVPFQNGPTRGKDVFIPLDYIIGGPKMAGQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 362 GWRMLVECLSVGRGITLPSNSTGGVKSVALATGAYAHIRRQFKISIGKMEGIEEPLARIAGNAYVMDAAASLITYGIMLG 441
Cdd:PRK09463 321 GWRMLMECLSVGRGISLPSNSTGGAKLAALATGAYARIRRQFKLPIGKFEGIEEPLARIAGNAYLMDAARTLTTAAVDLG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 442 EKPAVLSAIVKYHCTHRGQQSIIDAMDITGGKGIMLGESNFLARAYQGAPIAITVEGANILTRSMMIFGQGAIRCHPYVL 521
Cdd:PRK09463 401 EKPSVLSAIAKYHLTERGRQVINDAMDIHGGKGICLGPNNFLARAYQAAPIAITVEGANILTRSLMIFGQGAIRCHPYVL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 522 EEMAAAQNND---VNAFDKLLFKHIGHVGSNTVRSFWLGLTRGLTSHTPTGDATKRYYQHLNRLSANLALLSDVSMAVLG 598
Cdd:PRK09463 481 KEMEAAQNNDkqaLKAFDKALFGHIGFVVSNAVRSFWLGLTGGRLSAAPVDDATKRYYRQLNRLSANLALLADVSMLVLG 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 599 GSLKRRERISARLGDVLSQLYLASAVLKRYDDEGRHEADLPLVHWGVQDALYRAEQAMDDLLQNFPNRVVAGLLTAMIFP 678
Cdd:PRK09463 561 GSLKRRERLSARLGDILSQLYLASAVLKRYEDEGRPEADLPLVHWAVQDALYQAEQALDGLLRNFPNRVVAGLLRVLVFP 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 679 TGRHYLAPSDKLDHAVAKILQVPNATRSRIGRGQYLTPAKHNPVGLLEEALRDVIAADPIHQRICKELGKN-LPFTRLDE 757
Cdd:PRK09463 641 LGRRYRAPSDKLDHQVAKLLQTPSATRDRLTRGQYLPPSENNPVGRLEEALLDVIAAEPIEKKICKALKKGkLPFLRLDE 720
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 446895789 758 LARNALAKGLIDKDEAAILAKAEESRLRSINVDDFEPEALATRPVKLPEKVRKVEAA 814
Cdd:PRK09463 721 LADEALAAGVISEEEAALLREAEEARLRVINVDDFDPEELAAKPVKLPEKVQKVEAA 777
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
46-805 |
0e+00 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 1208.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 46 WLLVPLAIILVPFNLTPMRKSMISAPVFRGFRKVMPPMSRTEKEAIDAGTTWWEGDLFQGKPDWKKLHNYPQPQLTAEEQ 125
Cdd:PRK13026 4 LIILLLIAIVLVFAVKPLRRQFITRPVFKFFKKVLPPLSDTEREAMEAGDVWWEGELFSGKPDWQKLHSYPKPTLTAEEQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 126 AFLDGPVEEACRMANDFQITHELADLPPELWAYLKEHRFFAMIIKKEYGGLEFSAYAQSRVLQKLSGVSGILAITVGVPN 205
Cdd:PRK13026 84 AFIDNEVETLLTMLDDWDIVQNRKDLPPEVWDYLKKEGFFALIIPKEYGGKGFSAYANSTIVSKIATRSVSAAVTVMVPN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 206 SLGPGELLQHYGTEEQKNHYLPRLARGQEIPCFALTSPEAGSDAGAIPDTGVVCMGEWQGQQVLGMRLTWNKRYITLAPI 285
Cdd:PRK13026 164 SLGPGELLTHYGTQEQKDYWLPRLADGTEIPCFALTGPEAGSDAGAIPDTGIVCRGEFEGEEVLGLRLTWDKRYITLAPV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 286 ATVLGLAFKLSDPDRLLGGEEELGITCALIPTSTPGVEIGRRHFPLNVPFQNGPTRGNDIFVPIDYIIGGPKMAGQGWRM 365
Cdd:PRK13026 244 ATVLGLAFKLRDPDGLLGDKKELGITCALIPTDHPGVEIGRRHNPLGMAFMNGTTRGKDVFIPLDWIIGGPDYAGRGWRM 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 366 LVECLSVGRGITLPSNSTGGVKSVALATGAYAHIRRQFKISIGKMEGIEEPLARIAGNAYVMDAAASLITYGIMLGEKPA 445
Cdd:PRK13026 324 LVECLSAGRGISLPALGTASGHMATRTTGAYAYVRRQFGMPIGQFEGVQEALARIAGNTYLLEAARRLTTTGLDLGVKPS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 446 VLSAIVKYHCTHRGQQSIIDAMDITGGKGIMLGESNFLARAYQGAPIAITVEGANILTRSMMIFGQGAIRCHPYVLEEMA 525
Cdd:PRK13026 404 VVTAIAKYHMTELARDVVNDAMDIHAGKGIQLGPKNYLGHAYMAVPIAITVEGANILTRNLMIFGQGATRCHPYVLAEME 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 526 AAQNND----VNAFDKLLFKHIGHVGSNTVRSFWLGLTRGLTSHTPTGDATKRYYQHLNRLSANLALLSDVSMAVLGGSL 601
Cdd:PRK13026 484 AAAMEDehegLEAFDSLLFKHIGYAARNAFRALFSALTGSRFISAPVSGETAQYYKDMSRLSAALALLADLSMLILGGDL 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 602 KRRERISARLGDVLSQLYLASAVLKRYDDEGRHEADLPLVHWGVQDALYRAEQAMDDLLQNFPNRVVAGLLTAMIFPTGR 681
Cdd:PRK13026 564 KRKEMLSARLGDVLSQLYLASATLKRFEDNGRQQDDLPAVHYAMQDCLHLAAKALDEFLRNFPNRPVAWLLRALIFPLGN 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 682 HYLAPSDKLDHAVAKILQVPNATRSRIGRGQYLTPAKHNPVGLLEEALRDVIAADPIHQRICKEL--GKNLPFTRLDELA 759
Cdd:PRK13026 644 HFRAPSDKLARQLAELMMTPGPARDRLTALCYIFEGDKDGVARVEQAFLAQYAVKPLYKKLKKAQreGKLPRKVPLLELF 723
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 446895789 760 RNALAKGLIDKDEAAILAKAEESRLRSINVDDFEP-----EALATRPVKLP 805
Cdd:PRK13026 724 AKALEKGVITADEAEKLLAADKLRLDAIQVDDFTPdfmekKTLQSRKEKLK 774
|
|
| ACDH_C |
pfam09317 |
Acyl-CoA dehydrogenase, C-terminal, bacterial type; This C-terminal domain is functionally ... |
514-792 |
6.96e-162 |
|
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: 471.20 E-value: 6.96e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 514 IRCHPYVLEEMAAAQNND----VNAFDKLLFKHIGHVGSNTVRSFWLGLTRGLTSHTPTGDATKRYYQHLNRLSANLALL 589
Cdd:pfam09317 1 IRCHPYVLKEMEAAQNEDkeqaLKAFDRALFGHIGFALSNAARSLVLGLTGGRFASAPVAGETARYYRQLNRLSAAFALL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 590 SDVSMAVLGGSLKRRERISARLGDVLSQLYLASAVLKRYDDEGRHEADLPLVHWGVQDALYRAEQAMDDLLQNFPNRVVA 669
Cdd:pfam09317 81 ADLAMLVLGGSLKRRERLSARLGDVLSQLYLASAVLKRFEDEGRPEADLPLVHWAMQDALYQAQQALDGVLRNFPNRPVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 670 GLLTAMIFPTGRHYLAPSDKLDHAVAKILQVPNATRSRIGRGQYLTPAKHNPVGLLEEALRDVIAADPIHQRICKELGK- 748
Cdd:pfam09317 161 WLLRVLVFPLGRRYRKPSDKLGHEVAQLLQEPGEARDRLTAGVYLPDDPDDPVGRLEAAFQAVLAAEPLEKKLKKAIKAg 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 446895789 749 NLPFTRLDELARNALAKGLIDKDEAAILAKAEESRLRSINVDDF 792
Cdd:pfam09317 241 KLPKLTLEELIEEALEKGVITEEEAELLREAEALRLDVIQVDDF 284
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
119-508 |
9.59e-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: 280.19 E-value: 9.59e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 119 QLTAEEQAFLDgPVEEAC--RMANDFQITHELADLPPELWAYLKEHRFFAMIIKKEYGGLEFSAYAQSRVLQKLSGVSGI 196
Cdd:COG1960 4 ELTEEQRALRD-EVREFAeeEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 197 LAITVGVPNslGPGELLQHYGTEEQKNHYLPRLARGQEIPCFALTSPEAGSDAGAIPDTGVvcmgeWQGQqvlGMRLTWN 276
Cdd:COG1960 83 LALPVGVHN--GAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAV-----RDGD---GYVLNGQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 277 KRYITLAPIATVLGLAFKLSDPDRllggeeELGITCALIPTSTPGVEIGRRHFPLNV-PFQNGPTRGNDIFVPIDYIIGG 355
Cdd:COG1960 153 KTFITNAPVADVILVLARTDPAAG------HRGISLFLVPKDTPGVTVGRIEDKMGLrGSDTGELFFDDVRVPAENLLGE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 356 PkmaGQGWRMLVECLSVGRgITLPSNSTGGVKSVALATGAYAHIRRQFKISIGKMEGIEEPLARIAGNAYVMDAAASLIT 435
Cdd:COG1960 227 E---GKGFKIAMSTLNAGR-LGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAA 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446895789 436 YGIMLGEKPAVLSAIVKYHCTHRGQQSIIDAMDITGGKGIMlgESNFLARAYQGAPIAITVEGANILTRSMMI 508
Cdd:COG1960 303 WLLDAGEDAALEAAMAKLFATEAALEVADEALQIHGGYGYT--REYPLERLYRDARILTIYEGTNEIQRLIIA 373
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
152-500 |
8.60e-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: 142.41 E-value: 8.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 152 PPELWAYLKEHRFFAMIIKKEYGGLEFSAYAQSRVLQKLSGVSGILAITVGVPNSLGPGELLQhYGTEEQKNHYLPRLAR 231
Cdd:cd01158 32 PREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVIVSVHNSLGANPIIK-FGTEEQKKKYLPPLAT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 232 GQEIPCFALTSPEAGSDAGAIPDTGVVCMGEWqgqqvlgmRLTWNKRYITLAPIATVLgLAFKLSDPDRllgGEEelGIT 311
Cdd:cd01158 111 GEKIGAFALSEPGAGSDAAALKTTAKKDGDDY--------VLNGSKMWITNGGEADFY-IVFAVTDPSK---GYR--GIT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 312 CALIPTSTPGVEIGRRHFPL--------NVPFQngptrgnDIFVPIDYIIGGPkmaGQGWRMLVECLSVGRgITLPSNST 383
Cdd:cd01158 177 AFIVERDTPGLSVGKKEDKLgirgssttELIFE-------DVRVPKENILGEE---GEGFKIAMQTLDGGR-IGIAAQAL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 384 GGVKSVALATGAYAHIRRQFKISIGKMEGIEEPLARIAgnayVMDAAASLITYG-IML---GEKPAVLSAIVKYHCTHRG 459
Cdd:cd01158 246 GIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMA----TEIEAARLLTYKaARLkdnGEPFIKEAAMAKLFASEVA 321
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 446895789 460 QQSIIDAMDITGGKGIMlgeSNFLA-RAYQGAPIAITVEGAN 500
Cdd:cd01158 322 MRVTTDAVQIFGGYGYT---KDYPVeRYYRDAKITEIYEGTS 360
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
101-513 |
1.85e-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: 1.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 101 DLFQGKPDWKKLHNYP---QPQLTAEEQAFLdGPVEEACRMANDFQITHELADLPPELWAYLKEHRFFAMIIKKEYGGLE 177
Cdd:cd01161 5 NMFLGDIVTKQVFPYPsvlTEEQTEELNMLV-GPVEKFFEEVNDPAKNDQLEKIPRKTLTQLKELGLFGLQVPEEYGGLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 178 FSAYAQSRVLQKLsGVSGILAITVGVPNSLG-PGELLqhYGTEEQKNHYLPRLARGQEIPCFALTSPEAGSDAGAIPDTG 256
Cdd:cd01161 84 LNNTQYARLAEIV-GMDLGFSVTLGAHQSIGfKGILL--FGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 257 VVcmgEWQGQQVLgmrLTWNKRYITLAPIATVLGLAFKLSDPDRllGGEEELGITCALIPTSTPGVEIGRRHFPLNVPFQ 336
Cdd:cd01161 161 VL---SEDGKHYV---LNGSKIWITNGGIADIFTVFAKTEVKDA--TGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 337 NGPT-RGNDIFVPIDYIIGgpkMAGQGWRMLVECLSVGRgITLPSNSTGGVKSVALATGAYAHIRRQFKISIGKMEGIEE 415
Cdd:cd01161 233 NTAEvYFEDVKIPVENVLG---EVGDGFKVAMNILNNGR-FGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 416 PLARIAGNAYVMDAAASLITyGIM---LGEKPAVLSAIVKYHCTHRGQQSIIDAMDITGGKGIMlgESNFLARAYQGAPI 492
Cdd:cd01161 309 KLANMAILQYATESMAYMTS-GNMdrgLKAEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFM--REYGVERVLRDLRI 385
|
410 420
....*....|....*....|.
gi 446895789 493 AITVEGANILTRsMMIFGQGA 513
Cdd:cd01161 386 FRIFEGTNEILR-LFIALTGL 405
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
207-511 |
2.42e-34 |
|
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: 133.95 E-value: 2.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 207 LGPGELLQHYGTEEQKNHYLPRLARGQEIPCFALTSPEAGSDAGAIPDTGVVCMGEWqgqqvlgmRLTWNKRYITLAPIA 286
Cdd:cd00567 42 LLGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGY--------VLNGRKIFISNGGDA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 287 TVLGLAFKLSDPdrllgGEEELGITCALIPTSTPGVEIGRrhfPLNVPFQNG-PTRG---NDIFVPIDYIIGGPkmaGQG 362
Cdd:cd00567 114 DLFIVLARTDEE-----GPGHRGISAFLVPADTPGVTVGR---IWDKMGMRGsGTGElvfDDVRVPEDNLLGEE---GGG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 363 WRMLVECLSVGRgITLPSNSTGGVKSVALATGAYAHIRRQFKISIGKMEGIEEPLARIAGNAYVMDA----AASLITYGI 438
Cdd:cd00567 183 FELAMKGLNVGR-LLLAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLllyrAAWLLDQGP 261
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446895789 439 mlgEKPAVLSAIVKYHCTHRGQQSIIDAMDITGGKGimLGESNFLARAYQGAPIAITVEGANilTRSMMIFGQ 511
Cdd:cd00567 262 ---DEARLEAAMAKLFATEAAREVADLAMQIHGGRG--YSREYPVERYLRDARAARIAEGTA--EIQRLIIAR 327
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
152-474 |
1.52e-23 |
|
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: 103.64 E-value: 1.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 152 PPELWAYLKEHRFFAMIIKKEYGGLEFSAYAQSRVLQKLSGVSGILAITVGVPNSLGPGELLQHyGTEEQKNHYLPRLAR 231
Cdd:cd01156 35 PRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVALSYGAHSNLCINQIYRN-GSAAQKEKYLPKLIS 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 232 GQEIPCFALTSPEAGSDagaipdtgVVCM---GEWQGQQVLgmrLTWNKRYITLAPIATVLgLAFKLSDPDRllggeEEL 308
Cdd:cd01156 114 GEHIGALAMSEPNAGSD--------VVSMklrAEKKGDRYV---LNGSKMWITNGPDADTL-VVYAKTDPSA-----GAH 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 309 GITCALIPTSTPGVEIGRRHFPLNVpfqngptRG--------NDIFVPIDYIIGGpkmAGQGWRMLVECLSVGRGItLPS 380
Cdd:cd01156 177 GITAFIVEKGMPGFSRAQKLDKLGM-------RGsntcelvfEDCEVPEENILGG---ENKGVYVLMSGLDYERLV-LAG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 381 NSTGGVKSVALATGAYAHIRRQFKISIGKMEGIEEPLARI-----AGNAYVMDAAASLITygimlGEKPAVLSAIVKYHC 455
Cdd:cd01156 246 GPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMytrlnASRSYLYTVAKACDR-----GNMDPKDAAGVILYA 320
|
330
....*....|....*....
gi 446895789 456 THRGQQSIIDAMDITGGKG 474
Cdd:cd01156 321 AEKATQVALDAIQILGGNG 339
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
119-423 |
1.34e-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: 97.81 E-value: 1.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 119 QLTAEEQAFLDGpVEEAC------RMANDFqithELADLPPELWAYLKEHRFFAMIIKkEYGGLEFSAYAQSRVLQKLSG 192
Cdd:cd01151 12 LLTEEERAIRDT-AREFCqeelapRVLEAY----REEKFDRKIIEEMGELGLLGATIK-GYGCAGLSSVAYGLIAREVER 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 193 VSGILAITVGVPNSLGPGELlQHYGTEEQKNHYLPRLARGQEIPCFALTSPEAGSDAGaipdtGVVCMGEWQGQqvlGMR 272
Cdd:cd01151 86 VDSGYRSFMSVQSSLVMLPI-YDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPG-----GMETRARKDGG---GYK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 273 LTWNKRYITLAPIATVLGLAFKLSDPDRLLGgeeelgitcALIPTSTPGVEIGRRH--FPLNVPfQNGPTRGNDIFVPID 350
Cdd:cd01151 157 LNGSKTWITNSPIADVFVVWARNDETGKIRG---------FILERGMKGLSAPKIQgkFSLRAS-ITGEIVMDNVFVPEE 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446895789 351 YIIGGPKmagqGWRMLVECLSVGR-GItlpsnSTG--GVKSVALATG-AYAHIRRQFKISIGKMEGIEEPLARIAGN 423
Cdd:cd01151 227 NLLPGAE----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 |
1.63e-19 |
|
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: 84.44 E-value: 1.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 121 TAEEQAFLDG----------PVEEACRMANDFqitheladlPPELWAYLKEHRFFAMIIKKEYGGLEFSAYAQSRVLQKL 190
Cdd:pfam02771 1 TEEQEALRDTvrefaeeeiaPHAAEWDEEGEF---------PRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEEL 71
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 446895789 191 SGVSGILAITVGVPNSLGpGELLQHYGTEEQKNHYLPRLARG 232
Cdd:pfam02771 72 ARADASVALALSVHSSLG-APPILRFGTEEQKERYLPKLASG 112
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
120-474 |
1.32e-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: 85.57 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 120 LTAEEQAFLDgpveeacrMANDFQiTHELA----------DLPPELWAYLKEHRFFAMIIKKEYGGLEFSAYAQSRVLQK 189
Cdd:cd01162 1 LNEEQRAIQE--------VARAFA-AKEMAphaadwdqkkHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 190 LSGVSGILAITVGVPNSLGpgELLQHYGTEEQKNHYLPRLARGQEIPCFALTSPEAGSDAGAIPDTGVVCMGEWQgqqvl 269
Cdd:cd01162 72 LSTGCVSTAAYISIHNMCA--WMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYV----- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 270 gmrLTWNKRYITLAPIATVLGLAFKLsdpdrllGGEEELGITCALIPTSTPGVEIGRRHFPLNVPFQngPTRG---NDIF 346
Cdd:cd01162 145 ---LNGSKAFISGAGDSDVYVVMART-------GGEGPKGISCFVVEKGTPGLSFGANEKKMGWNAQ--PTRAvifEDCR 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 347 VPIDYIIGGpkmAGQGWRMLVECLSVGRgITLPSNSTGGVKSVALATGAYAHIRRQFKISIGKMEGIEEPLAriagnayv 426
Cdd:cd01162 213 VPVENRLGG---EGQGFGIAMAGLNGGR-LNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLA-------- 280
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 446895789 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 |
1.30e-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: 79.47 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 152 PPELWAYLKEHRFFAMIIKKEYGGLEFSAYAQSRVLQKLsGVSGILAITVGVPNSLGpGELLQHYGTEEQKNHYLPRLAR 231
Cdd:cd01160 32 PREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEEL-ARAGGSGPGLSLHTDIV-SPYITRAGSPEQKERVLPQMVA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 232 GQEIPCFALTSPEAGSDAGAIPDTGVVCMGEWQgqqvlgmrLTWNKRYITLAPIATVLGLAFKLSDPDRLLGgeeelGIT 311
Cdd:cd01160 110 GKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYV--------LNGSKTFITNGMLADVVIVVARTGGEARGAG-----GIS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 312 CALIPTSTPGVEIGRRHFPLNVPFQNGPTRG-NDIFVPIDYIIGgpkMAGQGWRMLVECLSVGRgITLPSNSTGGVKSVA 390
Cdd:cd01160 177 LFLVERGTPGFSRGRKLKKMGWKAQDTAELFfDDCRVPAENLLG---EENKGFYYLMQNLPQER-LLIAAGALAAAEFML 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 391 LATGAYAHIRRQFKISIGKMEGIEEPLARIAGNAYVMDAAASLITYGIMLGEKPAVLSAIVKYHCTHRGQQSIIDAMDIT 470
Cdd:cd01160 253 EETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKYWATELQNRVAYECVQLH 332
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 446895789 471 GGKGIMLGESnfLARAYQGAPIAITVEGAN-----ILTRSM 506
Cdd:cd01160 333 GGWGYMREYP--IARAYRDARVQPIYGGTTeimkeLISRQM 371
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
155-474 |
9.07e-13 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 71.06 E-value: 9.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 155 LWAYLKEHRFFAMIIKKEYGGLEFSAYAQSRVLQKLSGVSGILAITVGVPNSLGPGELLQHyGTEEQKNHYLPRLARGQE 234
Cdd:PLN02519 64 LWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGSVGLSYGAHSNLCINQLVRN-GTPAQKEKYLPKLISGEH 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 235 IPCFALTSPEAGSDagaipdtgVVCMGEWQGQQVLGMRLTWNKRYITLAPIATVLgLAFKLSDPDrllGGEEelGITCAL 314
Cdd:PLN02519 143 VGALAMSEPNSGSD--------VVSMKCKAERVDGGYVLNGNKMWCTNGPVAQTL-VVYAKTDVA---AGSK--GITAFI 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 315 IPTSTPGVEIGRRHFPLNVpfqngptRGNDI--------FVPIDYIIGGpkmAGQGWRMLVECLSVGRgITLPSNSTGGV 386
Cdd:PLN02519 209 IEKGMPGFSTAQKLDKLGM-------RGSDTcelvfencFVPEENVLGQ---EGKGVYVMMSGLDLER-LVLAAGPLGLM 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 387 KSVALATGAYAHIRRQFKISIGKMEGIEEPLARI-----AGNAYVMDAAASLITygimlGEKPAVLSAIVKYHCTHRGQQ 461
Cdd:PLN02519 278 QACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMytslqSSRSYVYSVARDCDN-----GKVDRKDCAGVILCAAERATQ 352
|
330
....*....|...
gi 446895789 462 SIIDAMDITGGKG 474
Cdd:PLN02519 353 VALQAIQCLGGNG 365
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
237-335 |
2.02e-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: 63.84 E-value: 2.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 237 CFALTSPEAGSDAGAIPDTGVVCMGEwqgqqvlGMRLTWNKRYITLAPIATVLGLAFKLSDPDRllggeeELGITCALIP 316
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAADGDGG-------GWVLNGTKWWITNAGIADLFLVLARTGGDDR------HGGISLFLVP 67
|
90
....*....|....*....
gi 446895789 317 TSTPGVEIGRRHFPLNVPF 335
Cdd:pfam02770 68 KDAPGVSVRRIETKLGVRG 86
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
169-474 |
3.62e-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: 65.68 E-value: 3.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 169 IKKEYGGLEFSAYAQSRVLQKLS-GVSGILAITVGvpNSLGPGELLQHyGTEEQKNHYLPRLARGQEIPCFALTSPEAGS 247
Cdd:cd01157 51 IPEDCGGLGLGTFDTCLITEELAyGCTGVQTAIEA--NSLGQMPVIIS-GNDEQKKKYLGRMTEEPLMCAYCVTEPGAGS 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 248 DAGAIPDTGVVCMGEW--QGQQVL---GMRLTWnkrYITLAPiatvlglafklSDPDRLLGGEEelGITCALIPTSTPGV 322
Cdd:cd01157 128 DVAGIKTKAEKKGDEYiiNGQKMWitnGGKANW---YFLLAR-----------SDPDPKCPASK--AFTGFIVEADTPGI 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 323 EIGRRHfpLNVPFQNGPTRG---NDIFVPIDYIIGGPkmaGQGWRMLVECLSVGRgitlPSNSTG--GVKSVALATGA-Y 396
Cdd:cd01157 192 QPGRKE--LNMGQRCSDTRGitfEDVRVPKENVLIGE---GAGFKIAMGAFDKTR----PPVAAGavGLAQRALDEATkY 262
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446895789 397 AHIRRQFKISIGKMEGIEEPLARIAGNAYVMDAAASLITYGIMLGEKPAVLSAIVKYHCTHRGQQSIIDAMDITGGKG 474
Cdd:cd01157 263 ALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAKAFAADIANQLATDAVQIFGGNG 340
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
120-427 |
1.69e-10 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 63.72 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 120 LTAEEQAFldgpveeacRMANDFQITHELADLPPELWAylKEHRFFAMIIK-----------KEYG--GLEFSAYAQSrv 186
Cdd:PLN02526 29 LTPEEQAL---------RKRVRECMEKEVAPIMTEYWE--KAEFPFHIIPKlgslgiaggtiKGYGcpGLSITASAIA-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 187 LQKLSGVSGILAITVGVPNSLGPGELLQhYGTEEQKNHYLPRLARGQEIPCFALTSPEAGSDAGAIPDTGVVCMGEW--Q 264
Cdd:PLN02526 96 TAEVARVDASCSTFILVHSSLAMLTIAL-CGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWilN 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 265 GQqvlgmrltwnKRYITLAPIATVLGLAFKLSDPDRLLG---GEEELGITCALIPTstpgvEIGRRHfplnvpFQNGPTR 341
Cdd:PLN02526 175 GQ----------KRWIGNSTFADVLVIFARNTTTNQINGfivKKGAPGLKATKIEN-----KIGLRM------VQNGDIV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 342 GNDIFVPIDYIIGGPkmagQGWRMLVECLSVGRgITLPSNSTGGVKSVALATGAYAHIRRQFKISIGKMEGIEEPLARIA 421
Cdd:PLN02526 234 LKDVFVPDEDRLPGV----NSFQDTNKVLAVSR-VMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRML 308
|
....*.
gi 446895789 422 GNAYVM 427
Cdd:PLN02526 309 GNIQAM 314
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
171-375 |
2.97e-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: 62.75 E-value: 2.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 171 KEYGGLEFSAYAQSRVLQKL--SGVSGILAItVGVpNSLGPgeLLQHYGTEEQKNHYLPRLARGQEIPCFALTSPEAGSD 248
Cdd:cd01152 56 KEYGGRGASLMEQLIFREEMaaAGAPVPFNQ-IGI-DLAGP--TILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSD 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 249 AGAIPDTGVVCMGEWQ--GQQVlgmrltWNkryiTLAPIATVLGLAFKlSDPDrllgGEEELGITCALIPTSTPGVEIgR 326
Cdd:cd01152 132 LAGLRTRAVRDGDDWVvnGQKI------WT----SGAHYADWAWLLVR-TDPE----APKHRGISILLVDMDSPGVTV-R 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446895789 327 RHFPLnvpfqNGPTRGN-----DIFVPIDYIIGGPkmaGQGWRMLVECLSVGRG 375
Cdd:cd01152 196 PIRSI-----NGGEFFNevfldDVRVPDANRVGEV---NDGWKVAMTTLNFERV 241
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
360-500 |
7.99e-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: 54.95 E-value: 7.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 360 GQGWRMLVECLSVGRgITLPSNSTGGVKSVALATGAYAHIRRQFKISIGKMEGIEEPLARIAGNAYVMDAAASLITYGIM 439
Cdd:pfam00441 1 GRGFRVAMETLNHER-LAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALD 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446895789 440 LGEKPAVLSAIVKYHCTHRGQQSIIDAMDITGGKGIMLGESnfLARAYQGAPIAITVEGAN 500
Cdd:pfam00441 80 AGGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYP--VERLYRDARVLRIGEGTS 138
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
123-474 |
9.30e-09 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 58.20 E-value: 9.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 123 EEQAFLDGPVEEAcrMAND-----FQITHELADLPPELWAYLKEHRFFAMIIKKEYGGLEFSAYAQSRVLQKLSgvsgil 197
Cdd:PRK12341 7 EEQELLLASIREL--ITRNfpeeyFRTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEVS------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 198 aiTVGVP-NSLGPGELL---QHYGTEEQ-KNHYLPRLARGQEIPCFALTSPEAGSDAGAIPDTGVVCMGEwqgqqvlgMR 272
Cdd:PRK12341 79 --KCGAPaFLITNGQCIhsmRRFGSAEQlRKTAESTLETGDPAYALALTEPGAGSDNNSATTTYTRKNGK--------VY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 273 LTWNKRYITLAPIAT-VLGLAFKLSDPDRllggeeELGITCALIPTSTPGVEIGRRHfplNVPFQNGPTRG---NDIFVP 348
Cdd:PRK12341 149 LNGQKTFITGAKEYPyMLVLARDPQPKDP------KKAFTLWWVDSSKPGIKINPLH---KIGWHMLSTCEvylDNVEVE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 349 IDYIIGgpkMAGQGWRMLVECLSVGRgITLPSNSTGGVKSVALATGAYAHIRRQFKISIGKMEGIEEPLARIAGNAYVMD 428
Cdd:PRK12341 220 ESDLVG---EEGMGFLNVMYNFEMER-LINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMR 295
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 446895789 429 AAASLITYGIMLGEKPAVLSAIVKYHCTHRGQQSIIDAMDITGGKG 474
Cdd:PRK12341 296 NMVYKVAWQADNGQSLRTSAALAKLYCARTAMEVIDDAIQIMGGLG 341
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
166-328 |
7.95e-08 |
|
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: 55.47 E-value: 7.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 166 AMIIKKEYGGLEFSAYAQSRVLQKLSGVSGILAITVGvpnSLGPGELLQHYGTEEQKNHYLPRLARGQEIPCFALTSPEA 245
Cdd:cd01153 52 ALGVPEEYGGQGLPITVYSALAEIFSRGDAPLMYASG---TQGAAATLLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 246 GSDAG-----AIPDTGvvcmGEWqgqqvlgmRLTWNKRYIT--------------LA----PIATVLGLAFKLSdPDRLL 302
Cdd:cd01153 129 GSDLGalrtkAVYQAD----GSW--------RINGVKRFISagehdmsenivhlvLArsegAPPGVKGLSLFLV-PKFLD 195
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446895789 303 GG----------EEELGI----TCALIPTSTPGVEIGRRH 328
Cdd:cd01153 196 DGerngvtvariEEKMGLhgspTCELVFDNAKGELIGEEG 235
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
119-475 |
5.66e-07 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 52.53 E-value: 5.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 119 QLTAEEQAFLDGPVEeacRMAND-----FQITHELADLPPELWAYLKEHRFFAMIIKKEYGGLEFSAYAQSRVLQKLSGV 193
Cdd:PRK03354 4 NLNDEQELFVAGIRE---LMASEnweayFAECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 194 SGILAITVGVPNslGPGELLQHyGTEEQKNHYLPRLARGQEIPCFALTSPEAGSDAGAIPDTGVVCMGEwqgqqvlgMRL 273
Cdd:PRK03354 81 GAPTYVLYQLPG--GFNTFLRE-GTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGK--------VYL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 274 TWNKRYIT-LAPIATVLGLAFKLSDPDRLLGGEeelgitcALIPTSTPGVEIG-------RRHFPLNVPFQNGPTRGNDI 345
Cdd:PRK03354 150 NGSKCFITsSAYTPYIVVMARDGASPDKPVYTE-------WFVDMSKPGIKVTkleklglRMDSCCEITFDDVELDEKDM 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 346 FvpidyiiggpKMAGQGWRMLVECLSVGRGITLPSNStgGVKSVALATGA-YAHIRRQFKISIGKMEGIEEPLARIAGNA 424
Cdd:PRK03354 223 F----------GREGNGFNRVKEEFDHERFLVALTNY--GTAMCAFEDAArYANQRVQFGEAIGRFQLIQEKFAHMAIKL 290
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 446895789 425 YVMDAAASLITYGIMLGEKPAVLSAIVKYHCTHRGQQSIIDAMDITGGKGI 475
Cdd:PRK03354 291 NSMKNMLYEAAWKADNGTITSGDAAMCKYFCANAAFEVVDSAMQVLGGVGI 341
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
211-355 |
2.12e-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: 47.77 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 211 ELLQHYGTEEQKNHYLPRLARGQEIPCFALTSPE-AGSDAgaipdTGVVCMGEWQGQQVLgmrLTWNKRYITLA-----P 284
Cdd:cd01155 102 EVLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDA-----TNIECSIERDGDDYV---INGRKWWSSGAgdprcK 173
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446895789 285 IATVLGlafkLSDPDRLLGGEEELGItcaLIPTSTPGVEIGRrhfPLNV------PFQNGPTRGNDIFVPIDYIIGG 355
Cdd:cd01155 174 IAIVMG----RTDPDGAPRHRQQSMI---LVPMDTPGVTIIR---PLSVfgyddaPHGHAEITFDNVRVPASNLILG 240
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
133-259 |
5.99e-05 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 46.79 E-value: 5.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446895789 133 EEACRMANDFQITheladLPP---ELWAYLKEHRFFAMIIKKEYGG--LEFSAYAQSRVLQKLSGVSgiLAITVGVpnSL 207
Cdd:PTZ00456 84 SEGCVLLKDGNVT-----TPKgfkEAYQALKAGGWTGISEPEEYGGqaLPLSVGFITRELMATANWG--FSMYPGL--SI 154
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 446895789 208 GPGELLQHYGTEEQKNHYLPRLARGQEIPCFALTSPEAGSDAGAIPDTGVVC 259
Cdd:PTZ00456 155 GAANTLMAWGSEEQKEQYLTKLVSGEWSGTMCLTEPQCGTDLGQVKTKAEPS 206
|
|
| |
