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Conserved domains on  [gi|578826892|ref|XP_006720558|]
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isovaleryl-CoA dehydrogenase, mitochondrial isoform X11 [Homo sapiens]

Protein Classification

acyl-CoA dehydrogenase family protein( domain architecture ID 550)

acyl-CoA dehydrogenase (ACAD) family protein similar to acyl-CoA dehydrogenase that catalyzes the alpha,beta dehydrogenation of an acyl-CoA to form 2,3-dehydroacyl-CoA; requires an acceptor such as FAD, which becomes reduced

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ACAD super family cl09933
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
 44-323 0e+00

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)


The actual alignment was detected with superfamily member cd01156:

Pssm-ID: 447864 [Multi-domain]  Cd Length: 376  Bit Score: 557.41  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892  44 GLSEEQRQLRQTMAKFLQEHLAPKAQEIDRSNEFknLREFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASG 123
Cdd:cd01156    1 GLDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEF--PRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 124 AVGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGP 203
Cdd:cd01156   79 SVALSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGP 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 204 DADVLIVYAKTDLAavPASRGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGL 283
Cdd:cd01156  159 DADTLVVYAKTDPS--AGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGL 236

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 578826892 284 DLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQ 323
Cdd:cd01156  237 DYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQ 276
 
Name Accession Description Interval E-value
IVD cd01156
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ...
 44-323 0e+00

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: 557.41  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892  44 GLSEEQRQLRQTMAKFLQEHLAPKAQEIDRSNEFknLREFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASG 123
Cdd:cd01156    1 GLDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEF--PRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 124 AVGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGP 203
Cdd:cd01156   79 SVALSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGP 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 204 DADVLIVYAKTDLAavPASRGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGL 283
Cdd:cd01156  159 DADTLVVYAKTDPS--AGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGL 236

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 578826892 284 DLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQ 323
Cdd:cd01156  237 DYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQ 276
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 10-323 1.17e-162

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 460.50  E-value: 1.17e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892  10 LLGWRVAswRLRPPLAGFVSQRAHSLLpvddaingLSEEQRQLRQTMAKFLQEHLAPKAQEIDRSNEFKNLREFWKQLGN 89
Cdd:PLN02519   1 MLLSAAK--ARRRGLARRFSSSSSSLL--------FDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPKDVNLWKLMGD 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892  90 LGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSE 169
Cdd:PLN02519  71 FNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGSVGLSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 170 PNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGPDADVLIVYAKTDLAAvpASRGITAFIVEKGMPGFSTSKKLDKLGMR 249
Cdd:PLN02519 151 PNSGSDVVSMKCKAERVDGGYVLNGNKMWCTNGPVAQTLVVYAKTDVAA--GSKGITAFIIEKGMPGFSTAQKLDKLGMR 228

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578826892 250 GSNTCELIFEDCKIPAANILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQ 323
Cdd:PLN02519 229 GSDTCELVFENCFVPEENVLGQEGKGVYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQ 302
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 45-324 7.95e-124

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: 360.69  E-value: 7.95e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892  45 LSEEQRQLRQTMAKFLQEHLAPKAQEIDRSNEFKnlREFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGA 124
Cdd:COG1960    5 LTEEQRALRDEVREFAEEEIAPEAREWDREGEFP--RELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADAS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 125 VGLSYGAHsNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGPD 204
Cdd:COG1960   83 LALPVGVH-NGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 205 ADVLIVYAKTDLAavPASRGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGLD 284
Cdd:COG1960  162 ADVILVLARTDPA--AGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLN 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 578826892 285 LERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQG 324
Cdd:COG1960  240 AGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQA 279
Acyl-CoA_dh_N pfam02771
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ...
 46-160 6.43e-51

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: 164.94  E-value: 6.43e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892   46 SEEQRQLRQTMAKFLQEHLAPKAQEIDRSNEFKnlREFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAV 125
Cdd:pfam02771   1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFP--RELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASV 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 578826892  126 GLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGE 160
Cdd:pfam02771  79 ALALSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
 
Name Accession Description Interval E-value
IVD cd01156
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ...
 44-323 0e+00

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: 557.41  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892  44 GLSEEQRQLRQTMAKFLQEHLAPKAQEIDRSNEFknLREFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASG 123
Cdd:cd01156    1 GLDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEF--PRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 124 AVGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGP 203
Cdd:cd01156   79 SVALSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGP 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 204 DADVLIVYAKTDLAavPASRGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGL 283
Cdd:cd01156  159 DADTLVVYAKTDPS--AGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGL 236

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 578826892 284 DLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQ 323
Cdd:cd01156  237 DYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQ 276
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 10-323 1.17e-162

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 460.50  E-value: 1.17e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892  10 LLGWRVAswRLRPPLAGFVSQRAHSLLpvddaingLSEEQRQLRQTMAKFLQEHLAPKAQEIDRSNEFKNLREFWKQLGN 89
Cdd:PLN02519   1 MLLSAAK--ARRRGLARRFSSSSSSLL--------FDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPKDVNLWKLMGD 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892  90 LGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSE 169
Cdd:PLN02519  71 FNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGSVGLSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 170 PNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGPDADVLIVYAKTDLAAvpASRGITAFIVEKGMPGFSTSKKLDKLGMR 249
Cdd:PLN02519 151 PNSGSDVVSMKCKAERVDGGYVLNGNKMWCTNGPVAQTLVVYAKTDVAA--GSKGITAFIIEKGMPGFSTAQKLDKLGMR 228

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578826892 250 GSNTCELIFEDCKIPAANILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQ 323
Cdd:PLN02519 229 GSDTCELVFENCFVPEENVLGQEGKGVYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQ 302
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 45-324 7.95e-124

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: 360.69  E-value: 7.95e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892  45 LSEEQRQLRQTMAKFLQEHLAPKAQEIDRSNEFKnlREFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGA 124
Cdd:COG1960    5 LTEEQRALRDEVREFAEEEIAPEAREWDREGEFP--RELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADAS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 125 VGLSYGAHsNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGPD 204
Cdd:COG1960   83 LALPVGVH-NGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 205 ADVLIVYAKTDLAavPASRGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGLD 284
Cdd:COG1960  162 ADVILVLARTDPA--AGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLN 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 578826892 285 LERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQG 324
Cdd:COG1960  240 AGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQA 279
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
 47-324 1.47e-114

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: 336.93  E-value: 1.47e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892  47 EEQRQLRQTMAKFLQEHLAPKAQEIDRSNEFKnlREFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAVG 126
Cdd:cd01158    1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFP--REVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 127 LSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGPDAD 206
Cdd:cd01158   79 VIVSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEAD 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 207 VLIVYAKTDLAAvpASRGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGLDLE 286
Cdd:cd01158  159 FYIVFAVTDPSK--GYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGG 236

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 578826892 287 RLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQG 324
Cdd:cd01158  237 RIGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQG 274
ACAD cd00567
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
 47-324 1.90e-89

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: 271.46  E-value: 1.90e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892  47 EEQRQLRQTMAKFLQEHLAPKAQEIDRSNEFknLREFWKQLGNLGVlgitapvqyggsglgylehvlvmeeisrasgavg 126
Cdd:cd00567    1 EEQRELRDSAREFAAEELEPYARERRETPEE--PWELLAELGLLLG---------------------------------- 44

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 127 lsygahsnlcINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGPDAD 206
Cdd:cd00567   45 ----------AALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDAD 114

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 207 VLIVYAKTDLAAvPASRGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGLDLE 286
Cdd:cd00567  115 LFIVLARTDEEG-PGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVG 193

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 578826892 287 RLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQG 324
Cdd:cd00567  194 RLLLAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQA 231
LCAD cd01160
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ...
 47-323 1.05e-87

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: 268.60  E-value: 1.05e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892  47 EEQRQLRQTMAKFLQEHLAPKAQEIDRSNEFKnlREFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRAsGAVG 126
Cdd:cd01160    1 EEHDAFRDVVRRFFAKEVAPFHHEWEKAGEVP--REVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARA-GGSG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 127 LSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGPDAD 206
Cdd:cd01160   78 PGLSLHTDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLAD 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 207 VLIVYAKTDLAAVPASrGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGLDLE 286
Cdd:cd01160  158 VVIVVARTGGEARGAG-GISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQE 236

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 578826892 287 RLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQ 323
Cdd:cd01160  237 RLLIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQ 273
PTZ00461 PTZ00461
isovaleryl-CoA dehydrogenase; Provisional
 9-322 8.29e-83

isovaleryl-CoA dehydrogenase; Provisional


Pssm-ID: 185640 [Multi-domain]  Cd Length: 410  Bit Score: 257.17  E-value: 8.29e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892   9 RLLGWRVASWRLRPPLAGFVSQRAHSLL--PvddainglSEEQRQLRQTMAKFLQEHLAPKAQEIDRSNEFKnlREFWKQ 86
Cdd:PTZ00461   7 SSLGRRSATCGWTAAATMTSASRAFMDLynP--------TPEHAALRETVAKFSREVVDKHAREDDINMHFN--RDLFKQ 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892  87 LGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALA 166
Cdd:PTZ00461  77 LGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDPGFCLAYLAHSMLFVNNFYYSASPAQRARWLPKVLTGEHVGAMG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 167 MSEPNAGSDVVSMKLKAEKKGN-HYILNGNKFWITNGPDADVLIVYAKTDlaavpasRGITAFIVEKGMPGFSTSKKLDK 245
Cdd:PTZ00461 157 MSEPGAGTDVLGMRTTAKKDSNgNYVLNGSKIWITNGTVADVFLIYAKVD-------GKITAFVVERGTKGFTQGPKIDK 229

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578826892 246 LGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHF 322
Cdd:PTZ00461 230 CGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELERVTLAAMAVGIAERSVELMTSYASERKAFGKPISNF 306
VLCAD cd01161
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ...
 34-322 2.42e-78

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: 245.46  E-value: 2.42e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892  34 SLLPVDDAIN-GLSEEQRQLRQTMAKFLQEHLAP-KAQEIDrsnefKNLREFWKQLGNLGVLGITAPVQYGGSGLGYLEH 111
Cdd:cd01161   15 QVFPYPSVLTeEQTEELNMLVGPVEKFFEEVNDPaKNDQLE-----KIPRKTLTQLKELGLFGLQVPEEYGGLGLNNTQY 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 112 VLVMEEISRASGaVGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKK--GNH 189
Cdd:cd01161   90 ARLAEIVGMDLG-FSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLSedGKH 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 190 YILNGNKFWITNGPDADVLIVYAKTDLAAVPASR--GITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELIFEDCKIPAAN 267
Cdd:cd01161  169 YVLNGSKIWITNGGIADIFTVFAKTEVKDATGSVkdKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVEN 248

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 578826892 268 ILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHF 322
Cdd:cd01161  249 VLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEF 303
IBD cd01162
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ...
 45-327 4.02e-71

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: 225.79  E-value: 4.02e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892  45 LSEEQRQLRQTMAKFLQEHLAPKAQEIDRSNEFKnlREFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGA 124
Cdd:cd01162    1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFP--VDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 125 VGlSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGPD 204
Cdd:cd01162   79 TA-AYISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGD 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 205 ADVLIVYAKTDlaaVPASRGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGLD 284
Cdd:cd01162  158 SDVYVVMARTG---GEGPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLN 234

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 578826892 285 LERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQGRPF 327
Cdd:cd01162  235 GGRLNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQF 277
GCD cd01151
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ...
 45-323 2.46e-69

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: 221.85  E-value: 2.46e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892  45 LSEEQRQLRQTMAKFLQEHLAPKAQEIDRSNEFKnlREFWKQLGNLGVLGITaPVQYGGSGLGYLEHVLVMEEISRASGA 124
Cdd:cd01151   13 LTEEERAIRDTAREFCQEELAPRVLEAYREEKFD--RKIIEEMGELGLLGAT-IKGYGCAGLSSVAYGLIAREVERVDSG 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 125 VGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGPD 204
Cdd:cd01151   90 YRSFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSPI 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 205 ADVLIVYAKTDLAAvpasrGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELIFEDCKIPAANILGHENkGVYVLMSGLD 284
Cdd:cd01151  170 ADVFVVWARNDETG-----KIRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPGAE-GLRGPFKCLN 243

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 578826892 285 LERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQ 323
Cdd:cd01151  244 NARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQ 282
MCAD cd01157
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ...
 45-327 9.21e-63

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: 204.36  E-value: 9.21e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892  45 LSEEQRQLRQTMAKFLQEHLAPKAQEIDRSNEFKnlREFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEIsrASGA 124
Cdd:cd01157    1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYP--WPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEEL--AYGC 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 125 VGLSYGAHSN-LCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGP 203
Cdd:cd01157   77 TGVQTAIEANsLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 204 DADVLIVYAKTDL-AAVPASRGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSG 282
Cdd:cd01157  157 KANWYFLLARSDPdPKCPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGA 236

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 578826892 283 LDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQGRPF 327
Cdd:cd01157  237 FDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSF 281
Acyl-CoA_dh_N pfam02771
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ...
 46-160 6.43e-51

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: 164.94  E-value: 6.43e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892   46 SEEQRQLRQTMAKFLQEHLAPKAQEIDRSNEFKnlREFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAV 125
Cdd:pfam02771   1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFP--RELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASV 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 578826892  126 GLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGE 160
Cdd:pfam02771  79 ALALSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
ACAD_fadE6_17_26 cd01152
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ...
 47-294 4.92e-41

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: 147.49  E-value: 4.92e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892  47 EEQRQLRQTMAKFLQEHLAP---KAQEIDRSNEFKNLREFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRAsG 123
Cdd:cd01152    1 PSEEAFRAEVRAWLAAHLPPelrEESALGYREGREDRRRWQRALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAA-G 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 124 AVGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGP 203
Cdd:cd01152   80 APVPFNQIGIDLAGPTILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAH 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 204 DADVLIVYAKTDLaAVPASRGITAFIVEKGMPGFsTSKKLDKLgMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGL 283
Cdd:cd01152  160 YADWAWLLVRTDP-EAPKHRGISILLVDMDSPGV-TVRPIRSI-NGGEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTL 236

                        250
                 ....*....|.
gi 578826892 284 DLERLVLAGGP 294
Cdd:cd01152  237 NFERVSIGGSA 247
PRK12341 PRK12341
acyl-CoA dehydrogenase;
45-323 6.58e-40

acyl-CoA dehydrogenase;


Pssm-ID: 183454 [Multi-domain]  Cd Length: 381  Bit Score: 144.49  E-value: 6.58e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892  45 LSEEQR----QLRQTMAK-FLQEHLApkaqEIDRSNEFKnlREFWKQLGN--LGVLGItaPVQYGGSGLGYLEHVLVMEE 117
Cdd:PRK12341   5 LTEEQElllaSIRELITRnFPEEYFR----TCDENGTYP--REFMRALADngISMLGV--PEEFGGTPADYVTQMLVLEE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 118 ISRASGAVglsYGAHSNLCINQLVRNGNEAQKEK-YLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNK 196
Cdd:PRK12341  77 VSKCGAPA---FLITNGQCIHSMRRFGSAEQLRKtAESTLETGDPAYALALTEPGAGSDNNSATTTYTRKNGKVYLNGQK 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 197 FWITNGPDADVLIVYAKTDLAAVPASRgITAFIVEKGMPGFSTsKKLDKLGMRGSNTCELIFEDCKIPAANILGHENKGV 276
Cdd:PRK12341 154 TFITGAKEYPYMLVLARDPQPKDPKKA-FTLWWVDSSKPGIKI-NPLHKIGWHMLSTCEVYLDNVEVEESDLVGEEGMGF 231

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 578826892 277 YVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQ 323
Cdd:PRK12341 232 LNVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQ 278
PLN02526 PLN02526
acyl-coenzyme A oxidase
 45-323 3.43e-39

acyl-coenzyme A oxidase


Pssm-ID: 178141 [Multi-domain]  Cd Length: 412  Bit Score: 143.45  E-value: 3.43e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892  45 LSEEQRQLRQTMAKFLQEHLAPKAQEIDRSNEFKnlREFWKQLGNLGVLGITAPvQYGGSGLGYLEHVLVMEEISRASGA 124
Cdd:PLN02526  29 LTPEEQALRKRVRECMEKEVAPIMTEYWEKAEFP--FHIIPKLGSLGIAGGTIK-GYGCPGLSITASAIATAEVARVDAS 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 125 VGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGPD 204
Cdd:PLN02526 106 CSTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIGNSTF 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 205 ADVLIVYAKTdlaavPASRGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELIFEDC------KIPAANILGHENKgvyv 278
Cdd:PLN02526 186 ADVLVIFARN-----TTTNQINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVfvpdedRLPGVNSFQDTNK---- 256

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 578826892 279 lmsGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQ 323
Cdd:PLN02526 257 ---VLAVSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQ 298
ACAD_fadE5 cd01153
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ...
 55-316 2.97e-35

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: 132.51  E-value: 2.97e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892  55 TMAKFLQEHLAPKAQEIDRSN-EFKNLR--------EFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAV 125
Cdd:cd01153    4 EVARLAENVLAPLNADGDREGpVFDDGRvvvpppfkEALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDAPL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 126 GLSYGAHSnlCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGN-HYILNGNKFWITNG-- 202
Cdd:cd01153   84 MYASGTQG--AAATLLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRFISAGeh 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 203 --PDADVLIVYAKTDlAAVPASRGITAFIVEK----GMPGFSTSKKLD-KLGMRGSNTCELIFEDCKipaANILGHENKG 275
Cdd:cd01153  162 dmSENIVHLVLARSE-GAPPGVKGLSLFLVPKflddGERNGVTVARIEeKMGLHGSPTCELVFDNAK---GELIGEEGMG 237

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 578826892 276 VYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFG 316
Cdd:cd01153  238 LAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGG 278
Acyl-CoA_dh_M pfam02770
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ...
 164-259 3.26e-33

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: 118.54  E-value: 3.26e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892  164 ALAMSEPNAGSDVVSMKLKA-EKKGNHYILNGNKFWITNGPDADVLIVYAKTDLAAvpASRGITAFIVEKGMPGFSTSKK 242
Cdd:pfam02770   1 AFALTEPGAGSDVASLKTTAaDGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDD--RHGGISLFLVPKDAPGVSVRRI 78

                          90
                  ....*....|....*..
gi 578826892  243 LDKLGMRGSNTCELIFE 259
Cdd:pfam02770  79 ETKLGVRGLPTGELVFD 95
PRK03354 PRK03354
crotonobetainyl-CoA dehydrogenase; Validated
 45-323 1.18e-31

crotonobetainyl-CoA dehydrogenase; Validated


Pssm-ID: 179566 [Multi-domain]  Cd Length: 380  Bit Score: 122.25  E-value: 1.18e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892  45 LSEEQR----QLRQTMAKflqEHLAPKAQEIDRSNEFKnlREFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISR 120
Cdd:PRK03354   5 LNDEQElfvaGIRELMAS---ENWEAYFAECDRDSVYP--ERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 121 ASGAVGLSYGAHSNlcINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWIT 200
Cdd:PRK03354  80 LGAPTYVLYQLPGG--FNTFLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFIT 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 201 NGPDADVLIVYAKTdlAAVPASRGITAFIVEKGMPGFSTSkKLDKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLM 280
Cdd:PRK03354 158 SSAYTPYIVVMARD--GASPDKPVYTEWFVDMSKPGIKVT-KLEKLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVK 234

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 578826892 281 SGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQ 323
Cdd:PRK03354 235 EEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQ 277
PTZ00456 PTZ00456
acyl-CoA dehydrogenase; Provisional
 78-276 2.30e-27

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185635 [Multi-domain]  Cd Length: 622  Bit Score: 112.65  E-value: 2.30e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892  78 KNLREFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAV----GLSYGAhsnlcINQLVRNGNEAQKEKYL 153
Cdd:PTZ00456  99 KGFKEAYQALKAGGWTGISEPEEYGGQALPLSVGFITRELMATANWGFsmypGLSIGA-----ANTLMAWGSEEQKEQYL 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 154 PKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGN-HYILNGNKFWITNGpDAD-----VLIVYAKTDlAAVPASRGITA 227
Cdd:PTZ00456 174 TKLVSGEWSGTMCLTEPQCGTDLGQVKTKAEPSADgSYKITGTKIFISAG-DHDlteniVHIVLARLP-NSLPTTKGLSL 251

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 578826892 228 FIVEKGMP----GFSTSKKLD------KLGMRGSNTCELIFEDCKipaANILGHENKGV 276
Cdd:PTZ00456 252 FLVPRHVVkpdgSLETAKNVKciglekKMGIKGSSTCQLSFENSV---GYLIGEPNAGM 307
ACAD_FadE2 cd01155
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ...
 51-319 9.13e-25

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: 103.62  E-value: 9.13e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892  51 QLRQTMAKFLQEHLAPKAQEIDRSNE------------FKNLREFWKQLG--NLGVlgitaPVQYGGSGLGYLEHVLVME 116
Cdd:cd01155    5 ELRARVKAFMEEHVYPAEQEFLEYYAeggdrwwtpppiIEKLKAKAKAEGlwNLFL-----PEVSGLSGLTNLEYAYLAE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 117 EISR---ASGAVGLSYGAHSNLCInqLVRNGNEAQKEKYLPKLISGEYIGALAMSEPN-AGSDVVSMKLKAEKKGNHYIL 192
Cdd:cd01155   80 ETGRsffAPEVFNCQAPDTGNMEV--LHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERDGDDYVI 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 193 NGNKFWITNG--PDADVLIVYAKTDLAAVPASRGITAFIVEKGMPGFSTSKKLDKLG---MRGSNtCELIFEDCKIPAAN 267
Cdd:cd01155  158 NGRKWWSSGAgdPRCKIAIVMGRTDPDGAPRHRQQSMILVPMDTPGVTIIRPLSVFGyddAPHGH-AEITFDNVRVPASN 236

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 578826892 268 ILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKI 319
Cdd:cd01155  237 LILGEGRGFEIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKL 288
AidB cd01154
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ...
 140-319 2.70e-20

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: 90.89  E-value: 2.70e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 140 LVRNGNEAQKEkYLPKLISGEY----IGALAMSEPNAGSDVVSMKLKAEK-KGNHYILNGNKfWITNGPDADVLIVYAKT 214
Cdd:cd01154  123 LRKYGPEELKQ-YLPGLLSDRYktglLGGTWMTEKQGGSDLGANETTAERsGGGVYRLNGHK-WFASAPLADAALVLARP 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 215 DlAAVPASRGITAFIVEKGMP-----GFSTSKKLDKLGMRGSNTCELIFEDCKipaANILGHENKGVYVLMSGLDLERLV 289
Cdd:cd01154  201 E-GAPAGARGLSLFLVPRLLEdgtrnGYRIRRLKDKLGTRSVATGEVEFDDAE---AYLIGDEGKGIYYILEMLNISRLD 276

                        170       180       190
                 ....*....|....*....|....*....|
gi 578826892 290 LAGGPLGLMQAVLDHTIPYLHVREAFGQKI 319
Cdd:cd01154  277 NAVAALGIMRRALSEAYHYARHRRAFGKPL 306
PLN02876 PLN02876
acyl-CoA dehydrogenase
 46-319 9.00e-16

acyl-CoA dehydrogenase


Pssm-ID: 215473 [Multi-domain]  Cd Length: 822  Bit Score: 78.30  E-value: 9.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892  46 SEEQRQLRQTMAKFLQEHLAPKAQEIDR---SN-------EFKNLREFWKQLG--NL--------------------GVL 93
Cdd:PLN02876 403 SEKVLELRKKLIKFMEDHIYPMENEFYKlaqSSsrwtvhpEEERLKELAKKEGlwNLwipldsaararkllfednkhMVS 482

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892  94 GITAPvQYGGSGLGYLEHVLVMEEISRASGAVG-LSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPN- 171
Cdd:PLN02876 483 GDSAD-QLLGAGLSNLEYGYLCEIMGRSVWAPQvFNCGAPDTGNMEVLLRYGNKEQQLEWLIPLLEGKIRSGFAMTEPQv 561

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 172 AGSDVVSMKLKAEKKGNHYILNGNKFWiTNG---PDADVLIVYAKTDLAAvPASRGITAFIVEKGMPGFSTSKKLDKLGM 248
Cdd:PLN02876 562 ASSDATNIECSIRRQGDSYVINGTKWW-TSGamdPRCRVLIVMGKTDFNA-PKHKQQSMILVDIQTPGVQIKRPLLVFGF 639

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578826892 249 RGS--NTCELIFEDCKIPAANILGHENKGVYVLMSGLDLERL----VLAGGPLGLMQAVLDHTIPylhvREAFGQKI 319
Cdd:PLN02876 640 DDAphGHAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLhhcmRLIGAAERGMQLMVQRALS----RKAFGKLI 712
DszC cd01163
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ...
 64-329 6.95e-15

Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, which catalyzes the first two steps of DBT desulfurization in mesophilic bacteria. DszC converts DBT to DBT-sulfoxide, which is then converted to DBT-sulfone. Bacteria with this enzyme are candidates for the removal of organic sulfur compounds from fossil fuels, which pollute the environment. An equivalent enzyme tdsC, is found in thermophilic bacteria. This alignment also contains a closely related uncharacterized subgroup.


Pssm-ID: 173852 [Multi-domain]  Cd Length: 377  Bit Score: 74.67  E-value: 6.95e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892  64 LAPKAQEIDRSNEFKnlREFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAHSNLcINQLVRN 143
Cdd:cd01163   10 IAEGAAERDRQRGLP--YEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALRAHFGF-VEALLLA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 144 GNEAQKEKYLPKLISGEYIGAlAMSE---PNAGSDVVSMklkaEKKGNHYILNGNKFWITNGPDADVLIVYAKTDLAAvp 220
Cdd:cd01163   87 GPEQFRKRWFGRVLNGWIFGN-AVSErgsVRPGTFLTAT----VRDGGGYVLNGKKFYSTGALFSDWVTVSALDEEGK-- 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 221 asrgITAFIVEKGMPGFSTSKKLDKLGMR--GSNTceLIFEDCKIPAANILGHENKGVYVLMSGLdLERLVLAGGPLGLM 298
Cdd:cd01163  160 ----LVFAAVPTDRPGITVVDDWDGFGQRltASGT--VTFDNVRVEPDEVLPRPNAPDRGTLLTA-IYQLVLAAVLAGIA 232

                        250       260       270
                 ....*....|....*....|....*....|.
gi 578826892 299 QAVLDHTIPYlhVREafgqkighfQGRPFPP 329
Cdd:cd01163  233 RAALDDAVAY--VRS---------RTRPWIH 252
PRK13026 PRK13026
acyl-CoA dehydrogenase; Reviewed
 70-324 2.37e-13

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 237277 [Multi-domain]  Cd Length: 774  Bit Score: 71.14  E-value: 2.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892  70 EIDRSNEFKNL-REFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAHSNLCINQLVRN-GNEA 147
Cdd:PRK13026  99 DWDIVQNRKDLpPEVWDYLKKEGFFALIIPKEYGGKGFSAYANSTIVSKIATRSVSAAVTVMVPNSLGPGELLTHyGTQE 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 148 QKEKYLPKLISGEYIGALAMSEPNAGSDVVSMK-----LKAEKKGNHYI---LNGNKFWITNGPDADVL----IVYAKTD 215
Cdd:PRK13026 179 QKDYWLPRLADGTEIPCFALTGPEAGSDAGAIPdtgivCRGEFEGEEVLglrLTWDKRYITLAPVATVLglafKLRDPDG 258

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 216 LAAVPASRGITAFIVEKGMPGFSTSKKLDKLGMR---GSNTCELIFedckIPAANILG---HENKGVYVLMSGLDLERlv 289
Cdd:PRK13026 259 LLGDKKELGITCALIPTDHPGVEIGRRHNPLGMAfmnGTTRGKDVF----IPLDWIIGgpdYAGRGWRMLVECLSAGR-- 332

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 578826892 290 laGGPLGLMQAVLDH-----TIPYLHVREAFGQKIGHFQG 324
Cdd:PRK13026 333 --GISLPALGTASGHmatrtTGAYAYVRRQFGMPIGQFEG 370
fadE PRK09463
acyl-CoA dehydrogenase; Reviewed
 82-324 7.81e-12

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 236528 [Multi-domain]  Cd Length: 777  Bit Score: 66.38  E-value: 7.81e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892  82 EFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAHSNLCINQ-LVRNGNEAQKEKYLPKLISGE 160
Cdd:PRK09463 113 EVWQFIKEHGFFGMIIPKEYGGLEFSAYAHSRVLQKLASRSGTLAVTVMVPNSLGPGElLLHYGTDEQKDHYLPRLARGE 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 161 YIGALAMSEPNAGSDVVSMK-----LKAEKKGNHYI---LNGNKFWITNGPDADVL-----------IVYAKTDLaavpa 221
Cdd:PRK09463 193 EIPCFALTSPEAGSDAGSIPdtgvvCKGEWQGEEVLgmrLTWNKRYITLAPIATVLglafklydpdgLLGDKEDL----- 267

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 222 srGITAFIVEKGMPGFSTSKKLDKLG---MRGSNTCELIFedckIPAANILG---HENKGVYVLMSGLDLERLV-LAGGP 294
Cdd:PRK09463 268 --GITCALIPTDTPGVEIGRRHFPLNvpfQNGPTRGKDVF----IPLDYIIGgpkMAGQGWRMLMECLSVGRGIsLPSNS 341

                        250       260       270
                 ....*....|....*....|....*....|
gi 578826892 295 LGLMQAVLDHTIPYLHVREAFGQKIGHFQG 324
Cdd:PRK09463 342 TGGAKLAALATGAYARIRRQFKLPIGKFEG 371
PTZ00457 PTZ00457
acyl-CoA dehydrogenase; Provisional
 78-302 9.12e-12

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185636 [Multi-domain]  Cd Length: 520  Bit Score: 66.06  E-value: 9.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892  78 KNLREFWKQLGNLGvlGITAPVQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLI 157
Cdd:PTZ00457  53 EQIRSNDKILGNLY--GARIATEYGGLGLGHTAHALIYEEVGTNCDSKLLSTIQHSGFCTYLLSTVGSKELKGKYLTAMS 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 158 SGEYIGALAMSEPNaGSDVVSMKLKAEKKGN-HYILNGNKFWItNGPDADVLIVYAKT------DLAAVPASRgITAFIV 230
Cdd:PTZ00457 131 DGTIMMGWATEEGC-GSDISMNTTKASLTDDgSYVLTGQKRCE-FAASATHFLVLAKTltqtaaEEGATEVSR-NSFFIC 207

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578826892 231 EKGMPGFSTskkldklgmrgsNTCELIFEDckIPAANILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVL 302
Cdd:PTZ00457 208 AKDAKGVSV------------NGDSVVFEN--TPAADVVGVVGEGFKDAMITLFTEQYLYAASLLGIMKRVV 265
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 273-324 5.17e-11

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: 59.96  E-value: 5.17e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578826892  273 NKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQG 324
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQL 52
PRK11561 PRK11561
isovaleryl CoA dehydrogenase; Provisional
 159-317 5.18e-09

isovaleryl CoA dehydrogenase; Provisional


Pssm-ID: 183199 [Multi-domain]  Cd Length: 538  Bit Score: 57.45  E-value: 5.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 159 GEYIGaLAMSEPNAGSDVVSMKLKAEK-KGNHYILNGNKfWITNGPDADVLIVYAKTDlaavpasRGITAFIVEKGMP-G 236
Cdd:PRK11561 177 GLLIG-MGMTEKQGGSDVLSNTTRAERlADGSYRLVGHK-WFFSVPQSDAHLVLAQAK-------GGLSCFFVPRFLPdG 247

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 237 FSTSKKL----DKLGMRGSNTCELIFEDCkipAANILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVR 312
Cdd:PRK11561 248 QRNAIRLerlkDKLGNRSNASSEVEFQDA---IGWLLGEEGEGIRLILKMGGMTRFDCALGSHGLMRRAFSVAIYHAHQR 324


                 ....*
gi 578826892 313 EAFGQ 317
Cdd:PRK11561 325 QVFGK 329
AXO cd01150
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ...
 115-282 5.29e-08

Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in the peroxisomal fatty acid beta-oxidation, the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. In a second oxidative half-reaction, the reduced FAD is reoxidized by molecular oxygen. AXO is generally a homodimer, but it has been reported to form a different type of oligomer in yeast. There are several subtypes of AXO's, based on substrate specificity. Palmitoyl-CoA oxidase acts on straight-chain fatty acids and prostanoids; whereas, the closely related Trihydroxycoprostanoly-CoA oxidase has the greatest activity for 2-methyl branched side chains of bile precursors. Pristanoyl-CoA oxidase, acts on 2-methyl branched fatty acids. AXO has an additional domain, C-terminal to the region with similarity to acyl-CoA dehydrogenases, which is included in this alignment.


Pssm-ID: 173839 [Multi-domain]  Cd Length: 610  Bit Score: 54.26  E-value: 5.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 115 MEEISRASGAVGLSYGA----HSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKA--EKKGN 188
Cdd:cd01150   84 MLALTNSLGGYDLSLGAklglHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTAtyDPLTQ 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 189 HYILN-----GNKFWITN-GPDADVLIVYAKTdlaAVPASR-GITAFIVE-------KGMPGFSTSKKLDKLGMRGSNTC 254
Cdd:cd01150  164 EFVINtpdftATKWWPGNlGKTATHAVVFAQL---ITPGKNhGLHAFIVPirdpkthQPLPGVTVGDIGPKMGLNGVDNG 240

                        170       180
                 ....*....|....*....|....*...
gi 578826892 255 ELIFEDCKIPAANILgheNKGVYVLMSG 282
Cdd:cd01150  241 FLQFRNVRIPRENLL---NRFGDVSPDG 265
PLN02636 PLN02636
acyl-coenzyme A oxidase
 114-316 6.88e-07

acyl-coenzyme A oxidase


Pssm-ID: 215342 [Multi-domain]  Cd Length: 686  Bit Score: 51.01  E-value: 6.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 114 VMEEISRASGAVGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKA--EKKGNHYI 191
Cdd:PLN02636 126 ITEAVGSVDMSLGIKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTAtfDPLTDEFV 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 192 LN-----GNKFWITNGP-DADVLIVYAKTDLAAvPASRGIT-----AFIV-------EKGMPGFSTSKKLDKLGMRGSNT 253
Cdd:PLN02636 206 INtpndgAIKWWIGNAAvHGKFATVFARLKLPT-HDSKGVSdmgvhAFIVpirdmktHQVLPGVEIRDCGHKVGLNGVDN 284

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578826892 254 CELIFEDCKIPAANILGH----------------ENKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFG 316
Cdd:PLN02636 285 GALRFRSVRIPRDNLLNRfgdvsrdgkytsslptINKRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQFG 363
PTZ00460 PTZ00460
acyl-CoA dehydrogenase; Provisional
 144-269 1.10e-05

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185639 [Multi-domain]  Cd Length: 646  Bit Score: 47.15  E-value: 1.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 144 GNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKA--EKKGNHYILN-----GNKFWITN-GPDADVLIVYAKtd 215
Cdd:PTZ00460 110 GTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTAtyDKQTNEFVIHtpsveAVKFWPGElGFLCNFALVYAK-- 187

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578826892 216 LAAVPASRGITAFIVE-------KGMPGFSTSKKLDKLGMRGSNTCELIFEDCKIPAANIL 269
Cdd:PTZ00460 188 LIVNGKNKGVHPFMVRirdkethKPLQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLL 248
NcnH cd01159
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ...
 62-269 5.33e-04

Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, which is active against Gram-positive bacteria. Polyketides are secondary metabolites, which have important biological functions such as antitumor, immunosupressive or antibiotic activities. NcnH is a hydroxylase involved in the biosynthesis of naphthocyclinone and possibly other polyketides.


Pssm-ID: 173848 [Multi-domain]  Cd Length: 370  Bit Score: 41.57  E-value: 5.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892  62 EHLAPKAQEidRSNEFKNLREFWKQ----LGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAVG---LSYGAHSn 134
Cdd:cd01159    4 EDLAPLIRE--RAPEAERARRLPDEvvraLREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSAAwvaSIVATHS- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826892 135 lciNQLVRNGNEAQKEKYlpklisGEYIGALAmsepnagSDVVSMKLKAEKKGNHYILNGNKFWITNGPDADVLIVYAK- 213
Cdd:cd01159   81 ---RMLAAFPPEAQEEVW------GDGPDTLL-------AGSYAPGGRAERVDGGYRVSGTWPFASGCDHADWILVGAIv 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 578826892 214 TDLAAVPASRgitAFIVEKGmpGFSTSKKLDKLGMRGSNTCELIFEDCKIPAANIL 269
Cdd:cd01159  145 EDDDGGPLPR---AFVVPRA--EYEIVDTWHVVGLRGTGSNTVVVDDVFVPEHRTL 195
 
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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