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Conserved domains on  [gi|1716756588|gb|TWN77580|]
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putative acyl-CoA dehydrogenase [Bacillus licheniformis]

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 ...
 26-409 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 cd01161:

Pssm-ID: 447864 [Multi-domain]  Cd Length: 409  Bit Score: 515.87  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588  26 EDFTEEDRLISKTTESFVKNEVMPLleSIDQ-QDHEsvKKLFQKAGELGLLSIEVPEDCGGLSLSKKLSGLVAEKMGAGG 104
Cdd:cd01161    25 EEQTEELNMLVGPVEKFFEEVNDPA--KNDQlEKIP--RKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEIVGMDL 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 105 SFSVSFNIHAGVGTLPYIYYGTEEQKQKYLPKLASGEWIGAYALTEPGAGSDALNAKTTAVLNREGTAWILNGEKQWITN 184
Cdd:cd01161   101 GFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLSEDGKHYVLNGSKIWITN 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 185 AQVADVYVVFAKT---------AEGMTAFIVERSFKGVSIGPEEKKMGIKGSSTATLILEEVEVPSDNVLGHIGKGHHVA 255
Cdd:cd01161   181 GGIADIFTVFAKTevkdatgsvKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGDGFKVA 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 256 LNILNMARLKLAFSNIGTAKQALNLAVSYAKQRKQFNKPIIGFSMIQEKIADMAVSIFGAESAAYRTADCLDNvldsalp 335
Cdd:cd01161   261 MNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDR------- 333

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1716756588 336 lddrlRKLTNYASECAINKVYCSEILGRIADEAVQIHGGYGYMQEYEVERLYRDARISRIFEGTNEINRLTIAK 409
Cdd:cd01161   334 -----GLKAEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIAL 402
 
Name Accession Description Interval E-value
VLCAD cd01161
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ...
 26-409 0e+00

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: 515.87  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588  26 EDFTEEDRLISKTTESFVKNEVMPLleSIDQ-QDHEsvKKLFQKAGELGLLSIEVPEDCGGLSLSKKLSGLVAEKMGAGG 104
Cdd:cd01161    25 EEQTEELNMLVGPVEKFFEEVNDPA--KNDQlEKIP--RKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEIVGMDL 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 105 SFSVSFNIHAGVGTLPYIYYGTEEQKQKYLPKLASGEWIGAYALTEPGAGSDALNAKTTAVLNREGTAWILNGEKQWITN 184
Cdd:cd01161   101 GFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLSEDGKHYVLNGSKIWITN 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 185 AQVADVYVVFAKT---------AEGMTAFIVERSFKGVSIGPEEKKMGIKGSSTATLILEEVEVPSDNVLGHIGKGHHVA 255
Cdd:cd01161   181 GGIADIFTVFAKTevkdatgsvKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGDGFKVA 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 256 LNILNMARLKLAFSNIGTAKQALNLAVSYAKQRKQFNKPIIGFSMIQEKIADMAVSIFGAESAAYRTADCLDNvldsalp 335
Cdd:cd01161   261 MNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDR------- 333

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1716756588 336 lddrlRKLTNYASECAINKVYCSEILGRIADEAVQIHGGYGYMQEYEVERLYRDARISRIFEGTNEINRLTIAK 409
Cdd:cd01161   334 -----GLKAEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIAL 402
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 27-414 6.20e-152

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: 441.20  E-value: 6.20e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588  27 DFTEEDRLISKTTESFVKNEVMPLLESIDQqDHESVKKLFQKAGELGLLSIEVPEDCGGLSLSKKLSGLVAEKMG-AGGS 105
Cdd:COG1960     4 ELTEEQRALRDEVREFAEEEIAPEAREWDR-EGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELArADAS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 106 FSVSFNIHAGVGtLPYIYYGTEEQKQKYLPKLASGEWIGAYALTEPGAGSDALNAKTTAVlnREGTAWILNGEKQWITNA 185
Cdd:COG1960    83 LALPVGVHNGAA-EALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAV--RDGDGYVLNGQKTFITNA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 186 QVADVYVVFAKT-----AEGMTAFIVERSFKGVSIGPEEKKMGIKGSSTATLILEEVEVPSDNVLGHIGKGHHVALNILN 260
Cdd:COG1960   160 PVADVILVLARTdpaagHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLN 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 261 MARLKLAFSNIGTAKQALNLAVSYAKQRKQFNKPIIGFSMIQEKIADMAVSIFGAESAAYRTADCLDNVLDSALplddrl 340
Cdd:COG1960   240 AGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAAL------ 313

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1716756588 341 rkltnyasECAINKVYCSEILGRIADEAVQIHGGYGYMQEYEVERLYRDARISRIFEGTNEINRLTIAKLLMKE 414
Cdd:COG1960   314 --------EAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGR 379
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 2-414 7.00e-79

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 254.03  E-value: 7.00e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588   2 GKAKLRWNEPLISQHESAAEGFTPEDFTEEDRlisKTTESFVKNEVMPLLESIDQQDH--ESVKkLFQKAGELGLLSIEV 79
Cdd:PLN02519    3 LSAAKARRRGLARRFSSSSSSLLFDDTQLQFK---ESVQQFAQENIAPHAAAIDATNSfpKDVN-LWKLMGDFNLHGITA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588  80 PEDCGGLSLSKKLSGLVAEKMG-AGGSFSVSFNIHAGVGTLPYIYYGTEEQKQKYLPKLASGEWIGAYALTEPGAGSDAL 158
Cdd:PLN02519   79 PEEYGGLGLGYLYHCIAMEEISrASGSVGLSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 159 NAKTTAvlNREGTAWILNGEKQWITNAQVADVYVVFAKT-----AEGMTAFIVERSFKGVSIGPEEKKMGIKGSSTATLI 233
Cdd:PLN02519  159 SMKCKA--ERVDGGYVLNGNKMWCTNGPVAQTLVVYAKTdvaagSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELV 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 234 LEEVEVPSDNVLGHIGKGHHVALNILNMARLKLAFSNIGTAKQALNLAVSYAKQRKQFNKPIIGFSMIQEKIADMAVSIF 313
Cdd:PLN02519  237 FENCFVPEENVLGQEGKGVYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQ 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 314 GAESAAYRTA-DCLDNVLDsalplddrlRKltnyasECAINKVYCSEILGRIADEAVQIHGGYGYMQEYEVERLYRDARI 392
Cdd:PLN02519  317 SSRSYVYSVArDCDNGKVD---------RK------DCAGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKL 381

                         410       420
                  ....*....|....*....|..
gi 1716756588 393 SRIFEGTNEINRLTIAKLLMKE 414
Cdd:PLN02519  382 YEIGAGTSEIRRMLIGRELFKE 403
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 249-409 7.43e-42

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: 147.40  E-value: 7.43e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 249 GKGHHVALNILNMARLKLAFSNIGTAKQALNLAVSYAKQRKQFNKPIIGFSMIQEKIADMAVSIFGAESAAYRTADCLDN 328
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 329 VLDSALplddrlrkltnyasECAINKVYCSEILGRIADEAVQIHGGYGYMQEYEVERLYRDARISRIFEGTNEINRLTIA 408
Cdd:pfam00441  81 GGPDGA--------------EASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIA 146


                  .
gi 1716756588 409 K 409
Cdd:pfam00441 147 R 147
 
Name Accession Description Interval E-value
VLCAD cd01161
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ...
 26-409 0e+00

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: 515.87  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588  26 EDFTEEDRLISKTTESFVKNEVMPLleSIDQ-QDHEsvKKLFQKAGELGLLSIEVPEDCGGLSLSKKLSGLVAEKMGAGG 104
Cdd:cd01161    25 EEQTEELNMLVGPVEKFFEEVNDPA--KNDQlEKIP--RKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEIVGMDL 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 105 SFSVSFNIHAGVGTLPYIYYGTEEQKQKYLPKLASGEWIGAYALTEPGAGSDALNAKTTAVLNREGTAWILNGEKQWITN 184
Cdd:cd01161   101 GFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLSEDGKHYVLNGSKIWITN 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 185 AQVADVYVVFAKT---------AEGMTAFIVERSFKGVSIGPEEKKMGIKGSSTATLILEEVEVPSDNVLGHIGKGHHVA 255
Cdd:cd01161   181 GGIADIFTVFAKTevkdatgsvKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGDGFKVA 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 256 LNILNMARLKLAFSNIGTAKQALNLAVSYAKQRKQFNKPIIGFSMIQEKIADMAVSIFGAESAAYRTADCLDNvldsalp 335
Cdd:cd01161   261 MNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDR------- 333

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1716756588 336 lddrlRKLTNYASECAINKVYCSEILGRIADEAVQIHGGYGYMQEYEVERLYRDARISRIFEGTNEINRLTIAK 409
Cdd:cd01161   334 -----GLKAEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIAL 402
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 27-414 6.20e-152

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: 441.20  E-value: 6.20e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588  27 DFTEEDRLISKTTESFVKNEVMPLLESIDQqDHESVKKLFQKAGELGLLSIEVPEDCGGLSLSKKLSGLVAEKMG-AGGS 105
Cdd:COG1960     4 ELTEEQRALRDEVREFAEEEIAPEAREWDR-EGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELArADAS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 106 FSVSFNIHAGVGtLPYIYYGTEEQKQKYLPKLASGEWIGAYALTEPGAGSDALNAKTTAVlnREGTAWILNGEKQWITNA 185
Cdd:COG1960    83 LALPVGVHNGAA-EALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAV--RDGDGYVLNGQKTFITNA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 186 QVADVYVVFAKT-----AEGMTAFIVERSFKGVSIGPEEKKMGIKGSSTATLILEEVEVPSDNVLGHIGKGHHVALNILN 260
Cdd:COG1960   160 PVADVILVLARTdpaagHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLN 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 261 MARLKLAFSNIGTAKQALNLAVSYAKQRKQFNKPIIGFSMIQEKIADMAVSIFGAESAAYRTADCLDNVLDSALplddrl 340
Cdd:COG1960   240 AGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAAL------ 313

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1716756588 341 rkltnyasECAINKVYCSEILGRIADEAVQIHGGYGYMQEYEVERLYRDARISRIFEGTNEINRLTIAKLLMKE 414
Cdd:COG1960   314 --------EAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGR 379
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
 30-413 2.36e-130

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: 385.85  E-value: 2.36e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588  30 EEDRLISKTTESFVKNEVMPLLESIDQQdHESVKKLFQKAGELGLLSIEVPEDCGGLSLSKKLSGLVAEKMGAG-GSFSV 108
Cdd:cd01158     1 EEHQMIRKTVRDFAEKEIAPLAAEMDEK-GEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVdASVAV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 109 SFNIHAGVGTLPYIYYGTEEQKQKYLPKLASGEWIGAYALTEPGAGSDALNAKTTAVlnREGTAWILNGEKQWITNAQVA 188
Cdd:cd01158    80 IVSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAK--KDGDDYVLNGSKMWITNGGEA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 189 DVYVVFAKT-----AEGMTAFIVERSFKGVSIGPEEKKMGIKGSSTATLILEEVEVPSDNVLGHIGKGHHVALNILNMAR 263
Cdd:cd01158   158 DFYIVFAVTdpskgYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGR 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 264 LKLAFSNIGTAKQALNLAVSYAKQRKQFNKPIIGFSMIQEKIADMAVSIFGAESAAYRTADCLDNVLdsalplddrlrkl 343
Cdd:cd01158   238 IGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGE------------- 304

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 344 tNYASECAINKVYCSEILGRIADEAVQIHGGYGYMQEYEVERLYRDARISRIFEGTNEINRLTIAKLLMK 413
Cdd:cd01158   305 -PFIKEAAMAKLFASEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLLK 373
IVD cd01156
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ...
 27-413 7.48e-110

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: 333.22  E-value: 7.48e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588  27 DFTEEDRLISKTTESFVKNEVMPLLESIDQQDHESVKkLFQKAGELGLLSIEVPEDCGGLSLSKKLSGLVAEKMG-AGGS 105
Cdd:cd01156     1 GLDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRD-LWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISrASGS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 106 FSVSFNIHAGVgTLPYIY-YGTEEQKQKYLPKLASGEWIGAYALTEPGAGSDALNAKTTAvlNREGTAWILNGEKQWITN 184
Cdd:cd01156    80 VALSYGAHSNL-CINQIYrNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRA--EKKGDRYVLNGSKMWITN 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 185 AQVADVYVVFAKT-----AEGMTAFIVERSFKGVSIGPEEKKMGIKGSSTATLILEEVEVPSDNVLGHIGKGHHVALNIL 259
Cdd:cd01156   157 GPDADTLVVYAKTdpsagAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGL 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 260 NMARLKLAFSNIGTAKQALNLAVSYAKQRKQFNKPIIGFSMIQEKIADMAVSIFGAESAAYRTADCLDNvlDSALPLDdr 339
Cdd:cd01156   237 DYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDR--GNMDPKD-- 312

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1716756588 340 lrkltnyaseCAINKVYCSEILGRIADEAVQIHGGYGYMQEYEVERLYRDARISRIFEGTNEINRLTIAKLLMK 413
Cdd:cd01156   313 ----------AAGVILYAAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGRELFK 376
ACAD cd00567
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
 30-409 4.23e-109

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: 329.63  E-value: 4.23e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588  30 EEDRLISKTTESFVKNEVMPLLESIDQqDHESVKKLFQKAGELGllsievpedcgglslskklsglvaekmgaggsfsvs 109
Cdd:cd00567     1 EEQRELRDSAREFAAEELEPYARERRE-TPEEPWELLAELGLLL------------------------------------ 43

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 110 fnihagvGTLPYIYYGTEEQKQKYLPKLASGEWIGAYALTEPGAGSDALNAKTTAVlnREGTAWILNGEKQWITNAQVAD 189
Cdd:cd00567    44 -------GAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTAR--KDGDGYVLNGRKIFISNGGDAD 114

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 190 VYVVFAKTAE------GMTAFIVERSFKGVSIGPEEKKMGIKGSSTATLILEEVEVPSDNVLGHIGKGHHVALNILNMAR 263
Cdd:cd00567   115 LFIVLARTDEegpghrGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGR 194

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 264 LKLAFSNIGTAKQALNLAVSYAKQRKQFNKPIIGFSMIQEKIADMAVSIFGAESAAYRTADCLDnvldsALPLDDRLrkl 343
Cdd:cd00567   195 LLLAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLD-----QGPDEARL--- 266

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1716756588 344 tnyasECAINKVYCSEILGRIADEAVQIHGGYGYMQEYEVERLYRDARISRIFEGTNEINRLTIAK 409
Cdd:cd00567   267 -----EAAMAKLFATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
IBD cd01162
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ...
 29-414 2.61e-94

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: 293.20  E-value: 2.61e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588  29 TEEDRLISKTTESFVKNEVMPLLESIDQQDHESVKKLfQKAGELGLLSIEVPEDCGGLSLSKKLSGLVAEKMGAGG-SFS 107
Cdd:cd01162     2 NEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVL-RKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCvSTA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 108 VSFNIHAGVGTLpYIYYGTEEQKQKYLPKLASGEWIGAYALTEPGAGSDALNAKTTAVlnREGTAWILNGEKQWITNAQV 187
Cdd:cd01162    81 AYISIHNMCAWM-IDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAV--REGDHYVLNGSKAFISGAGD 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 188 ADVYVVFAKT----AEGMTAFIVERSFKGVSIGPEEKKMGIKGSSTATLILEEVEVPSDNVLGHIGKGHHVALNILNMAR 263
Cdd:cd01162   158 SDVYVVMARTggegPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGR 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 264 LKLAFSNIGTAKQALNLAVSYAKQRKQFNKPIIGFSMIQEKIADMAVSIFGAESAAYRTADCLDNVLDSALPLddrlrkl 343
Cdd:cd01162   238 LNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPDAVKL------- 310

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1716756588 344 tnyaseCAINKVYCSEILGRIADEAVQIHGGYGYMQEYEVERLYRDARISRIFEGTNEINRLTIAKLLMKE 414
Cdd:cd01162   311 ------CAMAKRFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLTR 375
LCAD cd01160
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ...
 30-409 7.89e-90

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: 281.70  E-value: 7.89e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588  30 EEDRLISKTTESFVKNEVMPLLESIDQQDhESVKKLFQKAGELGLLSIEVPEDCGGLSLSKKLSGLVAEKMGAGGSFSVS 109
Cdd:cd01160     1 EEHDAFRDVVRRFFAKEVAPFHHEWEKAG-EVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARAGGSGPG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 110 FNIHAGVGTLPYIYYGTEEQKQKYLPKLASGEWIGAYALTEPGAGSDALNAKTTAvlNREGTAWILNGEKQWITNAQVAD 189
Cdd:cd01160    80 LSLHTDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTA--RKDGDHYVLNGSKTFITNGMLAD 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 190 VYVVFAKT------AEGMTAFIVERSFKGVSIGPEEKKMGIKGSSTATLILEEVEVPSDNVLGHIGKGHHVALNILNMAR 263
Cdd:cd01160   158 VVIVVARTggeargAGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQER 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 264 LKLAFSNIGTAKQALNLAVSYAKQRKQFNKPIIGFSMIQEKIADMAVSIFGAESAAYRTADcldnvLDSALPLDdrlrkl 343
Cdd:cd01160   238 LLIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAW-----RHEQGRLD------ 306

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1716756588 344 tnyASECAINKVYCSEILGRIADEAVQIHGGYGYMQEYEVERLYRDARISRIFEGTNEINRLTIAK 409
Cdd:cd01160   307 ---VAEASMAKYWATELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISR 369
GCD cd01151
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ...
 29-409 7.66e-81

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: 258.83  E-value: 7.66e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588  29 TEEDRLISKTTESFVKNEVMPLLESIDQQDHESvKKLFQKAGELGLLSIeVPEDCGGLSLSKKLSGLVA---EKMGAGGS 105
Cdd:cd01151    14 TEEERAIRDTAREFCQEELAPRVLEAYREEKFD-RKIIEEMGELGLLGA-TIKGYGCAGLSSVAYGLIArevERVDSGYR 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 106 FSVSfnIHAGVGTLPYIYYGTEEQKQKYLPKLASGEWIGAYALTEPGAGSDALNAKTTAvlNREGTAWILNGEKQWITNA 185
Cdd:cd01151    92 SFMS--VQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRA--RKDGGGYKLNGSKTWITNS 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 186 QVADVYVVFAKTAE--GMTAFIVERSFKGVSIGPEEKKMGIKGSSTATLILEEVEVPSDNVLGHIgKGHHVALNILNMAR 263
Cdd:cd01151   168 PIADVFVVWARNDEtgKIRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPGA-EGLRGPFKCLNNAR 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 264 LKLAFSNIGTAKQALNLAVSYAKQRKQFNKPIIGFSMIQEKIADMAVSIFGAESAAYRTADCLDNVLdsALPLDDRLRKL 343
Cdd:cd01151   247 YGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGK--ATPEQISLLKR 324

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1716756588 344 TNyasecainkvyCSEILgRIADEAVQIHGGYGYMQEYEVERLYRDARISRIFEGTNEINRLTIAK 409
Cdd:cd01151   325 NN-----------CGKAL-EIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGR 378
MCAD cd01157
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ...
 28-412 2.24e-79

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: 254.43  E-value: 2.24e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588  28 FTEEDRLISKTTESFVKNEVMPLLESIDQQDHESVKkLFQKAGELGLLSIEVPEDCGGLSLSKKLSGLVAEKMgAGGSFS 107
Cdd:cd01157     1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWP-LIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEEL-AYGCTG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 108 VSFNIHA-GVGTLPYIYYGTEEQKQKYLPKLASGEWIGAYALTEPGAGSDALNAKTTAVlnREGTAWILNGEKQWITNAQ 186
Cdd:cd01157    79 VQTAIEAnSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAE--KKGDEYIINGQKMWITNGG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 187 VADVYVVFAKT--------AEGMTAFIVERSFKGVSIGPEEKKMGIKGSSTATLILEEVEVPSDNVLGHIGKGHHVALNI 258
Cdd:cd01157   157 KANWYFLLARSdpdpkcpaSKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGA 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 259 LNMARLKLAFSNIGTAKQALNLAVSYAKQRKQFNKPIIGFSMIQEKIADMAVSIFGAESAAYRTADCLDNVldsalpldd 338
Cdd:cd01157   237 FDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSG--------- 307

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1716756588 339 rlRKLTNYASecaINKVYCSEILGRIADEAVQIHGGYGYMQEYEVERLYRDARISRIFEGTNEINRLTIAKLLM 412
Cdd:cd01157   308 --RRNTYYAS---IAKAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHL 376
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 2-414 7.00e-79

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 254.03  E-value: 7.00e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588   2 GKAKLRWNEPLISQHESAAEGFTPEDFTEEDRlisKTTESFVKNEVMPLLESIDQQDH--ESVKkLFQKAGELGLLSIEV 79
Cdd:PLN02519    3 LSAAKARRRGLARRFSSSSSSLLFDDTQLQFK---ESVQQFAQENIAPHAAAIDATNSfpKDVN-LWKLMGDFNLHGITA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588  80 PEDCGGLSLSKKLSGLVAEKMG-AGGSFSVSFNIHAGVGTLPYIYYGTEEQKQKYLPKLASGEWIGAYALTEPGAGSDAL 158
Cdd:PLN02519   79 PEEYGGLGLGYLYHCIAMEEISrASGSVGLSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 159 NAKTTAvlNREGTAWILNGEKQWITNAQVADVYVVFAKT-----AEGMTAFIVERSFKGVSIGPEEKKMGIKGSSTATLI 233
Cdd:PLN02519  159 SMKCKA--ERVDGGYVLNGNKMWCTNGPVAQTLVVYAKTdvaagSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELV 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 234 LEEVEVPSDNVLGHIGKGHHVALNILNMARLKLAFSNIGTAKQALNLAVSYAKQRKQFNKPIIGFSMIQEKIADMAVSIF 313
Cdd:PLN02519  237 FENCFVPEENVLGQEGKGVYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQ 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 314 GAESAAYRTA-DCLDNVLDsalplddrlRKltnyasECAINKVYCSEILGRIADEAVQIHGGYGYMQEYEVERLYRDARI 392
Cdd:PLN02519  317 SSRSYVYSVArDCDNGKVD---------RK------DCAGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKL 381

                         410       420
                  ....*....|....*....|..
gi 1716756588 393 SRIFEGTNEINRLTIAKLLMKE 414
Cdd:PLN02519  382 YEIGAGTSEIRRMLIGRELFKE 403
PTZ00461 PTZ00461
isovaleryl-CoA dehydrogenase; Provisional
 29-416 2.11e-69

isovaleryl-CoA dehydrogenase; Provisional


Pssm-ID: 185640 [Multi-domain]  Cd Length: 410  Bit Score: 229.44  E-value: 2.11e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588  29 TEEDRLISKTTESFVKNEVMPLLESIDQQDHESVKkLFQKAGELGLLSIEVPEDCGGLSLSKKLSGLVAEKMGA-GGSFS 107
Cdd:PTZ00461   38 TPEHAALRETVAKFSREVVDKHAREDDINMHFNRD-LFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKyDPGFC 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 108 VSFNIHAGVGTLPYIYYGTEEQKQKYLPKLASGEWIGAYALTEPGAGSDALNAKTTAVLNREGTaWILNGEKQWITNAQV 187
Cdd:PTZ00461  117 LAYLAHSMLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNGN-YVLNGSKIWITNGTV 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 188 ADVYVVFAKTAEGMTAFIVERSFKGVSIGPEEKKMGIKGSSTATLILEEVEVPSDNVLGHIGKGHHVALNILNMARLKLA 267
Cdd:PTZ00461  196 ADVFLIYAKVDGKITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELERVTLA 275

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 268 FSNIGTAKQALNLAVSYAKQRKQFNKPIIGFSMIQEKIADMAVSIFGAESAAYrtadcldNVLDSALPLD-DRLrkltny 346
Cdd:PTZ00461  276 AMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVY-------SVSHNVHPGNkNRL------ 342

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 347 ASECAinKVYCSEILGRIADEAVQIHGGYGYMQEYEVERLYRDARISRIFEGTNEINRLTIAKLLMKEVQ 416
Cdd:PTZ00461  343 GSDAA--KLFATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIEAHHKNITKDLLKGLK 410
ACAD_fadE5 cd01153
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ...
 38-402 1.26e-59

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: 203.39  E-value: 1.26e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588  38 TTESFVKNEVMPLLESIDQQ----DHESV------KKLFQKAGELGLLSIEVPEDCGGLSLSKKLSGLVAEKMGAG-GSF 106
Cdd:cd01153     4 EVARLAENVLAPLNADGDREgpvfDDGRVvvpppfKEALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGdAPL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 107 SVSFNIHAGVGTLpyIYYGTEEQKQKYLPKLASGEWIGAYALTEPGAGSDALNAKTTAVLNREGTaWILNGEKQWITNAQ 186
Cdd:cd01153    84 MYASGTQGAAATL--LAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADGS-WRINGVKRFISAGE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 187 VAD----VYVVFAKTAE------GMTAFIV-------ERSfkGVSIGPEEKKMGIKGSSTATLILEEVEVPsdnVLGHIG 249
Cdd:cd01153   161 HDMseniVHLVLARSEGappgvkGLSLFLVpkflddgERN--GVTVARIEEKMGLHGSPTCELVFDNAKGE---LIGEEG 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 250 KGHHVALNILNMARLKLAFSNIGTAKQALNLAVSYAKQRKQFNKPIIGFS--------MIQEKIADMAVSIFGAESAAYR 321
Cdd:cd01153   236 MGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLIKAAPavtiihhpDVRRSLMTQKAYAEGSRALDLY 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 322 TADCLDNVLDSALPLDDR--LRKLTNYASecAINKVYCSEILGRIADEAVQIHGGYGYMQEYEVERLYRDARISRIFEGT 399
Cdd:cd01153   316 TATVQDLAERKATEGEDRkaLSALADLLT--PVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGT 393


                  ...
gi 1716756588 400 NEI 402
Cdd:cd01153   394 TGI 396
PRK12341 PRK12341
acyl-CoA dehydrogenase;
27-402 5.67e-53

acyl-CoA dehydrogenase;


Pssm-ID: 183454 [Multi-domain]  Cd Length: 381  Bit Score: 184.93  E-value: 5.67e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588  27 DF--TEEDRLISKTTESFVKNEVM-PLLESIDQQdHESVKKLFQKAGELGLLSIEVPEDCGGLSLSKKLSGLVAEKMGAG 103
Cdd:PRK12341    2 DFslTEEQELLLASIRELITRNFPeEYFRTCDEN-GTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEVSKC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 104 GS----FSVSFNIHAgvgtlpYIYYGTEEQKQK-YLPKLASGEWIGAYALTEPGAGSDALNAKTTAVlNREGTAwILNGE 178
Cdd:PRK12341   81 GApaflITNGQCIHS------MRRFGSAEQLRKtAESTLETGDPAYALALTEPGAGSDNNSATTTYT-RKNGKV-YLNGQ 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 179 KQWITNAQVADVYVVFAK------TAEGMTAFIVERSFKGVSIGPEEKkMGIKGSSTATLILEEVEVPSDNVLGHIGKGH 252
Cdd:PRK12341  153 KTFITGAKEYPYMLVLARdpqpkdPKKAFTLWWVDSSKPGIKINPLHK-IGWHMLSTCEVYLDNVEVEESDLVGEEGMGF 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 253 HVALNILNMARLKLAFSNIGTAKQALNLAVSYAKQRKQFNKPIIGFSMIQEKIADMAVSIFGAESAAYRTADCLDNVLDS 332
Cdd:PRK12341  232 LNVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQSL 311

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 333 ALPlddrlrkltnyaseCAINKVYCSEILGRIADEAVQIHGGYGYMQEYEVERLYRDARISRIFEGTNEI 402
Cdd:PRK12341  312 RTS--------------AALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEI 367
PRK03354 PRK03354
crotonobetainyl-CoA dehydrogenase; Validated
 57-414 9.39e-51

crotonobetainyl-CoA dehydrogenase; Validated


Pssm-ID: 179566 [Multi-domain]  Cd Length: 380  Bit Score: 178.87  E-value: 9.39e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588  57 QDHESVKKLFQKAGELGLLSIEVPEDCGGLSLSKKLSGLVAEKMG-AGGSFSVSFNIHAGVGTLpyIYYGTEEQKQKYLP 135
Cdd:PRK03354   34 RDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGrLGAPTYVLYQLPGGFNTF--LREGTQEQIDKIMA 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 136 KLASGEWIGAYALTEPGAGSDALNAKTTavLNREGTAWILNGEKQWITNAQVADVYVVFAKTAEG-----MTAFIVERSF 210
Cdd:PRK03354  112 FRGTGKQMWNSAITEPGAGSDVGSLKTT--YTRRNGKVYLNGSKCFITSSAYTPYIVVMARDGASpdkpvYTEWFVDMSK 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 211 KGVSIGPEEKkMGIKGSSTATLILEEVEVPSDNVLGHIGKGHHVALNILNMARLKLAFSNIGTAKQALNLAVSYAKQRKQ 290
Cdd:PRK03354  190 PGIKVTKLEK-LGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQ 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 291 FNKPIIGFSMIQEKIADMAVSIFGAESAAYRTADCLDN-VLDSAlplddrlrkltnyasECAINKVYCSEILGRIADEAV 369
Cdd:PRK03354  269 FGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNgTITSG---------------DAAMCKYFCANAAFEVVDSAM 333

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1716756588 370 QIHGGYGYMQEYEVERLYRDARISRIFEGTNEINRLTIAKLLMKE 414
Cdd:PRK03354  334 QVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAVLKQ 378
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 249-409 7.43e-42

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: 147.40  E-value: 7.43e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 249 GKGHHVALNILNMARLKLAFSNIGTAKQALNLAVSYAKQRKQFNKPIIGFSMIQEKIADMAVSIFGAESAAYRTADCLDN 328
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 329 VLDSALplddrlrkltnyasECAINKVYCSEILGRIADEAVQIHGGYGYMQEYEVERLYRDARISRIFEGTNEINRLTIA 408
Cdd:pfam00441  81 GGPDGA--------------EASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIA 146


                  .
gi 1716756588 409 K 409
Cdd:pfam00441 147 R 147
ACAD_fadE6_17_26 cd01152
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ...
 73-409 8.60e-42

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: 154.81  E-value: 8.60e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588  73 GLLSIEVPEDCGGLSLSKKLSGLVAEKMGAGGSfSVSFNIhAGVGTL-PYI-YYGTEEQKQKYLPKLASGEWIGAYALTE 150
Cdd:cd01152    48 GWAAPGWPKEYGGRGASLMEQLIFREEMAAAGA-PVPFNQ-IGIDLAgPTIlAYGTDEQKRRFLPPILSGEEIWCQGFSE 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 151 PGAGSDALNAKTTAVlnREGTAWILNGEKQWITNAQVADVYVVFAKTA------EGMTAFIVERSFKGVSIGPEEKKMGi 224
Cdd:cd01152   126 PGAGSDLAGLRTRAV--RDGDDWVVNGQKIWTSGAHYADWAWLLVRTDpeapkhRGISILLVDMDSPGVTVRPIRSING- 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 225 kGSSTATLILEEVEVPSDNVLGHIGKGHHVALNILNMARLklafSNIGTAKQALNLAVSYAKQRKQFNKPIIGFSMIQEK 304
Cdd:cd01152   203 -GEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTLNFERV----SIGGSAATFFELLLARLLLLTRDGRPLIDDPLVRQR 277

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 305 IADMAVSIFGAESAAYRTADCLDNVLDSALplddrlrkltnyasECAINKVYCSEILGRIADEAVQIHGGYGYMQEY--- 381
Cdd:cd01152   278 LARLEAEAEALRLLVFRLASALAAGKPPGA--------------EASIAKLFGSELAQELAELALELLGTAALLRDPapg 343

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1716756588 382 -----EVERLYRDARISRIFEGTNEINRLTIAK 409
Cdd:cd01152   344 aelagRWEADYLRSRATTIYGGTSEIQRNIIAE 376
ACAD_FadE2 cd01155
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ...
 42-413 1.82e-41

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: 154.08  E-value: 1.82e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588  42 FVKNEVMPL----------LESIDQQDHESVKKLFQKAGELGLLSIEVPEDCGGLSLSKKLSGLVAEKMGAGGSFSVSFN 111
Cdd:cd01155    13 FMEEHVYPAeqefleyyaeGGDRWWTPPPIIEKLKAKAKAEGLWNLFLPEVSGLSGLTNLEYAYLAEETGRSFFAPEVFN 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 112 IHA-GVGTLPYIY-YGTEEQKQKYLPKLASGEWIGAYALTEPG-AGSDALNAKTTAVlnREGTAWILNGEKQWITNAQVA 188
Cdd:cd01155    93 CQApDTGNMEVLHrYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIE--RDGDDYVINGRKWWSSGAGDP 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 189 D--VYVVFAKTaEGMTA--------FIVERSFKGVSIgpeEKKMGIKGSSTA-----TLILEEVEVPSDNVLGHIGKGHH 253
Cdd:cd01155   171 RckIAIVMGRT-DPDGAprhrqqsmILVPMDTPGVTI---IRPLSVFGYDDAphghaEITFDNVRVPASNLILGEGRGFE 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 254 VALNILNMARLKLAFSNIGTAKQALNLAVSYAKQRKQFNKPIIGFSMIQEKIADMAVSIFGAESAAYRTADCLDNVLDSA 333
Cdd:cd01155   247 IAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAHMIDTVGNKA 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 334 LplddrlrkltnyASECAINKVYCSEILGRIADEAVQIHGGYGYMQEYEVERLYRDARISRIFEGTNEINRLTIAKLLMK 413
Cdd:cd01155   327 A------------RKEIAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIARMELK 394
AidB cd01154
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ...
 124-413 1.76e-39

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: 149.06  E-value: 1.76e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 124 YGTEEQKQKYLPKLASGE---WIGAYALTEPGAGSDALNAKTTAVLNrEGTAWILNGEKqWITNAQVADVYVVFAKT--- 197
Cdd:cd01154   126 YGPEELKQYLPGLLSDRYktgLLGGTWMTEKQGGSDLGANETTAERS-GGGVYRLNGHK-WFASAPLADAALVLARPega 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 198 ---AEGMTAFIVER-----SFKGVSIGPEEKKMGIKGSSTAtlileEVEVpsDNVLGHI----GKGHHVALNILNMARLK 265
Cdd:cd01154   204 pagARGLSLFLVPRlledgTRNGYRIRRLKDKLGTRSVATG-----EVEF--DDAEAYLigdeGKGIYYILEMLNISRLD 276

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 266 LAFSNIGTAKQALNLAVSYAKQRKQFNKPIIGFSMIQEKIADMAVSIFGAESAAYRTADcldnVLDSALPLDDRLRKLTN 345
Cdd:cd01154   277 NAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAAR----AFDRAAADKPVEAHMAR 352

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1716756588 346 YASecAINKVYCSEILGRIADEAVQIHGGYGYMQEYEVERLYRDARISRIFEGTNEINRLTIAKLLMK 413
Cdd:cd01154   353 LAT--PVAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQALDVLRVLVK 418
PLN02526 PLN02526
acyl-coenzyme A oxidase
 29-409 3.48e-38

acyl-coenzyme A oxidase


Pssm-ID: 178141 [Multi-domain]  Cd Length: 412  Bit Score: 145.38  E-value: 3.48e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588  29 TEEDRLISKTTESFVKNEVMPLLESIdqqdHESVKKLFQ---KAGELGLLSIEVP-EDCGGLSLSKklSGL-VAEKMGAG 103
Cdd:PLN02526   30 TPEEQALRKRVRECMEKEVAPIMTEY----WEKAEFPFHiipKLGSLGIAGGTIKgYGCPGLSITA--SAIaTAEVARVD 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 104 GSFSVSFNIHAGVGTLPYIYYGTEEQKQKYLPKLASGEWIGAYALTEPGAGSDALNAKTTAVLNREGtaWILNGEKQWIT 183
Cdd:PLN02526  104 ASCSTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGG--WILNGQKRWIG 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 184 NAQVADVYVVFAK--TAEGMTAFIVERSFKGVSIGPEEKKMGIKGSSTATLILEEVEVPSDNVLGHIGKGHHVAlNILNM 261
Cdd:PLN02526  182 NSTFADVLVIFARntTTNQINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRLPGVNSFQDTN-KVLAV 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 262 ARLKLAFSNIGTAKQALNLAVSYAKQRKQFNKPIIGFSMIQEKIADMavsifgaesaayrtadcLDNVLDSALpLDDRLR 341
Cdd:PLN02526  261 SRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRM-----------------LGNIQAMFL-VGWRLC 322

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1716756588 342 KLtnYAS------ECAINKVYCSEILGRIADEAVQIHGGYGYMQEYEVERLYRDARISRIFEGTNEINRLTIAK 409
Cdd:PLN02526  323 KL--YESgkmtpgHASLGKAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGR 394
PTZ00456 PTZ00456
acyl-CoA dehydrogenase; Provisional
 63-452 5.76e-31

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185635 [Multi-domain]  Cd Length: 622  Bit Score: 127.68  E-value: 5.76e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588  63 KKLFQKAGELGLLSIEVPEDCGGLSLSKKLSGLVAEKMG-AGGSFSVSFNIHAGVG-TLpyIYYGTEEQKQKYLPKLASG 140
Cdd:PTZ00456  102 KEAYQALKAGGWTGISEPEEYGGQALPLSVGFITRELMAtANWGFSMYPGLSIGAAnTL--MAWGSEEQKEQYLTKLVSG 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 141 EWIGAYALTEPGAGSDALNAKTTAVLNREGTaWILNGEKQWIT----NAQVADVYVVFAK------TAEGMTAFIVER-- 208
Cdd:PTZ00456  180 EWSGTMCLTEPQCGTDLGQVKTKAEPSADGS-YKITGTKIFISagdhDLTENIVHIVLARlpnslpTTKGLSLFLVPRhv 258

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 209 --------SFKGVSIGPEEKKMGIKGSSTATLILEEvevPSDNVLGHIGKGHHVALNILNMARLKLAFSNIGTAKQALNL 280
Cdd:PTZ00456  259 vkpdgsleTAKNVKCIGLEKKMGIKGSSTCQLSFEN---SVGYLIGEPNAGMKQMFTFMNTARVGTALEGVCHAELAFQN 335

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 281 AVSYAKQRKQF------------NKPIIGFSMIQEKIADMAVSIFGAESAAYRTADCLDNVLDSALP-----LDDRLRKL 343
Cdd:PTZ00456  336 ALRYARERRSMralsgtkepekpADRIICHANVRQNILFAKAVAEGGRALLLDVGRLLDIHAAAKDAatreaLDHEIGFY 415

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 344 TNYASECAinkvycSEILGRIADEAVQIHGGYGYMQEYEVERLYRDARISRIFEGTNEINRLtiaKLLMKEVQQNGISEP 423
Cdd:PTZ00456  416 TPIAKGCL------TEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQAL---DFIGRKVLSLKGGNE 486

                         410       420
                  ....*....|....*....|....*....
gi 1716756588 424 EAQLGSEGNRNRRFIQLSNRLFGKTLKAL 452
Cdd:PTZ00456  487 VARFGKRVSKLVRAHLFSRGALGQYARRL 515
Acyl-CoA_dh_N pfam02771
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ...
 29-141 9.42e-31

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: 115.64  E-value: 9.42e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588  29 TEEDRLISKTTESFVKNEVMPLLESIDQQDHESvKKLFQKAGELGLLSIEVPEDCGGLSLSKKLSGLVAEKMG-AGGSFS 107
Cdd:pfam02771   1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFP-RELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELArADASVA 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1716756588 108 VSFNIHAGVGTLPYIYYGTEEQKQKYLPKLASGE 141
Cdd:pfam02771  80 LALSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
Acyl-CoA_dh_M pfam02770
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ...
 145-235 2.21e-29

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: 111.22  E-value: 2.21e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 145 AYALTEPGAGSDALNAKTTAVlNREGTAWILNGEKQWITNAQVADVYVVFAKTA-----EGMTAFIVERSFKGVSIGPEE 219
Cdd:pfam02770   1 AFALTEPGAGSDVASLKTTAA-DGDGGGWVLNGTKWWITNAGIADLFLVLARTGgddrhGGISLFLVPKDAPGVSVRRIE 79

                          90
                  ....*....|....*.
gi 1716756588 220 KKMGIKGSSTATLILE 235
Cdd:pfam02770  80 TKLGVRGLPTGELVFD 95
PRK13026 PRK13026
acyl-CoA dehydrogenase; Reviewed
 40-376 1.54e-25

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 237277 [Multi-domain]  Cd Length: 774  Bit Score: 111.59  E-value: 1.54e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588  40 ESFVKNEVMPLLESID-----QQDHESVKKLFQKAGELGLLSIEVPEDCGGLSLSKKLSGLVAEKMGaggSFSVSFNIHA 114
Cdd:PRK13026   83 QAFIDNEVETLLTMLDdwdivQNRKDLPPEVWDYLKKEGFFALIIPKEYGGKGFSAYANSTIVSKIA---TRSVSAAVTV 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 115 ------GVGTLpYIYYGTEEQKQKYLPKLASGEWIGAYALTEPGAGSDALNAKTTAVLNR---EGTAWI---LNGEKQWI 182
Cdd:PRK13026  160 mvpnslGPGEL-LTHYGTQEQKDYWLPRLADGTEIPCFALTGPEAGSDAGAIPDTGIVCRgefEGEEVLglrLTWDKRYI 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 183 TNAQVADVY-VVF----------AKTAEGMTAFIVERSFKGVSIGPEEKKMGI---KGSSTAtlilEEVEVPSDNVLG-- 246
Cdd:PRK13026  239 TLAPVATVLgLAFklrdpdgllgDKKELGITCALIPTDHPGVEIGRRHNPLGMafmNGTTRG----KDVFIPLDWIIGgp 314

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 247 -HIGKGHHVALNILNMAR-LKLAFSNIGTAKQALNLAVSYAKQRKQFNKPIIGFSMIQEKIADMAVSIFGAESAAYRTAD 324
Cdd:PRK13026  315 dYAGRGWRMLVECLSAGRgISLPALGTASGHMATRTTGAYAYVRRQFGMPIGQFEGVQEALARIAGNTYLLEAARRLTTT 394

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1716756588 325 CLDnvldsalplddrLRKLTNYASecAINKVYCSEILGRIADEAVQIHGGYG 376
Cdd:PRK13026  395 GLD------------LGVKPSVVT--AIAKYHMTELARDVVNDAMDIHAGKG 432
fadE PRK09463
acyl-CoA dehydrogenase; Reviewed
 124-400 7.15e-25

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 236528 [Multi-domain]  Cd Length: 777  Bit Score: 109.52  E-value: 7.15e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 124 YGTEEQKQKYLPKLASGEWIGAYALTEPGAGSDALNAKTTAVL-----NREGTAWI-LNGEKQWITNAQVADVY-VVF-- 194
Cdd:PRK09463  175 YGTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGSIPDTGVVckgewQGEEVLGMrLTWNKRYITLAPIATVLgLAFkl 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 195 --------AKTAEGMTAFIVERSFKGVSIGPEEKKMG-------IKGsstatlilEEVEVPSDNVLG---HIGKGHHVAL 256
Cdd:PRK09463  255 ydpdgllgDKEDLGITCALIPTDTPGVEIGRRHFPLNvpfqngpTRG--------KDVFIPLDYIIGgpkMAGQGWRMLM 326

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 257 NILNMAR-LKLAFSNIGTAKQALNLAVSYAKQRKQFNKPIIGFSMIQEKIADMAvsifgaeSAAYrtadcldnVLDSAlp 335
Cdd:PRK09463  327 ECLSVGRgISLPSNSTGGAKLAALATGAYARIRRQFKLPIGKFEGIEEPLARIA-------GNAY--------LMDAA-- 389

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1716756588 336 lddrlRKLTNYA----------SecAINKVYCSEILGRIADEAVQIHGGYGYM---QEYeVERLYRDARISRIFEGTN 400
Cdd:PRK09463  390 -----RTLTTAAvdlgekpsvlS--AIAKYHLTERGRQVINDAMDIHGGKGIClgpNNF-LARAYQAAPIAITVEGAN 459
AXO cd01150
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ...
 15-480 2.15e-21

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: 98.17  E-value: 2.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588  15 QHESAAEGFTPEDFT------EEDRLISKTTESFVKNEVMPLLESIDQQDH-----ESVKKLFQKAGELGL-LSIEVPED 82
Cdd:cd01150     4 DKERASATFDWKALThileggEENLRRKREVERELESDPLFQRELPSKHLSreelyEELKRKAKTDVERMGeLMADDPEK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588  83 cgGLSLSKKLsglvaekMGAGGSFSVSFNIHAGVgTLPYIY-YGTEEQKQKYLPKLASGEWIGAYALTEPGAGSDALNAK 161
Cdd:cd01150    84 --MLALTNSL-------GGYDLSLGAKLGLHLGL-FGNAIKnLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLE 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 162 TTAVLNREGTAWILN-----GEKQWITNAQV-ADVYVVFAK-----TAEGMTAFIVE-------RSFKGVSIGPEEKKMG 223
Cdd:cd01150   154 TTATYDPLTQEFVINtpdftATKWWPGNLGKtATHAVVFAQlitpgKNHGLHAFIVPirdpkthQPLPGVTVGDIGPKMG 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 224 IKGSSTATLILEEVEVPSDNVLG----------------HIGKGHHVALNILNMARLKLAFSNIGTAKQALNLAVSYAKQ 287
Cdd:cd01150   234 LNGVDNGFLQFRNVRIPRENLLNrfgdvspdgtyvspfkDPNKRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAV 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 288 RKQFNK-------PIIGFSMIQEKIADM-AVSI---FGAESAAYRTADCLDnvlDSALPLDDRLRKLtnYASECAInKVY 356
Cdd:cd01150   314 RRQFGPkpsdpevQILDYQLQQYRLFPQlAAAYafhFAAKSLVEMYHEIIK---ELLQGNSELLAEL--HALSAGL-KAV 387

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 357 CSEILGRIADEAVQIHGGYGYMQEYEVERLYRDARISRIFEGTNEINRLTIAKLLMKEVQQngISEPEAQLGSEGNRNRR 436
Cdd:cd01150   388 ATWTAAQGIQECREACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTANYLLKKYAQ--AFSLADYLEAYEWLAAH 465

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 1716756588 437 FIQLSNRLFGKTLKALIRSRVNTQEDQEYARLLADMKKEIYVME 480
Cdd:cd01150   466 LLRHAAAQLEKLKKSGSGSFEARNNSQVHLRCAAKAHTEYTVLQ 509
PLN02876 PLN02876
acyl-CoA dehydrogenase
 124-416 6.86e-20

acyl-CoA dehydrogenase


Pssm-ID: 215473 [Multi-domain]  Cd Length: 822  Bit Score: 93.71  E-value: 6.86e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 124 YGTEEQKQKYLPKLASGEWIGAYALTEPG-AGSDALNAKTTAVlnREGTAWILNGEKQWITNAQ--VADVYVVFAKT--- 197
Cdd:PLN02876  532 YGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDATNIECSIR--RQGDSYVINGTKWWTSGAMdpRCRVLIVMGKTdfn 609

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 198 ---AEGMTAFIVERSFKGVSIGPEEKKMGIKGS--STATLILEEVEVPSDNVLGHIGKGHHVALNILNMARLKLAFSNIG 272
Cdd:PLN02876  610 apkHKQQSMILVDIQTPGVQIKRPLLVFGFDDAphGHAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHHCMRLIG 689

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 273 TAKQALNLAVSYAKQRKQFNKPIIGFSMIQEKIADMAVSIFGAESAayrtadcldnVLDSAlpldDRLRKLTNYASE--C 350
Cdd:PLN02876  690 AAERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLL----------VLEAA----DQLDRLGNKKARgiI 755

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1716756588 351 AINKVYCSEILGRIADEAVQIHGGYGYMQEYEVERLYRDARISRIFEGTNEINRLTIAKLLMKEVQ 416
Cdd:PLN02876  756 AMAKVAAPNMALKVLDMAMQVHGAAGVSSDTVLAHLWATARTLRIADGPDEVHLGTIAKLELQRAK 821
Acyl-CoA_dh_2 pfam08028
Acyl-CoA dehydrogenase, C-terminal domain;
271-401 1.75e-18

Acyl-CoA dehydrogenase, C-terminal domain;


Pssm-ID: 429790 [Multi-domain]  Cd Length: 133  Bit Score: 82.01  E-value: 1.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 271 IGTAKQALNLAVSYAKQRKQ--FNKPIIGFSMIQEKIADMAVSIFGAESAAYRTADCLDNVLDSALPLDDRLRKltnyas 348
Cdd:pfam08028   7 LGAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAARIDAARLLLERAAARIEAAAAAGKPVTPALRA------ 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1716756588 349 ECAINKVYCSEILGRIADEAVQIHGGYGYMQEYEVERLYRDARISRIFEGTNE 401
Cdd:pfam08028  81 EARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
PRK11561 PRK11561
isovaleryl CoA dehydrogenase; Provisional
 148-463 8.38e-18

isovaleryl CoA dehydrogenase; Provisional


Pssm-ID: 183199 [Multi-domain]  Cd Length: 538  Bit Score: 86.73  E-value: 8.38e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 148 LTEPGAGSDALnAKTTAVLNREGTAWILNGEKqWITNAQVADVYVVFAKTAEGMTAFIVER-----SFKGVSIGPEEKKM 222
Cdd:PRK11561  184 MTEKQGGSDVL-SNTTRAERLADGSYRLVGHK-WFFSVPQSDAHLVLAQAKGGLSCFFVPRflpdgQRNAIRLERLKDKL 261

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 223 GIKGSSTAtlileEVEV--PSDNVLGHIGKGHHVALNILNMARLKLAFSNIGTAKQALNLAVSYAKQRKQFNKPIIGFSM 300
Cdd:PRK11561  262 GNRSNASS-----EVEFqdAIGWLLGEEGEGIRLILKMGGMTRFDCALGSHGLMRRAFSVAIYHAHQRQVFGKPLIEQPL 336

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 301 IQEKIADMAVSIFGAESAAYRTADCLDNVLDsalPLDDRLRKLTNYASECAInkvyCSEILGRIAdEAVQIHGGYGYMQE 380
Cdd:PRK11561  337 MRQVLSRMALQLEGQTALLFRLARAWDRRAD---AKEALWARLFTPAAKFVI----CKRGIPFVA-EAMEVLGGIGYCEE 408

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 381 YEVERLYRDARISRIFEGTNEINRLTIAKLLMKevqQNGISEPEAQLGSEgnrnrrfIQLSNRLFGKTLKALIRSRVNTQ 460
Cdd:PRK11561  409 SELPRLYREMPVNSIWEGSGNIMCLDVLRVLNK---QPGVYDLLSEAFVE-------VKGQDRHFDRAVRQLQQRLRKPA 478


                  ...
gi 1716756588 461 EDQ 463
Cdd:PRK11561  479 EEQ 481
DszC cd01163
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ...
 71-329 2.14e-16

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: 81.22  E-value: 2.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588  71 ELGLLSIEVPEDCGGLSLS-KKLSGLVAEKMGAGGSFSVSFNIHAG-VGTLpyIYYGTEEQKQKYLPKLASGEWIGAyAL 148
Cdd:cd01163    33 QSGLGTLRVPKEYGGLGASlPDLYEVVRELAAADSNIAQALRAHFGfVEAL--LLAGPEQFRKRWFGRVLNGWIFGN-AV 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 149 TEpgAGSDALNAKTTAVLnREGTAWILNGEKQWITNAQVADVYVVFAKTAEG-MTAFIVERSFKGVSIGPEEKKMGIKGS 227
Cdd:cd01163   110 SE--RGSVRPGTFLTATV-RDGGGYVLNGKKFYSTGALFSDWVTVSALDEEGkLVFAAVPTDRPGITVVDDWDGFGQRLT 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 228 STATLILEEVEVPSDNVLGHIGKGHHvalNILNMARLKLAFSNI--GTAKQALNLAVSYAKQRKqfnKPIIGFS------ 299
Cdd:cd01163   187 ASGTVTFDNVRVEPDEVLPRPNAPDR---GTLLTAIYQLVLAAVlaGIARAALDDAVAYVRSRT---RPWIHSGaesard 260

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1716756588 300 --MIQEKIADMAVSIFGAESAAYRTADCLDNV 329
Cdd:cd01163   261 dpYVQQVVGDLAARLHAAEALVLQAARALDAA 292
PLN02636 PLN02636
acyl-coenzyme A oxidase
 100-417 5.75e-16

acyl-coenzyme A oxidase


Pssm-ID: 215342 [Multi-domain]  Cd Length: 686  Bit Score: 81.06  E-value: 5.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 100 MGAGGSFSVSFNIHAGV------GTLpyIYYGTEEQKQKYLPKLASGEWIGAYALTEPGAGSDALNAKTTAVLNREGTAW 173
Cdd:PLN02636  127 TEAVGSVDMSLGIKLGVqyslwgGSV--INLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFDPLTDEF 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 174 ILN-----GEKQWITNAQVADVYV-VFAK-----------TAEGMTAFIVE-RSFK------GVSIGPEEKKMGIKGSST 229
Cdd:PLN02636  205 VINtpndgAIKWWIGNAAVHGKFAtVFARlklpthdskgvSDMGVHAFIVPiRDMKthqvlpGVEIRDCGHKVGLNGVDN 284

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 230 ATLILEEVEVPSDNVLGHIG----------------KGHHVALNILNMARLKLAFSNIGTAKQALNLAVSYAKQRKQFNK 293
Cdd:PLN02636  285 GALRFRSVRIPRDNLLNRFGdvsrdgkytsslptinKRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQFGP 364

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 294 P------IIGFSMIQEKIADMAVSIFGAESAayrTADCLDNVLDSALPLDDRLrkLTNYASECAINKVYCSEILGRIADE 367
Cdd:PLN02636  365 PkqpeisILDYQSQQHKLMPMLASTYAFHFA---TEYLVERYSEMKKTHDDQL--VADVHALSAGLKAYITSYTAKALST 439

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1716756588 368 AVQIHGGYGYMQEYEVERLYRDARISRIFEGTNEINRLTIAKLLMKEVQQ 417
Cdd:PLN02636  440 CREACGGHGYAAVNRFGSLRNDHDIFQTFEGDNTVLLQQVAADLLKQYKE 489
PTZ00460 PTZ00460
acyl-CoA dehydrogenase; Provisional
 118-425 7.89e-14

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185639 [Multi-domain]  Cd Length: 646  Bit Score: 74.50  E-value: 7.89e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 118 TLPYI-YYGTEEQKQKYLPKLASGEWIGAYALTEPGAGSDALNAKTTAVLNREGTAWILN-----------GEKQWITNA 185
Cdd:PTZ00460  102 VIPAFqVLGTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATYDKQTNEFVIHtpsveavkfwpGELGFLCNF 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 186 QVADVYVVFAKTAEGMTAFIVE-------RSFKGVSIGPEEKKMGIKGSSTATLILEEVEVPSDNVL---------GHIG 249
Cdd:PTZ00460  182 ALVYAKLIVNGKNKGVHPFMVRirdkethKPLQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLaryikvsedGQVE 261

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 250 KGHHVALNILNM--ARLKLAFSNIGTAKQALNLAVSYAKQRKQFNK------PIIGFSMIQEKIADMAVSIFGAESAAYR 321
Cdd:PTZ00460  262 RQGNPKVSYASMmyMRNLIIDQYPRFAAQALTVAIRYSIYRQQFTNdnkqenSVLEYQTQQQKLLPLLAEFYACIFGGLK 341

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 322 TADCLDNVLDSALPLDDRLRKLTnYASECAInKVYCSEILGRIADEAVQIHGGYGYMQEYEVERLYRDARISRIFEGTNE 401
Cdd:PTZ00460  342 IKELVDDNFNRVQKNDFSLLQLT-HAILSAA-KANYTYFVSNCAEWCRLSCGGHGYAHYSGLPAIYFDMSPNITLEGENQ 419

                         330       340
                  ....*....|....*....|....
gi 1716756588 402 INRLTIAKLLMKEVQQnGISEPEA 425
Cdd:PTZ00460  420 IMYLQLARYLLKQLQH-AVQKPEK 442
PTZ00457 PTZ00457
acyl-CoA dehydrogenase; Provisional
 84-340 2.87e-10

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185636 [Multi-domain]  Cd Length: 520  Bit Score: 62.98  E-value: 2.87e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588  84 GGLSLSKKLSGLVAEKMGAGG-SFSVSFNIHAGVGTLPYIYYGTEEQKQKYLPKLASGEWIGAYAlTEPGAGSDALNAKT 162
Cdd:PTZ00457   75 GGLGLGHTAHALIYEEVGTNCdSKLLSTIQHSGFCTYLLSTVGSKELKGKYLTAMSDGTIMMGWA-TEEGCGSDISMNTT 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 163 TAVLNREGTaWILNGEKQWItNAQVADVYVVFAKT------------AEGMTAFIVERSFKGVSIGPEekkmgikgssta 230
Cdd:PTZ00457  154 KASLTDDGS-YVLTGQKRCE-FAASATHFLVLAKTltqtaaeegateVSRNSFFICAKDAKGVSVNGD------------ 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 231 TLILEevEVPSDNVLGHIGKGHHVALNILNMARLKLAFSNIGTAKQALN-LAVSYAKQrkqfnkpiigfsMIQEKIADMA 309
Cdd:PTZ00457  220 SVVFE--NTPAADVVGVVGEGFKDAMITLFTEQYLYAASLLGIMKRVVQeLRGSNAEE------------GATDTVASFA 285

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1716756588 310 VSIFGAESAAYRTADCLDnvldsaLPLDDRL 340
Cdd:PTZ00457  286 CAMYAMESTLYALTANLD------LPTEDSL 310
PLN02443 PLN02443
acyl-coenzyme A oxidase
 125-419 2.08e-09

acyl-coenzyme A oxidase


Pssm-ID: 178062 [Multi-domain]  Cd Length: 664  Bit Score: 60.24  E-value: 2.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 125 GTEEQKQKYLPKLASGEWIGAYALTEPGAGSDALNAKTTAVLNREGTAWILN-----GEKQWITN-AQVADVYVVFAK-- 196
Cdd:PLN02443  114 GTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFDPKTDEFVIHsptltSSKWWPGGlGKVSTHAVVYARli 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 197 ---TAEGMTAFIVE-RSFK------GVSIGPEEKKMGIKGSST---ATLILEEVEVPSDNVLGHIGK----GHHVALNIL 259
Cdd:PLN02443  194 tngKDHGIHGFIVQlRSLDdhsplpGVTVGDIGMKFGNGAYNTmdnGFLRFDHVRIPRDQMLMRLSKvtreGKYVQSDVP 273

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 260 NmarlKLAFSNIGTAKQ------------ALNLAVSYAKQRKQFNK-------PIIGFSMIQEKIADMAVSIFgaesaAY 320
Cdd:PLN02443  274 R----QLVYGTMVYVRQtivadastalsrAVCIATRYSAVRRQFGSqdggpetQVIDYKTQQSRLFPLLASAY-----AF 344

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 321 RT---------ADCLDNVLD---SALP----LDDRLRKLTNYASECAInkvycseilgriaDEAVQIHGGYGYMQEYEVE 384
Cdd:PLN02443  345 RFvgewlkwlyTDVTQRLEAndfSTLPeahaCTAGLKSLTTSATADGI-------------EECRKLCGGHGYLCSSGLP 411

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1716756588 385 RLYRDARISRIFEGTNEINRLTIAKLLMKEVQQNG 419
Cdd:PLN02443  412 ELFAVYVPACTYEGDNVVLLLQVARFLMKTVSQLG 446
PLN02312 PLN02312
acyl-CoA oxidase
 123-291 2.82e-06

acyl-CoA oxidase


Pssm-ID: 215178 [Multi-domain]  Cd Length: 680  Bit Score: 50.16  E-value: 2.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 123 YYGTEEQKQKYLPKLASGEWIGAYALTEPGAGSDALNAKTTAVLNREGTAWILN-----GEKQWITN-AQVADVYVVFAK 196
Cdd:PLN02312  166 FLGTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTTYDPKTEEFVINtpcesAQKYWIGGaANHATHTIVFSQ 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716756588 197 -----TAEGMTAFIVE------RSFKGVSIGPEEKKMGIKGSSTATLILEEVEVPSDNVLGHIGK----GHHVA------ 255
Cdd:PLN02312  246 lhingKNEGVHAFIAQirdqdgNICPNIRIADCGHKIGLNGVDNGRIWFDNLRIPRENLLNSVADvspdGKYVSaikdpd 325

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1716756588 256 ------LNILNMARLKLAFSNIGTAKQALNLAVSYAKQRKQF 291
Cdd:PLN02312  326 qrfgafLAPLTSGRVTIAVSAIYSSKVGLAIAIRYSLSRRAF 367
 
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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