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Conserved domains on  [gi|493863265|ref|WP_006810010|]
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MULTISPECIES: acyl-CoA dehydrogenase FadE [Enterobacter]

Protein Classification

acyl-CoA dehydrogenase( domain architecture ID 17609095)

acyl-CoA dehydrogenase catalyzes the dehydrogenation of acyl-coenzyme A (CoA)

Graphical summary

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List of domain hits

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: 1781.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265   3 ILSILATVVLLGVLFYHRVSLLLSSLILLAWTAALGVAGLWNIWVLVPLAIILLPFNLTPMRKSMISAPVFKGFRKVMPP 82
Cdd:NF038187   1 LLSILAMLVLLGALAYHRVSLLTSSLILAAVMAAGTAAGLWSLWLWLPFLIIALPLNVPSIRQSLISAPALKAFRKVMPE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265  83 MSRTEKEAIDAGTTWWEGDLFQGNPDWKKLHNYPQPRLTAEEQAFIDGPVEEACRMANDFAITHEMADLPPELWAYLKEH 162
Cdd:NF038187  81 MSSTEKEAIDAGTTWWEADLFRGNPDWKKLHNYPKPRLTAEEQAFLDGPVEEVCRMVNDFQITHELADLPPEVWQYLKDH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 163 RFFAMIIKKEYGGLEFSAYAQARVLQKLAGVSGILAITVGVPNSLGPGELLQHYGTEEQKDHYLPRLARGQEIPCFALTS 242
Cdd:NF038187 161 RFFAMIIKKEYGGLEFSAYAQSRVLQKLAGVSSILASTVGVPNSLGPGELLQHYGTEEQKDHYLPRLARGEEIPCFALTS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 243 PEAGSDAGAIPDTGVVCMGEWQGQQVLGMRLTWNKRYITLAPIATVLGLAFKLSDPEKLLGGEEELGITCALIPTSTPGV 322
Cdd:NF038187 241 PEAGSDAGSIPDFGVVCKGEWQGEEVLGMRLTWNKRYITLAPVATVLGLAFKLRDPDHLLGDKEELGITCALIPTDTPGV 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 323 EIGRRHFPLNVPFQNGPTRGQDIFVPIDYIIGGPKMAGQGWRMLVECLSVGRGITLPSNSTGGLKSVAMGIGAYAHIRRQ 402
Cdd:NF038187 321 EIGRRHFPLNVPFQNGPTRGKDIFVPLDFIIGGPKMAGQGWRMLVECLSVGRGITLPSNSTGGLKSAALATGAYARIRRQ 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 403 FKISIGKMEGIEEPLARIAGNAYVMDAAASLITYGIMLGEKPAVLSAIVKYHCTHRAQQSIIDAMDIAGGKGIMLGEGNF 482
Cdd:NF038187 401 FKLPIGKMEGIEEPLARIAGNAYLMDAAATLTTTGIDLGEKPSVISAIVKYHCTHRGQRSIIDAMDIHGGKGICLGPNNF 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 483 LARGYQGAPIAITVEGANILTRSMMIFGQGAIRCHPYVLEEMAAAQNND----VDAFDKLLFKHIGHVGSNKVRSFWLGL 558
Cdd:NF038187 481 LARGYQGAPIAITVEGANILTRSMIIYGQGAIRCHPYVLAEMEAAQDNDseqaLNDFDKALFGHIGFVGSNLVRSFWLGL 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 559 TRGLTSATPTGDATKRYYQHLNRLSANLALLSDVSMAVLGGSLKRRERISARLGDVLSQIFLASAVLKRYDDEGRQEADL 638
Cdd:NF038187 561 TNGRFSSAPYKDATRRYYQQLNRLSANLALLSDVSMAVLGGSLKRRERISARLGDILSQLYLASATLKRYEDEGRQKEDL 640
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 639 PLVHWGVQDAMYQAEQAIDDLLANFPNRFVAGALRVVIFPTGRHHLAPSDKLDHKVAKILQVPSATRSRIGRGQYLAPTP 718
Cdd:NF038187 641 PLVHWAVQDSLYQAEQALDDLLRNFPNRLVAGLLRVIIFPFGRPLKAPSDKLDHKVAKILQTPSATRSRLGRGQYLTPSE 720
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 719 HNPVGLLEEALLDVMAADPIHQKICKQLGKNLPFTRLDELAKQALAGGIIDNSEAAILVKAEESRLRSINVDDFEPEELA 798
Cdd:NF038187 721 HNPVGLLEQALKDILAAEPIHDRVCKAAGKRLPFMRLDKLAEEGLALGVITEEEAALLERAEASRLRSINVDDFDPDELA 800
                        810
                 ....*....|....*.
gi 493863265 799 TQPVKLPEKHRKPEAA 814
Cdd:NF038187 801 AKPAKRPAKQKQDEAA 816
 
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: 1781.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265   3 ILSILATVVLLGVLFYHRVSLLLSSLILLAWTAALGVAGLWNIWVLVPLAIILLPFNLTPMRKSMISAPVFKGFRKVMPP 82
Cdd:NF038187   1 LLSILAMLVLLGALAYHRVSLLTSSLILAAVMAAGTAAGLWSLWLWLPFLIIALPLNVPSIRQSLISAPALKAFRKVMPE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265  83 MSRTEKEAIDAGTTWWEGDLFQGNPDWKKLHNYPQPRLTAEEQAFIDGPVEEACRMANDFAITHEMADLPPELWAYLKEH 162
Cdd:NF038187  81 MSSTEKEAIDAGTTWWEADLFRGNPDWKKLHNYPKPRLTAEEQAFLDGPVEEVCRMVNDFQITHELADLPPEVWQYLKDH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 163 RFFAMIIKKEYGGLEFSAYAQARVLQKLAGVSGILAITVGVPNSLGPGELLQHYGTEEQKDHYLPRLARGQEIPCFALTS 242
Cdd:NF038187 161 RFFAMIIKKEYGGLEFSAYAQSRVLQKLAGVSSILASTVGVPNSLGPGELLQHYGTEEQKDHYLPRLARGEEIPCFALTS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 243 PEAGSDAGAIPDTGVVCMGEWQGQQVLGMRLTWNKRYITLAPIATVLGLAFKLSDPEKLLGGEEELGITCALIPTSTPGV 322
Cdd:NF038187 241 PEAGSDAGSIPDFGVVCKGEWQGEEVLGMRLTWNKRYITLAPVATVLGLAFKLRDPDHLLGDKEELGITCALIPTDTPGV 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 323 EIGRRHFPLNVPFQNGPTRGQDIFVPIDYIIGGPKMAGQGWRMLVECLSVGRGITLPSNSTGGLKSVAMGIGAYAHIRRQ 402
Cdd:NF038187 321 EIGRRHFPLNVPFQNGPTRGKDIFVPLDFIIGGPKMAGQGWRMLVECLSVGRGITLPSNSTGGLKSAALATGAYARIRRQ 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 403 FKISIGKMEGIEEPLARIAGNAYVMDAAASLITYGIMLGEKPAVLSAIVKYHCTHRAQQSIIDAMDIAGGKGIMLGEGNF 482
Cdd:NF038187 401 FKLPIGKMEGIEEPLARIAGNAYLMDAAATLTTTGIDLGEKPSVISAIVKYHCTHRGQRSIIDAMDIHGGKGICLGPNNF 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 483 LARGYQGAPIAITVEGANILTRSMMIFGQGAIRCHPYVLEEMAAAQNND----VDAFDKLLFKHIGHVGSNKVRSFWLGL 558
Cdd:NF038187 481 LARGYQGAPIAITVEGANILTRSMIIYGQGAIRCHPYVLAEMEAAQDNDseqaLNDFDKALFGHIGFVGSNLVRSFWLGL 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 559 TRGLTSATPTGDATKRYYQHLNRLSANLALLSDVSMAVLGGSLKRRERISARLGDVLSQIFLASAVLKRYDDEGRQEADL 638
Cdd:NF038187 561 TNGRFSSAPYKDATRRYYQQLNRLSANLALLSDVSMAVLGGSLKRRERISARLGDILSQLYLASATLKRYEDEGRQKEDL 640
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 639 PLVHWGVQDAMYQAEQAIDDLLANFPNRFVAGALRVVIFPTGRHHLAPSDKLDHKVAKILQVPSATRSRIGRGQYLAPTP 718
Cdd:NF038187 641 PLVHWAVQDSLYQAEQALDDLLRNFPNRLVAGLLRVIIFPFGRPLKAPSDKLDHKVAKILQTPSATRSRLGRGQYLTPSE 720
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 719 HNPVGLLEEALLDVMAADPIHQKICKQLGKNLPFTRLDELAKQALAGGIIDNSEAAILVKAEESRLRSINVDDFEPEELA 798
Cdd:NF038187 721 HNPVGLLEQALKDILAAEPIHDRVCKAAGKRLPFMRLDKLAEEGLALGVITEEEAALLERAEASRLRSINVDDFDPDELA 800
                        810
                 ....*....|....*.
gi 493863265 799 TQPVKLPEKHRKPEAA 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: 1587.92  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265  42 LWNIWVLVPLAIILLPFNLTPMRKSMISAPVFKGFRKVMPPMSRTEKEAIDAGTTWWEGDLFQGNPDWKKLHNYPQPRLT 121
Cdd:PRK09463   1 LWSLWLLVPLAIILLPLNLPPLRRSLISAPLLKWFRKVLPPMSQTEREALEAGTVWWEGELFSGKPDWKKLLNYPKPTLT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 122 AEEQAFIDGPVEEACRMANDFAITHEMADLPPELWAYLKEHRFFAMIIKKEYGGLEFSAYAQARVLQKLAGVSGILAITV 201
Cdd:PRK09463  81 AEEQAFLDGPVEELCRMVNDWQITHELADLPPEVWQFIKEHGFFGMIIPKEYGGLEFSAYAHSRVLQKLASRSGTLAVTV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 202 GVPNSLGPGELLQHYGTEEQKDHYLPRLARGQEIPCFALTSPEAGSDAGAIPDTGVVCMGEWQGQQVLGMRLTWNKRYIT 281
Cdd:PRK09463 161 MVPNSLGPGELLLHYGTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGSIPDTGVVCKGEWQGEEVLGMRLTWNKRYIT 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 282 LAPIATVLGLAFKLSDPEKLLGGEEELGITCALIPTSTPGVEIGRRHFPLNVPFQNGPTRGQDIFVPIDYIIGGPKMAGQ 361
Cdd:PRK09463 241 LAPIATVLGLAFKLYDPDGLLGDKEDLGITCALIPTDTPGVEIGRRHFPLNVPFQNGPTRGKDVFIPLDYIIGGPKMAGQ 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 362 GWRMLVECLSVGRGITLPSNSTGGLKSVAMGIGAYAHIRRQFKISIGKMEGIEEPLARIAGNAYVMDAAASLITYGIMLG 441
Cdd:PRK09463 321 GWRMLMECLSVGRGISLPSNSTGGAKLAALATGAYARIRRQFKLPIGKFEGIEEPLARIAGNAYLMDAARTLTTAAVDLG 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 442 EKPAVLSAIVKYHCTHRAQQSIIDAMDIAGGKGIMLGEGNFLARGYQGAPIAITVEGANILTRSMMIFGQGAIRCHPYVL 521
Cdd:PRK09463 401 EKPSVLSAIAKYHLTERGRQVINDAMDIHGGKGICLGPNNFLARAYQAAPIAITVEGANILTRSLMIFGQGAIRCHPYVL 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 522 EEMAAAQNND---VDAFDKLLFKHIGHVGSNKVRSFWLGLTRGLTSATPTGDATKRYYQHLNRLSANLALLSDVSMAVLG 598
Cdd:PRK09463 481 KEMEAAQNNDkqaLKAFDKALFGHIGFVVSNAVRSFWLGLTGGRLSAAPVDDATKRYYRQLNRLSANLALLADVSMLVLG 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 599 GSLKRRERISARLGDVLSQIFLASAVLKRYDDEGRQEADLPLVHWGVQDAMYQAEQAIDDLLANFPNRFVAGALRVVIFP 678
Cdd:PRK09463 561 GSLKRRERLSARLGDILSQLYLASAVLKRYEDEGRPEADLPLVHWAVQDALYQAEQALDGLLRNFPNRVVAGLLRVLVFP 640
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 679 TGRHHLAPSDKLDHKVAKILQVPSATRSRIGRGQYLAPTPHNPVGLLEEALLDVMAADPIHQKICKQLGKN-LPFTRLDE 757
Cdd:PRK09463 641 LGRRYRAPSDKLDHQVAKLLQTPSATRDRLTRGQYLPPSENNPVGRLEEALLDVIAAEPIEKKICKALKKGkLPFLRLDE 720
                        730       740       750       760       770
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 493863265 758 LAKQALAGGIIDNSEAAILVKAEESRLRSINVDDFEPEELATQPVKLPEKHRKPEAA 814
Cdd:PRK09463 721 LADEALAAGVISEEEAALLREAEEARLRVINVDDFDPEELAAKPVKLPEKVQKVEAA 777
ACDH_C pfam09317
Acyl-CoA dehydrogenase, C-terminal, bacterial type; This C-terminal domain is functionally ...
514-792 1.77e-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: 467.35  E-value: 1.77e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265  514 IRCHPYVLEEMAAAQNND----VDAFDKLLFKHIGHVGSNKVRSFWLGLTRGLTSATPTGDATKRYYQHLNRLSANLALL 589
Cdd:pfam09317   1 IRCHPYVLKEMEAAQNEDkeqaLKAFDRALFGHIGFALSNAARSLVLGLTGGRFASAPVAGETARYYRQLNRLSAAFALL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265  590 SDVSMAVLGGSLKRRERISARLGDVLSQIFLASAVLKRYDDEGRQEADLPLVHWGVQDAMYQAEQAIDDLLANFPNRFVA 669
Cdd:pfam09317  81 ADLAMLVLGGSLKRRERLSARLGDVLSQLYLASAVLKRFEDEGRPEADLPLVHWAMQDALYQAQQALDGVLRNFPNRPVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265  670 GALRVVIFPTGRHHLAPSDKLDHKVAKILQVPSATRSRIGRGQYLAPTPHNPVGLLEEALLDVMAADPIHQKICKQLGK- 748
Cdd:pfam09317 161 WLLRVLVFPLGRRYRKPSDKLGHEVAQLLQEPGEARDRLTAGVYLPDDPDDPVGRLEAAFQAVLAAEPLEKKLKKAIKAg 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 493863265  749 NLPFTRLDELAKQALAGGIIDNSEAAILVKAEESRLRSINVDDF 792
Cdd:pfam09317 241 KLPKLTLEELIEEALEKGVITEEEAELLREAEALRLDVIQVDDF 284
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
119-508 1.69e-86

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: 279.42  E-value: 1.69e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 119 RLTAEEQAFIDgPVEEAC--RMANDFAITHEMADLPPELWAYLKEHRFFAMIIKKEYGGLEFSAYAQARVLQKLAGVSGI 196
Cdd:COG1960    4 ELTEEQRALRD-EVREFAeeEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADAS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 197 LAITVGVPNslGPGELLQHYGTEEQKDHYLPRLARGQEIPCFALTSPEAGSDAGAIPDTGVvcmgeWQGQqvlGMRLTWN 276
Cdd:COG1960   83 LALPVGVHN--GAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAV-----RDGD---GYVLNGQ 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 277 KRYITLAPIATVLGLAFKLsDPEKllggeEELGITCALIPTSTPGVEIGRRHFPLNV-PFQNGPTRGQDIFVPIDYIIGG 355
Cdd:COG1960  153 KTFITNAPVADVILVLART-DPAA-----GHRGISLFLVPKDTPGVTVGRIEDKMGLrGSDTGELFFDDVRVPAENLLGE 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 356 PkmaGQGWRMLVECLSVGRgITLPSNSTGGLKSVAMGIGAYAHIRRQFKISIGKMEGIEEPLARIAGNAYVMDAAASLIT 435
Cdd:COG1960  227 E---GKGFKIAMSTLNAGR-LGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAA 302
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493863265 436 YGIMLGEKPAVLSAIVKYHCTHRAQQSIIDAMDIAGGKGIMLGEGnfLARGYQGAPIAITVEGANILTRSMMI 508
Cdd:COG1960  303 WLLDAGEDAALEAAMAKLFATEAALEVADEALQIHGGYGYTREYP--LERLYRDARILTIYEGTNEIQRLIIA 373
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
145-500 1.77e-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: 141.64  E-value: 1.77e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 145 THEMadlPPELWAYLKEHRFFAMIIKKEYGGLEFSAYAQARVLQKLAGVSGILAITVGVPNSLGPGELLQhYGTEEQKDH 224
Cdd:cd01158   28 KGEF---PREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVIVSVHNSLGANPIIK-FGTEEQKKK 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 225 YLPRLARGQEIPCFALTSPEAGSDAGAIPDTGVVCMGEWqgqqvlgmRLTWNKRYITLAPIATVLgLAFKLSDPEKllgG 304
Cdd:cd01158  104 YLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDY--------VLNGSKMWITNGGEADFY-IVFAVTDPSK---G 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 305 EEelGITCALIPTSTPGVEIGRRHFPLNVpfQNGPT---RGQDIFVPIDYIIGGPkmaGQGWRMLVECLSVGRgItlpsn 381
Cdd:cd01158  172 YR--GITAFIVERDTPGLSVGKKEDKLGI--RGSSTtelIFEDVRVPKENILGEE---GEGFKIAMQTLDGGR-I----- 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 382 stgGLKSVAMGIG--------AYAHIRRQFKISIGKMEGIEEPLARIAgnayVMDAAASLITYG-IML---GEKPAVLSA 449
Cdd:cd01158  239 ---GIAAQALGIAqaaldaavDYAKERKQFGKPIADFQGIQFKLADMA----TEIEAARLLTYKaARLkdnGEPFIKEAA 311
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 493863265 450 IVKYHCTHRAQQSIIDAMDIAGGKGIMlgeGNFLA-RGYQGAPIAITVEGAN 500
Cdd:cd01158  312 MAKLFASEVAMRVTTDAVQIFGGYGYT---KDYPVeRYYRDAKITEIYEGTS 360
 
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: 1781.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265   3 ILSILATVVLLGVLFYHRVSLLLSSLILLAWTAALGVAGLWNIWVLVPLAIILLPFNLTPMRKSMISAPVFKGFRKVMPP 82
Cdd:NF038187   1 LLSILAMLVLLGALAYHRVSLLTSSLILAAVMAAGTAAGLWSLWLWLPFLIIALPLNVPSIRQSLISAPALKAFRKVMPE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265  83 MSRTEKEAIDAGTTWWEGDLFQGNPDWKKLHNYPQPRLTAEEQAFIDGPVEEACRMANDFAITHEMADLPPELWAYLKEH 162
Cdd:NF038187  81 MSSTEKEAIDAGTTWWEADLFRGNPDWKKLHNYPKPRLTAEEQAFLDGPVEEVCRMVNDFQITHELADLPPEVWQYLKDH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 163 RFFAMIIKKEYGGLEFSAYAQARVLQKLAGVSGILAITVGVPNSLGPGELLQHYGTEEQKDHYLPRLARGQEIPCFALTS 242
Cdd:NF038187 161 RFFAMIIKKEYGGLEFSAYAQSRVLQKLAGVSSILASTVGVPNSLGPGELLQHYGTEEQKDHYLPRLARGEEIPCFALTS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 243 PEAGSDAGAIPDTGVVCMGEWQGQQVLGMRLTWNKRYITLAPIATVLGLAFKLSDPEKLLGGEEELGITCALIPTSTPGV 322
Cdd:NF038187 241 PEAGSDAGSIPDFGVVCKGEWQGEEVLGMRLTWNKRYITLAPVATVLGLAFKLRDPDHLLGDKEELGITCALIPTDTPGV 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 323 EIGRRHFPLNVPFQNGPTRGQDIFVPIDYIIGGPKMAGQGWRMLVECLSVGRGITLPSNSTGGLKSVAMGIGAYAHIRRQ 402
Cdd:NF038187 321 EIGRRHFPLNVPFQNGPTRGKDIFVPLDFIIGGPKMAGQGWRMLVECLSVGRGITLPSNSTGGLKSAALATGAYARIRRQ 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 403 FKISIGKMEGIEEPLARIAGNAYVMDAAASLITYGIMLGEKPAVLSAIVKYHCTHRAQQSIIDAMDIAGGKGIMLGEGNF 482
Cdd:NF038187 401 FKLPIGKMEGIEEPLARIAGNAYLMDAAATLTTTGIDLGEKPSVISAIVKYHCTHRGQRSIIDAMDIHGGKGICLGPNNF 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 483 LARGYQGAPIAITVEGANILTRSMMIFGQGAIRCHPYVLEEMAAAQNND----VDAFDKLLFKHIGHVGSNKVRSFWLGL 558
Cdd:NF038187 481 LARGYQGAPIAITVEGANILTRSMIIYGQGAIRCHPYVLAEMEAAQDNDseqaLNDFDKALFGHIGFVGSNLVRSFWLGL 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 559 TRGLTSATPTGDATKRYYQHLNRLSANLALLSDVSMAVLGGSLKRRERISARLGDVLSQIFLASAVLKRYDDEGRQEADL 638
Cdd:NF038187 561 TNGRFSSAPYKDATRRYYQQLNRLSANLALLSDVSMAVLGGSLKRRERISARLGDILSQLYLASATLKRYEDEGRQKEDL 640
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 639 PLVHWGVQDAMYQAEQAIDDLLANFPNRFVAGALRVVIFPTGRHHLAPSDKLDHKVAKILQVPSATRSRIGRGQYLAPTP 718
Cdd:NF038187 641 PLVHWAVQDSLYQAEQALDDLLRNFPNRLVAGLLRVIIFPFGRPLKAPSDKLDHKVAKILQTPSATRSRLGRGQYLTPSE 720
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 719 HNPVGLLEEALLDVMAADPIHQKICKQLGKNLPFTRLDELAKQALAGGIIDNSEAAILVKAEESRLRSINVDDFEPEELA 798
Cdd:NF038187 721 HNPVGLLEQALKDILAAEPIHDRVCKAAGKRLPFMRLDKLAEEGLALGVITEEEAALLERAEASRLRSINVDDFDPDELA 800
                        810
                 ....*....|....*.
gi 493863265 799 TQPVKLPEKHRKPEAA 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: 1587.92  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265  42 LWNIWVLVPLAIILLPFNLTPMRKSMISAPVFKGFRKVMPPMSRTEKEAIDAGTTWWEGDLFQGNPDWKKLHNYPQPRLT 121
Cdd:PRK09463   1 LWSLWLLVPLAIILLPLNLPPLRRSLISAPLLKWFRKVLPPMSQTEREALEAGTVWWEGELFSGKPDWKKLLNYPKPTLT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 122 AEEQAFIDGPVEEACRMANDFAITHEMADLPPELWAYLKEHRFFAMIIKKEYGGLEFSAYAQARVLQKLAGVSGILAITV 201
Cdd:PRK09463  81 AEEQAFLDGPVEELCRMVNDWQITHELADLPPEVWQFIKEHGFFGMIIPKEYGGLEFSAYAHSRVLQKLASRSGTLAVTV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 202 GVPNSLGPGELLQHYGTEEQKDHYLPRLARGQEIPCFALTSPEAGSDAGAIPDTGVVCMGEWQGQQVLGMRLTWNKRYIT 281
Cdd:PRK09463 161 MVPNSLGPGELLLHYGTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGSIPDTGVVCKGEWQGEEVLGMRLTWNKRYIT 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 282 LAPIATVLGLAFKLSDPEKLLGGEEELGITCALIPTSTPGVEIGRRHFPLNVPFQNGPTRGQDIFVPIDYIIGGPKMAGQ 361
Cdd:PRK09463 241 LAPIATVLGLAFKLYDPDGLLGDKEDLGITCALIPTDTPGVEIGRRHFPLNVPFQNGPTRGKDVFIPLDYIIGGPKMAGQ 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 362 GWRMLVECLSVGRGITLPSNSTGGLKSVAMGIGAYAHIRRQFKISIGKMEGIEEPLARIAGNAYVMDAAASLITYGIMLG 441
Cdd:PRK09463 321 GWRMLMECLSVGRGISLPSNSTGGAKLAALATGAYARIRRQFKLPIGKFEGIEEPLARIAGNAYLMDAARTLTTAAVDLG 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 442 EKPAVLSAIVKYHCTHRAQQSIIDAMDIAGGKGIMLGEGNFLARGYQGAPIAITVEGANILTRSMMIFGQGAIRCHPYVL 521
Cdd:PRK09463 401 EKPSVLSAIAKYHLTERGRQVINDAMDIHGGKGICLGPNNFLARAYQAAPIAITVEGANILTRSLMIFGQGAIRCHPYVL 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 522 EEMAAAQNND---VDAFDKLLFKHIGHVGSNKVRSFWLGLTRGLTSATPTGDATKRYYQHLNRLSANLALLSDVSMAVLG 598
Cdd:PRK09463 481 KEMEAAQNNDkqaLKAFDKALFGHIGFVVSNAVRSFWLGLTGGRLSAAPVDDATKRYYRQLNRLSANLALLADVSMLVLG 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 599 GSLKRRERISARLGDVLSQIFLASAVLKRYDDEGRQEADLPLVHWGVQDAMYQAEQAIDDLLANFPNRFVAGALRVVIFP 678
Cdd:PRK09463 561 GSLKRRERLSARLGDILSQLYLASAVLKRYEDEGRPEADLPLVHWAVQDALYQAEQALDGLLRNFPNRVVAGLLRVLVFP 640
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 679 TGRHHLAPSDKLDHKVAKILQVPSATRSRIGRGQYLAPTPHNPVGLLEEALLDVMAADPIHQKICKQLGKN-LPFTRLDE 757
Cdd:PRK09463 641 LGRRYRAPSDKLDHQVAKLLQTPSATRDRLTRGQYLPPSENNPVGRLEEALLDVIAAEPIEKKICKALKKGkLPFLRLDE 720
                        730       740       750       760       770
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 493863265 758 LAKQALAGGIIDNSEAAILVKAEESRLRSINVDDFEPEELATQPVKLPEKHRKPEAA 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: 1190.92  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265  46 WVLVPLAIILLPFNLTPMRKSMISAPVFKGFRKVMPPMSRTEKEAIDAGTTWWEGDLFQGNPDWKKLHNYPQPRLTAEEQ 125
Cdd:PRK13026   4 LIILLLIAIVLVFAVKPLRRQFITRPVFKFFKKVLPPLSDTEREAMEAGDVWWEGELFSGKPDWQKLHSYPKPTLTAEEQ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 126 AFIDGPVEEACRMANDFAITHEMADLPPELWAYLKEHRFFAMIIKKEYGGLEFSAYAQARVLQKLAGVSGILAITVGVPN 205
Cdd:PRK13026  84 AFIDNEVETLLTMLDDWDIVQNRKDLPPEVWDYLKKEGFFALIIPKEYGGKGFSAYANSTIVSKIATRSVSAAVTVMVPN 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 206 SLGPGELLQHYGTEEQKDHYLPRLARGQEIPCFALTSPEAGSDAGAIPDTGVVCMGEWQGQQVLGMRLTWNKRYITLAPI 285
Cdd:PRK13026 164 SLGPGELLTHYGTQEQKDYWLPRLADGTEIPCFALTGPEAGSDAGAIPDTGIVCRGEFEGEEVLGLRLTWDKRYITLAPV 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 286 ATVLGLAFKLSDPEKLLGGEEELGITCALIPTSTPGVEIGRRHFPLNVPFQNGPTRGQDIFVPIDYIIGGPKMAGQGWRM 365
Cdd:PRK13026 244 ATVLGLAFKLRDPDGLLGDKKELGITCALIPTDHPGVEIGRRHNPLGMAFMNGTTRGKDVFIPLDWIIGGPDYAGRGWRM 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 366 LVECLSVGRGITLPSNSTGGLKSVAMGIGAYAHIRRQFKISIGKMEGIEEPLARIAGNAYVMDAAASLITYGIMLGEKPA 445
Cdd:PRK13026 324 LVECLSAGRGISLPALGTASGHMATRTTGAYAYVRRQFGMPIGQFEGVQEALARIAGNTYLLEAARRLTTTGLDLGVKPS 403
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 446 VLSAIVKYHCTHRAQQSIIDAMDIAGGKGIMLGEGNFLARGYQGAPIAITVEGANILTRSMMIFGQGAIRCHPYVLEEMA 525
Cdd:PRK13026 404 VVTAIAKYHMTELARDVVNDAMDIHAGKGIQLGPKNYLGHAYMAVPIAITVEGANILTRNLMIFGQGATRCHPYVLAEME 483
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 526 AAQNND----VDAFDKLLFKHIGHVGSNKVRSFWLGLTRGLTSATPTGDATKRYYQHLNRLSANLALLSDVSMAVLGGSL 601
Cdd:PRK13026 484 AAAMEDehegLEAFDSLLFKHIGYAARNAFRALFSALTGSRFISAPVSGETAQYYKDMSRLSAALALLADLSMLILGGDL 563
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 602 KRRERISARLGDVLSQIFLASAVLKRYDDEGRQEADLPLVHWGVQDAMYQAEQAIDDLLANFPNRFVAGALRVVIFPTGR 681
Cdd:PRK13026 564 KRKEMLSARLGDVLSQLYLASATLKRFEDNGRQQDDLPAVHYAMQDCLHLAAKALDEFLRNFPNRPVAWLLRALIFPLGN 643
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 682 HHLAPSDKLDHKVAKILQVPSATRSRIGRGQYLAPTPHNPVGLLEEALLDVMAADPIHQKICKQL--GKNLPFTRLDELA 759
Cdd:PRK13026 644 HFRAPSDKLARQLAELMMTPGPARDRLTALCYIFEGDKDGVARVEQAFLAQYAVKPLYKKLKKAQreGKLPRKVPLLELF 723
                        730       740       750       760
                 ....*....|....*....|....*....|....*....|....*..
gi 493863265 760 KQALAGGIIDNSEAAILVKAEESRLRSINVDDFEPEEL---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 1.77e-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: 467.35  E-value: 1.77e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265  514 IRCHPYVLEEMAAAQNND----VDAFDKLLFKHIGHVGSNKVRSFWLGLTRGLTSATPTGDATKRYYQHLNRLSANLALL 589
Cdd:pfam09317   1 IRCHPYVLKEMEAAQNEDkeqaLKAFDRALFGHIGFALSNAARSLVLGLTGGRFASAPVAGETARYYRQLNRLSAAFALL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265  590 SDVSMAVLGGSLKRRERISARLGDVLSQIFLASAVLKRYDDEGRQEADLPLVHWGVQDAMYQAEQAIDDLLANFPNRFVA 669
Cdd:pfam09317  81 ADLAMLVLGGSLKRRERLSARLGDVLSQLYLASAVLKRFEDEGRPEADLPLVHWAMQDALYQAQQALDGVLRNFPNRPVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265  670 GALRVVIFPTGRHHLAPSDKLDHKVAKILQVPSATRSRIGRGQYLAPTPHNPVGLLEEALLDVMAADPIHQKICKQLGK- 748
Cdd:pfam09317 161 WLLRVLVFPLGRRYRKPSDKLGHEVAQLLQEPGEARDRLTAGVYLPDDPDDPVGRLEAAFQAVLAAEPLEKKLKKAIKAg 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 493863265  749 NLPFTRLDELAKQALAGGIIDNSEAAILVKAEESRLRSINVDDF 792
Cdd:pfam09317 241 KLPKLTLEELIEEALEKGVITEEEAELLREAEALRLDVIQVDDF 284
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
119-508 1.69e-86

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: 279.42  E-value: 1.69e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 119 RLTAEEQAFIDgPVEEAC--RMANDFAITHEMADLPPELWAYLKEHRFFAMIIKKEYGGLEFSAYAQARVLQKLAGVSGI 196
Cdd:COG1960    4 ELTEEQRALRD-EVREFAeeEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADAS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 197 LAITVGVPNslGPGELLQHYGTEEQKDHYLPRLARGQEIPCFALTSPEAGSDAGAIPDTGVvcmgeWQGQqvlGMRLTWN 276
Cdd:COG1960   83 LALPVGVHN--GAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAV-----RDGD---GYVLNGQ 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 277 KRYITLAPIATVLGLAFKLsDPEKllggeEELGITCALIPTSTPGVEIGRRHFPLNV-PFQNGPTRGQDIFVPIDYIIGG 355
Cdd:COG1960  153 KTFITNAPVADVILVLART-DPAA-----GHRGISLFLVPKDTPGVTVGRIEDKMGLrGSDTGELFFDDVRVPAENLLGE 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 356 PkmaGQGWRMLVECLSVGRgITLPSNSTGGLKSVAMGIGAYAHIRRQFKISIGKMEGIEEPLARIAGNAYVMDAAASLIT 435
Cdd:COG1960  227 E---GKGFKIAMSTLNAGR-LGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAA 302
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493863265 436 YGIMLGEKPAVLSAIVKYHCTHRAQQSIIDAMDIAGGKGIMLGEGnfLARGYQGAPIAITVEGANILTRSMMI 508
Cdd:COG1960  303 WLLDAGEDAALEAAMAKLFATEAALEVADEALQIHGGYGYTREYP--LERLYRDARILTIYEGTNEIQRLIIA 373
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
145-500 1.77e-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: 141.64  E-value: 1.77e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 145 THEMadlPPELWAYLKEHRFFAMIIKKEYGGLEFSAYAQARVLQKLAGVSGILAITVGVPNSLGPGELLQhYGTEEQKDH 224
Cdd:cd01158   28 KGEF---PREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVIVSVHNSLGANPIIK-FGTEEQKKK 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 225 YLPRLARGQEIPCFALTSPEAGSDAGAIPDTGVVCMGEWqgqqvlgmRLTWNKRYITLAPIATVLgLAFKLSDPEKllgG 304
Cdd:cd01158  104 YLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDY--------VLNGSKMWITNGGEADFY-IVFAVTDPSK---G 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 305 EEelGITCALIPTSTPGVEIGRRHFPLNVpfQNGPT---RGQDIFVPIDYIIGGPkmaGQGWRMLVECLSVGRgItlpsn 381
Cdd:cd01158  172 YR--GITAFIVERDTPGLSVGKKEDKLGI--RGSSTtelIFEDVRVPKENILGEE---GEGFKIAMQTLDGGR-I----- 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 382 stgGLKSVAMGIG--------AYAHIRRQFKISIGKMEGIEEPLARIAgnayVMDAAASLITYG-IML---GEKPAVLSA 449
Cdd:cd01158  239 ---GIAAQALGIAqaaldaavDYAKERKQFGKPIADFQGIQFKLADMA----TEIEAARLLTYKaARLkdnGEPFIKEAA 311
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 493863265 450 IVKYHCTHRAQQSIIDAMDIAGGKGIMlgeGNFLA-RGYQGAPIAITVEGAN 500
Cdd:cd01158  312 MAKLFASEVAMRVTTDAVQIFGGYGYT---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 493863265 101 DLFQGNPDWKKLhnYPQPRLTAEEQA----FIDGPVEEACRMANDFAITHEMADLPPELWAYLKEHRFFAMIIKKEYGGL 176
Cdd:cd01161    5 NMFLGDIVTKQV--FPYPSVLTEEQTeelnMLVGPVEKFFEEVNDPAKNDQLEKIPRKTLTQLKELGLFGLQVPEEYGGL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 177 EFSAYAQARVLQKLaGVSGILAITVGVPNSLG-PGELLqhYGTEEQKDHYLPRLARGQEIPCFALTSPEAGSDAGAIPDT 255
Cdd:cd01161   83 GLNNTQYARLAEIV-GMDLGFSVTLGAHQSIGfKGILL--FGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 256 GVVcmgEWQGQQVLgmrLTWNKRYITLAPIATVLGLAFKLsdPEKLLGGEEELGITCALIPTSTPGVEIGRRHFPLNVPF 335
Cdd:cd01161  160 AVL---SEDGKHYV---LNGSKIWITNGGIADIFTVFAKT--EVKDATGSVKDKITAFIVERSFGGVTNGPPEKKMGIKG 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 336 QNGPT-RGQDIFVPIDYIIGgpkMAGQGWRMLVECLSVGRgITLPSNSTGGLKSVAMGIGAYAHIRRQFKISIGKMEGIE 414
Cdd:cd01161  232 SNTAEvYFEDVKIPVENVLG---EVGDGFKVAMNILNNGR-FGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQ 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 415 EPLARIAGNAYVMDAAASLITyGIM---LGEKPAVLSAIVKYHCTHRAQQSIIDAMDIAGGKGIMLGEGnfLARGYQGAP 491
Cdd:cd01161  308 EKLANMAILQYATESMAYMTS-GNMdrgLKAEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYG--VERVLRDLR 384
                        410       420
                 ....*....|....*....|..
gi 493863265 492 IAITVEGANILTRsMMIFGQGA 513
Cdd:cd01161  385 IFRIFEGTNEILR-LFIALTGL 405
ACAD cd00567
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
207-511 3.58e-33

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: 130.87  E-value: 3.58e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 207 LGPGELLQHYGTEEQKDHYLPRLARGQEIPCFALTSPEAGSDAGAIPDTGVVCMGEWqgqqvlgmRLTWNKRYITLAPIA 286
Cdd:cd00567   42 LLGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGY--------VLNGRKIFISNGGDA 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 287 TVLGLAFKLSDPekllgGEEELGITCALIPTSTPGVEIGRrhfPLNVPFQNG-PTRG---QDIFVPIDYIIGGPkmaGQG 362
Cdd:cd00567  114 DLFIVLARTDEE-----GPGHRGISAFLVPADTPGVTVGR---IWDKMGMRGsGTGElvfDDVRVPEDNLLGEE---GGG 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 363 WRMLVECLSVGRgITLPSNSTGGLKSvAMGIGA-YAHIRRQFKISIGKMEGIEEPLARIAGNAYVMDA----AASLITYG 437
Cdd:cd00567  183 FELAMKGLNVGR-LLLAAVALGAARA-ALDEAVeYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLllyrAAWLLDQG 260
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493863265 438 ImlgEKPAVLSAIVKYHCTHRAQQSIIDAMDIAGGKGimLGEGNFLARGYQGAPIAITVEGANilTRSMMIFGQ 511
Cdd:cd00567  261 P---DEARLEAAMAKLFATEAAREVADLAMQIHGGRG--YSREYPVERYLRDARAARIAEGTA--EIQRLIIAR 327
IVD cd01156
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ...
152-474 5.04e-24

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: 104.80  E-value: 5.04e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 152 PPELWAYLKEHRFFAMIIKKEYGGLEFSAYAQARVLQKLAGVSGILAITVGVPNSLGPGELLQHyGTEEQKDHYLPRLAR 231
Cdd:cd01156   35 PRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVALSYGAHSNLCINQIYRN-GSAAQKEKYLPKLIS 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 232 GQEIPCFALTSPEAGSDagaipdtgVVCM---GEWQGQQVLgmrLTWNKRYITLAPIATVLgLAFKLSDPEKllggeEEL 308
Cdd:cd01156  114 GEHIGALAMSEPNAGSD--------VVSMklrAEKKGDRYV---LNGSKMWITNGPDADTL-VVYAKTDPSA-----GAH 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 309 GITCALIPTSTPGVEIGRRHFPLNVpfqngptRG--------QDIFVPIDYIIGGpkmAGQGWRMLVECLSVGRGItLPS 380
Cdd:cd01156  177 GITAFIVEKGMPGFSRAQKLDKLGM-------RGsntcelvfEDCEVPEENILGG---ENKGVYVLMSGLDYERLV-LAG 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 381 NSTGGLKSVAMGIGAYAHIRRQFKISIGKMEGIEEPLARI-----AGNAYVMDAAASLITygimlGEKPAVLSAIVKYHC 455
Cdd:cd01156  246 GPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMytrlnASRSYLYTVAKACDR-----GNMDPKDAAGVILYA 320
                        330
                 ....*....|....*....
gi 493863265 456 THRAQQSIIDAMDIAGGKG 474
Cdd:cd01156  321 AEKATQVALDAIQILGGNG 339
GCD cd01151
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ...
120-478 3.33e-22

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: 99.74  E-value: 3.33e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 120 LTAEEQAFIDGpVEEAC--RMANDFAITHEMADLPPELWAYLKEHRFFAMIIKkEYGGLEFSAYAQARVLQKLAGVSGIL 197
Cdd:cd01151   13 LTEEERAIRDT-AREFCqeELAPRVLEAYREEKFDRKIIEEMGELGLLGATIK-GYGCAGLSSVAYGLIAREVERVDSGY 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 198 AITVGVPNSLGPGELlQHYGTEEQKDHYLPRLARGQEIPCFALTSPEAGSDAGaipdtGVVCMGEWQGQqvlGMRLTWNK 277
Cdd:cd01151   91 RSFMSVQSSLVMLPI-YDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPG-----GMETRARKDGG---GYKLNGSK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 278 RYITLAPIATVLGLAFKLSDPEKLLGgeeelgitcALIPTSTPGVEIGRRH--FPLNVPfQNGPTRGQDIFVPIDYIIGG 355
Cdd:cd01151  162 TWITNSPIADVFVVWARNDETGKIRG---------FILERGMKGLSAPKIQgkFSLRAS-ITGEIVMDNVFVPEENLLPG 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 356 PKmagqGWRMLVECLSVGR-GItlpsnSTGGLkSVAMGIGA----YAHIRRQFKISIGKMEGIEEPLARIAGNayvmdaa 430
Cdd:cd01151  232 AE----GLRGPFKCLNNARyGI-----AWGAL-GAAEDCYHtarqYVLDRKQFGRPLAAFQLVQKKLADMLTE------- 294
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 493863265 431 aslITYGIMLGEKPAVLS----------AIVKYHCTHRAQQSIIDAMDIAGGKGIMLG 478
Cdd:cd01151  295 ---IALGLLACLRVGRLKdqgkatpeqiSLLKRNNCGKALEIARTAREMLGGNGISDE 349
Acyl-CoA_dh_N pfam02771
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ...
121-232 1.17e-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: 87.90  E-value: 1.17e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265  121 TAEEQAFIDGPVEEACRMANDFAITHEMAD-LPPELWAYLKEHRFFAMIIKKEYGGLEFSAYAQARVLQKLAGVSGILAI 199
Cdd:pfam02771   1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGeFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVAL 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 493863265  200 TVGVPNSLGpGELLQHYGTEEQKDHYLPRLARG 232
Cdd:pfam02771  81 ALSVHSSLG-APPILRFGTEEQKERYLPKLASG 112
IBD cd01162
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ...
120-474 9.94e-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: 82.88  E-value: 9.94e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 120 LTAEEQAFIDgpveeacrMANDFAiTHEMA----------DLPPELWAYLKEHRFFAMIIKKEYGGLEFSAYAQARVLQK 189
Cdd:cd01162    1 LNEEQRAIQE--------VARAFA-AKEMAphaadwdqkkHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEA 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 190 LAGVSGILAITVGVPNSLGpgELLQHYGTEEQKDHYLPRLARGQEIPCFALTSPEAGSDAGAIPDTGVVCMGEWQgqqvl 269
Cdd:cd01162   72 LSTGCVSTAAYISIHNMCA--WMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYV----- 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 270 gmrLTWNKRYITLAPIATVLGLAFKLsdpekllGGEEELGITCALIPTSTPGVEIGRRHFPLNVPFQngPTRG---QDIF 346
Cdd:cd01162  145 ---LNGSKAFISGAGDSDVYVVMART-------GGEGPKGISCFVVEKGTPGLSFGANEKKMGWNAQ--PTRAvifEDCR 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 347 VPIDYIIGGpkmAGQGWRMLVECLSVGRgITLPSNSTGGLKSVAMGIGAYAHIRRQFKISIGKMEGIEEPLAriagnayv 426
Cdd:cd01162  213 VPVENRLGG---EGQGFGIAMAGLNGGR-LNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLA-------- 280
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 493863265 427 mDAAASLITYGIML---------GEKPAV-LSAIVKYHCTHRAQQSIIDAMDIAGGKG 474
Cdd:cd01162  281 -DMATELVASRLMVrraasaldrGDPDAVkLCAMAKRFATDECFDVANQALQLHGGYG 337
LCAD cd01160
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ...
152-476 4.01e-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: 74.84  E-value: 4.01e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 152 PPELWAYLKEHRFFAMIIKKEYGGLEFSAYAQARVLQKLAgVSGILAITVGVPNSLGpGELLQHYGTEEQKDHYLPRLAR 231
Cdd:cd01160   32 PREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELA-RAGGSGPGLSLHTDIV-SPYITRAGSPEQKERVLPQMVA 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 232 GQEIPCFALTSPEAGSDAGAIPDTGVVCMGEWQgqqvlgmrLTWNKRYITLAPIATVLGLAFKlSDPEKLLGGeeelGIT 311
Cdd:cd01160  110 GKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYV--------LNGSKTFITNGMLADVVIVVAR-TGGEARGAG----GIS 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 312 CALIPTSTPGVEIGRRHFPLNVPFQNGPTRG-QDIFVPIDYIIGgpkMAGQGWRMLVECLSVGRgITLPSNSTGGLKSVA 390
Cdd:cd01160  177 LFLVERGTPGFSRGRKLKKMGWKAQDTAELFfDDCRVPAENLLG---EENKGFYYLMQNLPQER-LLIAAGALAAAEFML 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 391 MGIGAYAHIRRQFKISIGKMEGIEEPLARIAGNAYVMDAAASLITYGIMLGEKPAVLSAIVKYHCTHRAQQSIIDAMDIA 470
Cdd:cd01160  253 EETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKYWATELQNRVAYECVQLH 332

                 ....*.
gi 493863265 471 GGKGIM 476
Cdd:cd01160  333 GGWGYM 338
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
155-474 3.90e-13

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 72.22  E-value: 3.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 155 LWAYLKEHRFFAMIIKKEYGGLEFSAYAQARVLQKLAGVSGILAITVGVPNSLGPGELLQHyGTEEQKDHYLPRLARGQE 234
Cdd:PLN02519  64 LWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGSVGLSYGAHSNLCINQLVRN-GTPAQKEKYLPKLISGEH 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 235 IPCFALTSPEAGSDagaipdtgVVCMGEWQGQQVLGMRLTWNKRYITLAPIATVLgLAFKLSDPEkllGGEEelGITCAL 314
Cdd:PLN02519 143 VGALAMSEPNSGSD--------VVSMKCKAERVDGGYVLNGNKMWCTNGPVAQTL-VVYAKTDVA---AGSK--GITAFI 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 315 IPTSTPGVEIGRRHFPLNVpfqngptRGQDI--------FVPIDYIIGGpkmAGQGWRMLVECLSVGRgITLPSNSTGGL 386
Cdd:PLN02519 209 IEKGMPGFSTAQKLDKLGM-------RGSDTcelvfencFVPEENVLGQ---EGKGVYVMMSGLDLER-LVLAAGPLGLM 277
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 387 KSVAMGIGAYAHIRRQFKISIGKMEGIEEPLARI-----AGNAYVMDAAASLITygimlGEKPAVLSAIVKYHCTHRAQQ 461
Cdd:PLN02519 278 QACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMytslqSSRSYVYSVARDCDN-----GKVDRKDCAGVILCAAERATQ 352
                        330
                 ....*....|...
gi 493863265 462 SIIDAMDIAGGKG 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 5.47e-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: 5.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265  237 CFALTSPEAGSDAGAIPDTGVVCMGEwqgqqvlGMRLTWNKRYITLAPIATVLGLAFKLSDPEKllggeeELGITCALIP 316
Cdd:pfam02770   1 AFALTEPGAGSDVASLKTTAADGDGG-------GWVLNGTKWWITNAGIADLFLVLARTGGDDR------HGGISLFLVP 67
                          90
                  ....*....|....*....
gi 493863265  317 TSTPGVEIGRRHFPLNVPF 335
Cdd:pfam02770  68 KDAPGVSVRRIETKLGVRG 86
PLN02526 PLN02526
acyl-coenzyme A oxidase
120-427 6.52e-12

acyl-coenzyme A oxidase


Pssm-ID: 178141 [Multi-domain]  Cd Length: 412  Bit Score: 68.34  E-value: 6.52e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 120 LTAEEQAFidgpveeacRMANDFAITHEMADLPPELWAylKEHRFFAMIIK-----------KEYG--GLEFSAYAQArv 186
Cdd:PLN02526  29 LTPEEQAL---------RKRVRECMEKEVAPIMTEYWE--KAEFPFHIIPKlgslgiaggtiKGYGcpGLSITASAIA-- 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 187 LQKLAGVSGILAITVGVPNSLGPGELLQhYGTEEQKDHYLPRLARGQEIPCFALTSPEAGSDAGAIPDTGVVCMGEW--Q 264
Cdd:PLN02526  96 TAEVARVDASCSTFILVHSSLAMLTIAL-CGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWilN 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 265 GQqvlgmrltwnKRYITLAPIATVLGLAFKLSDPEKLLG---GEEELGITCALIPTstpgvEIGRRHfplnvpFQNGPTR 341
Cdd:PLN02526 175 GQ----------KRWIGNSTFADVLVIFARNTTTNQINGfivKKGAPGLKATKIEN-----KIGLRM------VQNGDIV 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 342 GQDIFVPIDYIIGGPkmagQGWRMLVECLSVGRgITLPSNSTGglksVAMGIGAYAHI----RRQFKISIGKMEGIEEPL 417
Cdd:PLN02526 234 LKDVFVPDEDRLPGV----NSFQDTNKVLAVSR-VMVAWQPIG----ISMGVYDMCHRylkeRKQFGAPLAAFQINQEKL 304
                        330
                 ....*....|
gi 493863265 418 ARIAGNAYVM 427
Cdd:PLN02526 305 VRMLGNIQAM 314
MCAD cd01157
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ...
169-474 9.03e-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: 67.61  E-value: 9.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 169 IKKEYGGLEFSAYAQARVLQKLA-GVSGILAITVGvpNSLGPGELLQHyGTEEQKDHYLPRLARGQEIPCFALTSPEAGS 247
Cdd:cd01157   51 IPEDCGGLGLGTFDTCLITEELAyGCTGVQTAIEA--NSLGQMPVIIS-GNDEQKKKYLGRMTEEPLMCAYCVTEPGAGS 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 248 DAGAIPDTGVVCMGEW--QGQQVL---GMRLTWnkrYITLAPiatvlglafklSDPE-KLLGGEeelGITCALIPTSTPG 321
Cdd:cd01157  128 DVAGIKTKAEKKGDEYiiNGQKMWitnGGKANW---YFLLAR-----------SDPDpKCPASK---AFTGFIVEADTPG 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 322 VEIGRRHfpLNVPFQNGPTRG---QDIFVPIDYIIGGPkmaGQGWRMLVECLSVGRgitlPSNSTG--GLKSVAMGIGA- 395
Cdd:cd01157  191 IQPGRKE--LNMGQRCSDTRGitfEDVRVPKENVLIGE---GAGFKIAMGAFDKTR----PPVAAGavGLAQRALDEATk 261
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493863265 396 YAHIRRQFKISIGKMEGIEEPLARIAGNAYVMDAAASLITYGIMLGEKPAVLSAIVKYHCTHRAQQSIIDAMDIAGGKG 474
Cdd:cd01157  262 YALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAKAFAADIANQLATDAVQIFGGNG 340
ACAD_fadE6_17_26 cd01152
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ...
171-375 6.22e-11

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: 65.06  E-value: 6.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 171 KEYGGLEFSAYAQARVLQKLA-----GVSGILAItvgvpNSLGPgeLLQHYGTEEQKDHYLPRLARGQEIPCFALTSPEA 245
Cdd:cd01152   56 KEYGGRGASLMEQLIFREEMAaagapVPFNQIGI-----DLAGP--TILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGA 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 246 GSDAGAIPDTGVVCMGEWQ--GQQVlgmrltWNkryiTLAPIATVLGLAFKlSDPEkllgGEEELGITCALIPTSTPGVE 323
Cdd:cd01152  129 GSDLAGLRTRAVRDGDDWVvnGQKI------WT----SGAHYADWAWLLVR-TDPE----APKHRGISILLVDMDSPGVT 193
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 493863265 324 I-------GRRHFplNVPFQNgptrgqDIFVPIDYIIGGPkmaGQGWRMLVECLSVGRG 375
Cdd:cd01152  194 VrpirsinGGEFF--NEVFLD------DVRVPDANRVGEV---NDGWKVAMTTLNFERV 241
PRK12341 PRK12341
acyl-CoA dehydrogenase;
119-474 1.68e-10

acyl-CoA dehydrogenase;


Pssm-ID: 183454 [Multi-domain]  Cd Length: 381  Bit Score: 63.59  E-value: 1.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 119 RLTAEEQAFIDGPVEEACRMA--NDFAITHEMADLPPELWAYLKEHRFFAMIIKKEYGGLEFSAYAQARVLQKLAgvsgi 196
Cdd:PRK12341   4 SLTEEQELLLASIRELITRNFpeEYFRTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEVS----- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 197 laiTVGVP-NSLGPGELL---QHYGTEEQK----DHYLprlARGQEIPCFALTSPEAGSDAGAIPDTGVVCMGEwqgqqv 268
Cdd:PRK12341  79 ---KCGAPaFLITNGQCIhsmRRFGSAEQLrktaESTL---ETGDPAYALALTEPGAGSDNNSATTTYTRKNGK------ 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 269 lgMRLTWNKRYITLA---PIATVLGLAFKLSDPEKllggeeelGITCALIPTSTPGVEIGRRHfplNVPFQNGPTRG--- 342
Cdd:PRK12341 147 --VYLNGQKTFITGAkeyPYMLVLARDPQPKDPKK--------AFTLWWVDSSKPGIKINPLH---KIGWHMLSTCEvyl 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 343 QDIFVPIDYIIGgpkMAGQGWRMLVECLSVGRgITLPSNSTGGLKSVAMGIGAYAHIRRQFKISIGKMEGIEEPLARIAG 422
Cdd:PRK12341 214 DNVEVEESDLVG---EEGMGFLNVMYNFEMER-LINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAI 289
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 493863265 423 NAYVMDAAASLITYGIMLGEKPAVLSAIVKYHCTHRAQQSIIDAMDIAGGKG 474
Cdd:PRK12341 290 KIENMRNMVYKVAWQADNGQSLRTSAALAKLYCARTAMEVIDDAIQIMGGLG 341
PRK03354 PRK03354
crotonobetainyl-CoA dehydrogenase; Validated
119-475 2.71e-09

crotonobetainyl-CoA dehydrogenase; Validated


Pssm-ID: 179566 [Multi-domain]  Cd Length: 380  Bit Score: 59.85  E-value: 2.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 119 RLTAEEQAFIDGPVEeacRMAND-----FAITHEMADLPPELWAYLKEHRFFAMIIKKEYGGLEFSAYAQARVLQKLAGV 193
Cdd:PRK03354   4 NLNDEQELFVAGIRE---LMASEnweayFAECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGRL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 194 SGILAITVGVPNslGPGELLQHyGTEEQKDHYLPRLARGQEIPCFALTSPEAGSDAGAIPDTGVVCMGEwqgqqvlgMRL 273
Cdd:PRK03354  81 GAPTYVLYQLPG--GFNTFLRE-GTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGK--------VYL 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 274 TWNKRYIT-LAPIATVLGLAFKLSDPEKLLGGEeelgitcALIPTSTPGVEIG-------RRHFPLNVPFQNGPTRGQDI 345
Cdd:PRK03354 150 NGSKCFITsSAYTPYIVVMARDGASPDKPVYTE-------WFVDMSKPGIKVTkleklglRMDSCCEITFDDVELDEKDM 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 346 FvpidyiiggpKMAGQGWRMLVECLSVGRGITLPSNStgGLKSVAMGIGA-YAHIRRQFKISIGKMEGIEEPLARIAGNA 424
Cdd:PRK03354 223 F----------GREGNGFNRVKEEFDHERFLVALTNY--GTAMCAFEDAArYANQRVQFGEAIGRFQLIQEKFAHMAIKL 290
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 493863265 425 YVMDAAASLITYGIMLGEKPAVLSAIVKYHCTHRAQQSIIDAMDIAGGKGI 475
Cdd:PRK03354 291 NSMKNMLYEAAWKADNGTITSGDAAMCKYFCANAAFEVVDSAMQVLGGVGI 341
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
360-500 7.40e-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: 55.34  E-value: 7.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265  360 GQGWRMLVECLSVGRgITLPSNSTGGLKSVAMGIGAYAHIRRQFKISIGKMEGIEEPLARIAGNAYVMDAAASLITYGIM 439
Cdd:pfam00441   1 GRGFRVAMETLNHER-LAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALD 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493863265  440 LGEKPAVLSAIVKYHCTHRAQQSIIDAMDIAGGKGIMLGEGnfLARGYQGAPIAITVEGAN 500
Cdd:pfam00441  80 AGGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYP--VERLYRDARVLRIGEGTS 138
ACAD_fadE5 cd01153
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ...
166-328 9.91e-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: 52.01  E-value: 9.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 166 AMIIKKEYGGLEF-----SAYAQARvlqkLAGVSGILAITVGVPNSlgpgELLQHYGTEEQKDHYLPRLARGQEIPCFAL 240
Cdd:cd01153   52 ALGVPEEYGGQGLpitvySALAEIF----SRGDAPLMYASGTQGAA----ATLLAHGTEAQREKWIPRLAEGEWTGTMCL 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 241 TSPEAGSDAG-----AIPDTGvvcmGEWqgqqvlgmRLTWNKRYIT--------------LA----PIATVLGLAFKLSd 297
Cdd:cd01153  124 TEPDAGSDLGalrtkAVYQAD----GSW--------RINGVKRFISagehdmsenivhlvLArsegAPPGVKGLSLFLV- 190
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 493863265 298 PEKLLGG----------EEELGI----TCALIPTSTPGVEIGRRH 328
Cdd:cd01153  191 PKFLDDGerngvtvariEEKMGLhgspTCELVFDNAKGELIGEEG 235
PTZ00456 PTZ00456
acyl-CoA dehydrogenase; Provisional
133-259 3.32e-05

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185635 [Multi-domain]  Cd Length: 622  Bit Score: 47.56  E-value: 3.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 133 EEACRMANDFAIThemadLPP---ELWAYLKEHRFFAMIIKKEYGG--LEFSAYAQARVLQKLAGVSgiLAITVGVpnSL 207
Cdd:PTZ00456  84 SEGCVLLKDGNVT-----TPKgfkEAYQALKAGGWTGISEPEEYGGqaLPLSVGFITRELMATANWG--FSMYPGL--SI 154
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 493863265 208 GPGELLQHYGTEEQKDHYLPRLARGQEIPCFALTSPEAGSDAGAIPDTGVVC 259
Cdd:PTZ00456 155 GAANTLMAWGSEEQKEQYLTKLVSGEWSGTMCLTEPQCGTDLGQVKTKAEPS 206
ACAD_FadE2 cd01155
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ...
211-333 1.14e-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: 45.46  E-value: 1.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 211 ELLQHYGTEEQKDHYLPRLARGQEIPCFALTSPE-AGSDAgaipdTGVVCMGEWQGQQVLgmrLTWNKRYITLA-----P 284
Cdd:cd01155  102 EVLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDA-----TNIECSIERDGDDYV---INGRKWWSSGAgdprcK 173
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 493863265 285 IATVLGlafkLSDPEKLLGGEEELGItcaLIPTSTPGVEIGRrhfPLNV 333
Cdd:cd01155  174 IAIVMG----RTDPDGAPRHRQQSMI---LVPMDTPGVTIIR---PLSV 212
AidB cd01154
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ...
188-502 9.02e-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: 39.28  E-value: 9.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 188 QKLAGVSGILAITVG-VPnslgpgeLLQHYGTEEQKDHYLPRLARGQEIPCFA---LTSPEAGSDAGAIPDTGVVCMGE- 262
Cdd:cd01154  104 DAAAGLLCPLTMTDAaVY-------ALRKYGPEELKQYLPGLLSDRYKTGLLGgtwMTEKQGGSDLGANETTAERSGGGv 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 263 WqgqqvlgmRLTWNKrYITLAPIATVlglAFKLSDPEKLLGGEEelGITCALIPTSTP-----GVEI-------GRRHFP 330
Cdd:cd01154  177 Y--------RLNGHK-WFASAPLADA---ALVLARPEGAPAGAR--GLSLFLVPRLLEdgtrnGYRIrrlkdklGTRSVA 242
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 331 L-NVPFQNGptrgqdifvpIDYIIGGPkmaGQGWRMLVECLSVGRgitlPSNSTGglksvAMGI--------GAYAHIRR 401
Cdd:cd01154  243 TgEVEFDDA----------EAYLIGDE---GKGIYYILEMLNISR----LDNAVA-----ALGImrralseaYHYARHRR 300
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 402 QFKISIgkmegIEEPLAR--IAGNAYVMDAAASLITYGIMLGEKPA-----------VLSAIVKYHCTHRAQQSIIDAMD 468
Cdd:cd01154  301 AFGKPL-----IDHPLMRrdLAEMEVDVEAATALTFRAARAFDRAAadkpveahmarLATPVAKLIACKRAAPVTSEAME 375
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 493863265 469 IAGGKGIMlgEGNFLARGYQGAPIAITVEG-ANIL 502
Cdd:cd01154  376 VFGGNGYL--EEWPVARLHREAQVTPIWEGtGNIQ 408
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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