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Conserved domains on  [gi|1605303532|gb|QBR94628|]
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acyl-CoA dehydrogenase [Thermobifida fusca YX]

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 ...
 11-384 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 cd01158:

Pssm-ID: 447864 [Multi-domain]  Cd Length: 373  Bit Score: 532.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532  11 EEHEALREAIRSVAEDKIAPHAADVDEQSRFPQEAYEALRASDFHAPHVAEEYGGVGADALATCIVIEEIARVCASSSLI 90
Cdd:cd01158     1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532  91 PAV-NKLGSMPLILSGSDEVKQRYLPELASGEAMFSYGLSEREAGSDTASMRTRAVRDGDDWILNGQKSWITNAGISKYY 169
Cdd:cd01158    81 VSVhNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 170 TVMAVTDPD-GPRGrnISAFVVHIDDPGFSFGEPERKLGIKGSPTRELIFDNVRIPGDRLVGKVGEGLRTALRTLDHTRV 248
Cdd:cd01158   161 IVFAVTDPSkGYRG--ITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 249 TIGAQAVGIAQGALDYALGYVKERKQFGKAIADFQGIQFMLADMAMKLEAARQMVYVAAAKSERDDaDLSFYGAAAKCFA 328
Cdd:cd01158   239 GIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGE-PFIKEAAMAKLFA 317

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1605303532 329 SDVAMHITTDAVQLLGGYGYTRDYPVERMMRDAKITQIYEGTNQIQRVVMARQLLK 384
Cdd:cd01158   318 SEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLLK 373
 
Name Accession Description Interval E-value
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
 11-384 0e+00

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: 532.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532  11 EEHEALREAIRSVAEDKIAPHAADVDEQSRFPQEAYEALRASDFHAPHVAEEYGGVGADALATCIVIEEIARVCASSSLI 90
Cdd:cd01158     1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532  91 PAV-NKLGSMPLILSGSDEVKQRYLPELASGEAMFSYGLSEREAGSDTASMRTRAVRDGDDWILNGQKSWITNAGISKYY 169
Cdd:cd01158    81 VSVhNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 170 TVMAVTDPD-GPRGrnISAFVVHIDDPGFSFGEPERKLGIKGSPTRELIFDNVRIPGDRLVGKVGEGLRTALRTLDHTRV 248
Cdd:cd01158   161 IVFAVTDPSkGYRG--ITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 249 TIGAQAVGIAQGALDYALGYVKERKQFGKAIADFQGIQFMLADMAMKLEAARQMVYVAAAKSERDDaDLSFYGAAAKCFA 328
Cdd:cd01158   239 GIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGE-PFIKEAAMAKLFA 317

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1605303532 329 SDVAMHITTDAVQLLGGYGYTRDYPVERMMRDAKITQIYEGTNQIQRVVMARQLLK 384
Cdd:cd01158   318 SEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLLK 373
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 3-385 1.13e-173

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: 488.97  E-value: 1.13e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532   3 DFDLyrpTEEHEALREAIRSVAEDKIAPHAADVDEQSRFPQEAYEALRASDFHAPHVAEEYGGVGADALATCIVIEEIAR 82
Cdd:COG1960     2 DFEL---TEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELAR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532  83 VCASSSLIPAVNKLGSMPLILSGSDEVKQRYLPELASGEAMFSYGLSEREAGSDTASMRTRAVRDGDDWILNGQKSWITN 162
Cdd:COG1960    79 ADASLALPVGVHNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITN 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 163 AGISKYYTVMAVTDPDgPRGRNISAFVVHIDDPGFSFGEPERKLGIKGSPTRELIFDNVRIPGDRLVGKVGEGLRTALRT 242
Cdd:COG1960   159 APVADVILVLARTDPA-AGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMST 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 243 LDHTRVTIGAQAVGIAQGALDYALGYVKERKQFGKAIADFQGIQFMLADMAMKLEAARQMVYVAAAKSERDDaDLSFYGA 322
Cdd:COG1960   238 LNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGE-DAALEAA 316

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1605303532 323 AAKCFASDVAMHITTDAVQLLGGYGYTRDYPVERMMRDAKITQIYEGTNQIQRVVMARQLLKK 385
Cdd:COG1960   317 MAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGR 379
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 11-385 3.23e-87

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 269.82  E-value: 3.23e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532  11 EEHEALREAIRSVAEDKIAPHAADVDEQSRFPQEAYEALRASDF--HAPHVAEEYGGVGADALATCIVIEEIARVCASSS 88
Cdd:PLN02519   28 DTQLQFKESVQQFAQENIAPHAAAIDATNSFPKDVNLWKLMGDFnlHGITAPEEYGGLGLGYLYHCIAMEEISRASGSVG 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532  89 L-IPAVNKLGSMPLILSGSDEVKQRYLPELASGEAMFSYGLSEREAGSDTASMRTRAVRDGDDWILNGQKSWITNAGISK 167
Cdd:PLN02519  108 LsYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCTNGPVAQ 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 168 YYTVMAVTDPD-GPRGrnISAFVVHIDDPGFSFGEPERKLGIKGSPTRELIFDNVRIPGDRLVGKVGEGLRTALRTLDHT 246
Cdd:PLN02519  188 TLVVYAKTDVAaGSKG--ITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSGLDLE 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 247 RVTIGAQAVGIAQGALDYALGYVKERKQFGKAIADFQGIQFMLADMAMKLEAARQMVYVAAAKSERDDADLSfYGAAAKC 326
Cdd:PLN02519  266 RLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRK-DCAGVIL 344

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1605303532 327 FASDVAMHITTDAVQLLGGYGYTRDYPVERMMRDAKITQIYEGTNQIQRVVMARQLLKK 385
Cdd:PLN02519  345 CAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRELFKE 403
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 233-382 4.55e-51

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: 167.82  E-value: 4.55e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 233 GEGLRTALRTLDHTRVTIGAQAVGIAQGALDYALGYVKERKQFGKAIADFQGIQFMLADMAMKLEAARQMVYVAAAKSER 312
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 313 DDADlSFYGAAAKCFASDVAMHITTDAVQLLGGYGYTRDYPVERMMRDAKITQIYEGTNQIQRVVMARQL 382
Cdd:pfam00441  81 GGPD-GAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
 
Name Accession Description Interval E-value
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
 11-384 0e+00

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: 532.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532  11 EEHEALREAIRSVAEDKIAPHAADVDEQSRFPQEAYEALRASDFHAPHVAEEYGGVGADALATCIVIEEIARVCASSSLI 90
Cdd:cd01158     1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532  91 PAV-NKLGSMPLILSGSDEVKQRYLPELASGEAMFSYGLSEREAGSDTASMRTRAVRDGDDWILNGQKSWITNAGISKYY 169
Cdd:cd01158    81 VSVhNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 170 TVMAVTDPD-GPRGrnISAFVVHIDDPGFSFGEPERKLGIKGSPTRELIFDNVRIPGDRLVGKVGEGLRTALRTLDHTRV 248
Cdd:cd01158   161 IVFAVTDPSkGYRG--ITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 249 TIGAQAVGIAQGALDYALGYVKERKQFGKAIADFQGIQFMLADMAMKLEAARQMVYVAAAKSERDDaDLSFYGAAAKCFA 328
Cdd:cd01158   239 GIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGE-PFIKEAAMAKLFA 317

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1605303532 329 SDVAMHITTDAVQLLGGYGYTRDYPVERMMRDAKITQIYEGTNQIQRVVMARQLLK 384
Cdd:cd01158   318 SEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLLK 373
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 3-385 1.13e-173

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: 488.97  E-value: 1.13e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532   3 DFDLyrpTEEHEALREAIRSVAEDKIAPHAADVDEQSRFPQEAYEALRASDFHAPHVAEEYGGVGADALATCIVIEEIAR 82
Cdd:COG1960     2 DFEL---TEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELAR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532  83 VCASSSLIPAVNKLGSMPLILSGSDEVKQRYLPELASGEAMFSYGLSEREAGSDTASMRTRAVRDGDDWILNGQKSWITN 162
Cdd:COG1960    79 ADASLALPVGVHNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITN 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 163 AGISKYYTVMAVTDPDgPRGRNISAFVVHIDDPGFSFGEPERKLGIKGSPTRELIFDNVRIPGDRLVGKVGEGLRTALRT 242
Cdd:COG1960   159 APVADVILVLARTDPA-AGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMST 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 243 LDHTRVTIGAQAVGIAQGALDYALGYVKERKQFGKAIADFQGIQFMLADMAMKLEAARQMVYVAAAKSERDDaDLSFYGA 322
Cdd:COG1960   238 LNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGE-DAALEAA 316

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1605303532 323 AAKCFASDVAMHITTDAVQLLGGYGYTRDYPVERMMRDAKITQIYEGTNQIQRVVMARQLLKK 385
Cdd:COG1960   317 MAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGR 379
ACAD cd00567
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
 11-380 3.85e-130

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: 376.24  E-value: 3.85e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532  11 EEHEALREAIRSVAEDKIAPHAADVDEQSRFPQEAYEALRasdfhaphvaeeyggvgadalatcivieeiarvcasssli 90
Cdd:cd00567     1 EEQRELRDSAREFAAEELEPYARERRETPEEPWELLAELG---------------------------------------- 40

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532  91 pavNKLGSMPLILSGSDEVKQRYLPELASGEAMFSYGLSEREAGSDTASMRTRAVRDGDDWILNGQKSWITNAGISKYYT 170
Cdd:cd00567    41 ---LLLGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFI 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 171 VMAVTDPDGPRGRNISAFVVHIDDPGFSFGEPERKLGIKGSPTRELIFDNVRIPGDRLVGKVGEGLRTALRTLDHTRVTI 250
Cdd:cd00567   118 VLARTDEEGPGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLLL 197

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 251 GAQAVGIAQGALDYALGYVKERKQFGKAIADFQGIQFMLADMAMKLEAARQMVYVAAAKSERDDADLSFYGAAAKCFASD 330
Cdd:cd00567   198 AAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEARLEAAMAKLFATE 277

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1605303532 331 VAMHITTDAVQLLGGYGYTRDYPVERMMRDAKITQIYEGTNQIQRVVMAR 380
Cdd:cd00567   278 AAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
IBD cd01162
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ...
 10-385 1.26e-125

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: 366.77  E-value: 1.26e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532  10 TEEHEALREAIRSVAEDKIAPHAADVDEQSRFPQEAYEALRASDFHAPHVAEEYGGVGADALATCIVIEEIARVCASSSL 89
Cdd:cd01162     2 NEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTAA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532  90 IPAVNKLGSMPLILSGSDEVKQRYLPELASGEAMFSYGLSEREAGSDTASMRTRAVRDGDDWILNGQKSWITNAGISKYY 169
Cdd:cd01162    82 YISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSDVY 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 170 TVMAVTDPDGPRGrnISAFVVHIDDPGFSFGEPERKLGIKGSPTRELIFDNVRIPGDRLVGKVGEGLRTALRTLDHTRVT 249
Cdd:cd01162   162 VVMARTGGEGPKG--ISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRLN 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 250 IGAQAVGIAQGALDYALGYVKERKQFGKAIADFQGIQFMLADMAMKLEAARQMVYVAAAKSERDDADLSFYGAAAKCFAS 329
Cdd:cd01162   240 IASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPDAVKLCAMAKRFAT 319

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1605303532 330 DVAMHITTDAVQLLGGYGYTRDYPVERMMRDAKITQIYEGTNQIQRVVMARQLLKK 385
Cdd:cd01162   320 DECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLTR 375
IVD cd01156
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ...
 10-384 1.74e-117

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: 345.94  E-value: 1.74e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532  10 TEEHEALREAIRSVAEDKIAPHAADVDEQSRFPQEAYEALRASDFHAPHVAEEYGGVGADALATCIVIEEIARVCASSSL 89
Cdd:cd01156     3 DDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVAL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532  90 -IPAVNKLGSMPLILSGSDEVKQRYLPELASGEAMFSYGLSEREAGSDTASMRTRAVRDGDDWILNGQKSWITNAGISKY 168
Cdd:cd01156    83 sYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPDADT 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 169 YTVMAVTDPDgPRGRNISAFVVHIDDPGFSFGEPERKLGIKGSPTRELIFDNVRIPGDRLVGKVGEGLRTALRTLDHTRV 248
Cdd:cd01156   163 LVVYAKTDPS-AGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGLDYERL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 249 TIGAQAVGIAQGALDYALGYVKERKQFGKAIADFQGIQFMLADMAMKLEAARQMVYVAAAKSERDDADlSFYGAAAKCFA 328
Cdd:cd01156   242 VLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMD-PKDAAGVILYA 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1605303532 329 SDVAMHITTDAVQLLGGYGYTRDYPVERMMRDAKITQIYEGTNQIQRVVMARQLLK 384
Cdd:cd01156   321 AEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGRELFK 376
MCAD cd01157
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ...
 10-385 9.39e-117

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: 344.18  E-value: 9.39e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532  10 TEEHEALREAIRSVAEDKIAPHAADVDEQSRFPQEAYEALRASDFHAPHVAEEYGGVGADALATCIVIEEIARVCASSSL 89
Cdd:cd01157     2 TEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532  90 IPAVNKLGSMPLILSGSDEVKQRYLPELASGEAMFSYGLSEREAGSDTASMRTRAVRDGDDWILNGQKSWITNAGISKYY 169
Cdd:cd01157    82 AIEANSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWY 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 170 TVMAVTDPD--GPRGRNISAFVVHIDDPGFSFGEPERKLGIKGSPTRELIFDNVRIPGDRLVGKVGEGLRTALRTLDHTR 247
Cdd:cd01157   162 FLLARSDPDpkCPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDKTR 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 248 VTIGAQAVGIAQGALDYALGYVKERKQFGKAIADFQGIQFMLADMAMKLEAARqMVYVAAAKSERDDADLSFYGAAAKCF 327
Cdd:cd01157   242 PPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELAR-LAYQRAAWEVDSGRRNTYYASIAKAF 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1605303532 328 ASDVAMHITTDAVQLLGGYGYTRDYPVERMMRDAKITQIYEGTNQIQRVVMARQLLKK 385
Cdd:cd01157   321 AADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHLGK 378
VLCAD cd01161
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ...
 10-385 5.68e-104

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: 312.87  E-value: 5.68e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532  10 TEEHEALREAIRSVAEDKIAPhaADVDEQSRFPQEAYEALRASDFHAPHVAEEYGGVGADALATCIVIEEIARVCASSSL 89
Cdd:cd01161    28 TEELNMLVGPVEKFFEEVNDP--AKNDQLEKIPRKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEIVGMDLGFSVT 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532  90 IPAVNKLGSMPLILSGSDEVKQRYLPELASGEAMFSYGLSEREAGSDTASMRTRAVR--DGDDWILNGQKSWITNAGISK 167
Cdd:cd01161   106 LGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLseDGKHYVLNGSKIWITNGGIAD 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 168 YYTVMA---VTDPDGPRGRNISAFVVHIDDPGFSFGEPERKLGIKGSPTRELIFDNVRIPGDRLVGKVGEGLRTALRTLD 244
Cdd:cd01161   186 IFTVFAkteVKDATGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGDGFKVAMNILN 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 245 HTRVTIGAQAVGIAQGALDYALGYVKERKQFGKAIADFQGIQFMLADMAMKLEAARQMVYVAAAKSERD-DADLSFYGAA 323
Cdd:cd01161   266 NGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDRGlKAEYQIEAAI 345

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1605303532 324 AKCFASDVAMHITTDAVQLLGGYGYTRDYPVERMMRDAKITQIYEGTNQIQRVVMARQLLKK 385
Cdd:cd01161   346 SKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIALTGLQH 407
LCAD cd01160
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ...
 11-383 3.93e-103

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: 309.43  E-value: 3.93e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532  11 EEHEALREAIRSVAEDKIAPHAADVDEQSRFPQEAYEALRASDFHAPHVAEEYGGVGADALATCIVIEEIARVCASSSLI 90
Cdd:cd01160     1 EEHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARAGGSGPGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532  91 PAVNKLGSMPLILSGSDEVKQRYLPELASGEAMFSYGLSEREAGSDTASMRTRAVRDGDDWILNGQKSWITNAGISKYYT 170
Cdd:cd01160    81 SLHTDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADVVI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 171 VMAVTDPDGPRGRNISAFVVHIDDPGFSFGEPERKLGIKGSPTRELIFDNVRIPGDRLVGKVGEGLRTALRTLDHTRVTI 250
Cdd:cd01160   161 VVARTGGEARGAGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLLI 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 251 GAQAVGIAQGALDYALGYVKERKQFGKAIADFQGIQFMLADMAMKLEAARQMVYVAAAKSERDDADLSfYGAAAKCFASD 330
Cdd:cd01160   241 AAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVA-EASMAKYWATE 319

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1605303532 331 VAMHITTDAVQLLGGYGYTRDYPVERMMRDAKITQIYEGTNQIQRVVMARQLL 383
Cdd:cd01160   320 LQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQMV 372
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 11-385 3.23e-87

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 269.82  E-value: 3.23e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532  11 EEHEALREAIRSVAEDKIAPHAADVDEQSRFPQEAYEALRASDF--HAPHVAEEYGGVGADALATCIVIEEIARVCASSS 88
Cdd:PLN02519   28 DTQLQFKESVQQFAQENIAPHAAAIDATNSFPKDVNLWKLMGDFnlHGITAPEEYGGLGLGYLYHCIAMEEISRASGSVG 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532  89 L-IPAVNKLGSMPLILSGSDEVKQRYLPELASGEAMFSYGLSEREAGSDTASMRTRAVRDGDDWILNGQKSWITNAGISK 167
Cdd:PLN02519  108 LsYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCTNGPVAQ 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 168 YYTVMAVTDPD-GPRGrnISAFVVHIDDPGFSFGEPERKLGIKGSPTRELIFDNVRIPGDRLVGKVGEGLRTALRTLDHT 246
Cdd:PLN02519  188 TLVVYAKTDVAaGSKG--ITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSGLDLE 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 247 RVTIGAQAVGIAQGALDYALGYVKERKQFGKAIADFQGIQFMLADMAMKLEAARQMVYVAAAKSERDDADLSfYGAAAKC 326
Cdd:PLN02519  266 RLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRK-DCAGVIL 344

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1605303532 327 FASDVAMHITTDAVQLLGGYGYTRDYPVERMMRDAKITQIYEGTNQIQRVVMARQLLKK 385
Cdd:PLN02519  345 CAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRELFKE 403
PRK12341 PRK12341
acyl-CoA dehydrogenase;
7-385 4.39e-77

acyl-CoA dehydrogenase;


Pssm-ID: 183454 [Multi-domain]  Cd Length: 381  Bit Score: 242.71  E-value: 4.39e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532   7 YRPTEEHEALREAIRSV-AEDKIAPHAADVDEQSRFPQEAYEALRASDFHAPHVAEEYGGVGADALATCIVIEEIARVCA 85
Cdd:PRK12341    3 FSLTEEQELLLASIRELiTRNFPEEYFRTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEVSKCGA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532  86 SSSLIPAVNKLGSMplILSGSDE-VKQRYLPELASGEAMFSYGLSEREAGSDTASMRTRAVRDGDDWILNGQKSWITNAG 164
Cdd:PRK12341   83 PAFLITNGQCIHSM--RRFGSAEqLRKTAESTLETGDPAYALALTEPGAGSDNNSATTTYTRKNGKVYLNGQKTFITGAK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 165 ISKYYTVMAvTDPDGPRGRN-ISAFVVHIDDPGFSFgEPERKLGIKGSPTRELIFDNVRIPGDRLVGKVGEGLRTALRTL 243
Cdd:PRK12341  161 EYPYMLVLA-RDPQPKDPKKaFTLWWVDSSKPGIKI-NPLHKIGWHMLSTCEVYLDNVEVEESDLVGEEGMGFLNVMYNF 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 244 DHTRVTIGAQAVGIAQGALDYALGYVKERKQFGKAIADFQGIQFMLADMAMKLEAARQMVYVAAAKSErDDADLSFYGAA 323
Cdd:PRK12341  239 EMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQAD-NGQSLRTSAAL 317

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1605303532 324 AKCFASDVAMHITTDAVQLLGGYGYTRDYPVERMMRDAKITQIYEGTNQIQRVVMARQLLKK 385
Cdd:PRK12341  318 AKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQILKD 379
GCD cd01151
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ...
 10-380 1.31e-76

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: 241.88  E-value: 1.31e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532  10 TEEHEALREAIRSVAEDKIAPHAADVDEQSRFPQEAYEALRASDFHAPHVaEEYGGVGADALATCIVIEEIARVCAS-SS 88
Cdd:cd01151    14 TEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGATI-KGYGCAGLSSVAYGLIAREVERVDSGyRS 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532  89 LIPAVNKLGSMPLILSGSDEVKQRYLPELASGEAMFSYGLSEREAGSDTASMRTRAVRDGDDWILNGQKSWITNAGISKY 168
Cdd:cd01151    93 FMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSPIADV 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 169 YTVMAVTDPDGprgrNISAFVVHIDDPGFSFGEPERKLGIKGSPTRELIFDNVRIPGDRLVGKVgEGLRTALRTLDHTRV 248
Cdd:cd01151   173 FVVWARNDETG----KIRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPGA-EGLRGPFKCLNNARY 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 249 TIGAQAVGIAQGALDYALGYVKERKQFGKAIADFQGIQFMLADMAMKLEAARQMVYVAAAKSERDDAD---LSFygaaAK 325
Cdd:cd01151   248 GIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKATpeqISL----LK 323

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1605303532 326 CFASDVAMHITTDAVQLLGGYGYTRDYPVERMMRDAKITQIYEGTNQIQRVVMAR 380
Cdd:cd01151   324 RNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGR 378
PTZ00461 PTZ00461
isovaleryl-CoA dehydrogenase; Provisional
 5-384 1.78e-72

isovaleryl-CoA dehydrogenase; Provisional


Pssm-ID: 185640 [Multi-domain]  Cd Length: 410  Bit Score: 231.75  E-value: 1.78e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532   5 DLYRPTEEHEALREAIRSVAEDKIAPHAADVDEQSRFPQEAYEALRASDFHAPHVAEEYGGVGADALATCIVIEEIARV- 83
Cdd:PTZ00461   33 DLYNPTPEHAALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYd 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532  84 ---C----ASSSLIpaVNKLgsmplILSGSDEVKQRYLPELASGEAMFSYGLSEREAGSDTASMRTRAVRDGD-DWILNG 155
Cdd:PTZ00461  113 pgfClaylAHSMLF--VNNF-----YYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNgNYVLNG 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 156 QKSWITNAGISKYYTVMAVTDpdgprGRnISAFVVHIDDPGFSFGEPERKLGIKGSPTRELIFDNVRIPGDRLVGKVGEG 235
Cdd:PTZ00461  186 SKIWITNGTVADVFLIYAKVD-----GK-ITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKG 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 236 LRTALRTLDHTRVTIGAQAVGIAQGALDYALGYVKERKQFGKAIADFQGIQFMLADMAMKLEAARQMVYvAAAKSERDDA 315
Cdd:PTZ00461  260 MVGMMRNLELERVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVY-SVSHNVHPGN 338

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1605303532 316 DLSFYGAAAKCFASDVAMHITTDAVQLLGGYGYTRDYPVERMMRDAKITQIYEGTNQIQRVVMARQLLK 384
Cdd:PTZ00461  339 KNRLGSDAAKLFATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIEAHHKNITKDLLK 407
ACAD_fadE6_17_26 cd01152
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ...
 11-383 1.98e-68

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: 220.30  E-value: 1.98e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532  11 EEHEALREAIRS-VAEDKIAPHAADVDEQSRFPQEAYE----ALRASDFHAPHVAEEYGGVGADALATCIVIEEIARVCA 85
Cdd:cd01152     1 PSEEAFRAEVRAwLAAHLPPELREESALGYREGREDRRrwqrALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532  86 SSSlipaVNKLGSM---PLILS-GSDEVKQRYLPELASGEAMFSYGLSEREAGSDTASMRTRAVRDGDDWILNGQKSWIT 161
Cdd:cd01152    81 PVP----FNQIGIDlagPTILAyGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTS 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 162 NAGISKYYTVMAVTDPDGPRGRNISAFVVHIDDPGFSFgEPERKlgIKGSP-TRELIFDNVRIPGDRLVGKVGEGLRTAL 240
Cdd:cd01152   157 GAHYADWAWLLVRTDPEAPKHRGISILLVDMDSPGVTV-RPIRS--INGGEfFNEVFLDDVRVPDANRVGEVNDGWKVAM 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 241 RTLDHTRVTIGAQAVgIAQGALDYALGYVKERkqfGKAIADFQGIQFMLADMAMKLEAARQMVY-VAAAKSERDDADLSf 319
Cdd:cd01152   234 TTLNFERVSIGGSAA-TFFELLLARLLLLTRD---GRPLIDDPLVRQRLARLEAEAEALRLLVFrLASALAAGKPPGAE- 308

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1605303532 320 yGAAAKCFASDVAMHITTDAVQLLGGYGYTRDYP--------VERMMRDAKITQIYEGTNQIQRVVMARQLL 383
Cdd:cd01152   309 -ASIAKLFGSELAQELAELALELLGTAALLRDPApgaelagrWEADYLRSRATTIYGGTSEIQRNIIAERLL 379
ACAD_fadE5 cd01153
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ...
 15-374 1.76e-67

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: 218.80  E-value: 1.76e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532  15 ALREAIRsVAEDKIAPHAADVDEQ--------SRFPQ---EAYEALRASDFHAPHVAEEYGGVGAdALATCIVIEEIARV 83
Cdd:cd01153     1 VLEEVAR-LAENVLAPLNADGDREgpvfddgrVVVPPpfkEALDAFAEAGWMALGVPEEYGGQGL-PITVYSALAEIFSR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532  84 CASSSLIPAVNKLGSMPLILSGSDEVKQRYLPELASGEAMFSYGLSEREAGSDTASMRTRAVRDGD-DWILNGQKSWITN 162
Cdd:cd01153    79 GDAPLMYASGTQGAAATLLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRFISA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 163 A----GISKYYTVMAVTDPDGPRGRNISAFVV--HIDDP---GFSFGEPERKLGIKGSPTRELIFDNVRIPgdrLVGKVG 233
Cdd:cd01153   159 GehdmSENIVHLVLARSEGAPPGVKGLSLFLVpkFLDDGernGVTVARIEEKMGLHGSPTCELVFDNAKGE---LIGEEG 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 234 EGLRTALRTLDHTRVTIGAQAVGIAQGALDYALGYVKERKQFGKAIADFQG--------IQFMLADMAMKLEAARQMV-Y 304
Cdd:cd01153   236 MGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLIKAAPAvtiihhpdVRRSLMTQKAYAEGSRALDlY 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 305 VA--------AAKSERDDADLSFYGAA----AKCFASDVAMHITTDAVQLLGGYGYTRDYPVERMMRDAKITQIYEGTNQ 372
Cdd:cd01153   316 TAtvqdlaerKATEGEDRKALSALADLltpvVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTG 395


                  ..
gi 1605303532 373 IQ 374
Cdd:cd01153   396 IQ 397
PRK03354 PRK03354
crotonobetainyl-CoA dehydrogenase; Validated
 3-385 1.70e-56

crotonobetainyl-CoA dehydrogenase; Validated


Pssm-ID: 179566 [Multi-domain]  Cd Length: 380  Bit Score: 189.27  E-value: 1.70e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532   3 DFDLyrpTEEHEALREAIRS-VAEDKIAPHAADVDEQSRFPQEAYEALRASDFHAPHVAEEYGGVGADALATCIVIEEIA 81
Cdd:PRK03354    2 DFNL---NDEQELFVAGIRElMASENWEAYFAECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532  82 RVCASSSLIPAVnKLGSMPLILSGSDEVKQRYLPELASGEAMFSYGLSEREAGSDTASMRTRAVRDGDDWILNGQKSWIT 161
Cdd:PRK03354   79 RLGAPTYVLYQL-PGGFNTFLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFIT 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 162 NAGISKYYTVMAvTDPDGPRGRNISAFVVHIDDPGFSFgEPERKLGIKGSPTRELIFDNVRIPGDRLVGKVGEGLRTALR 241
Cdd:PRK03354  158 SSAYTPYIVVMA-RDGASPDKPVYTEWFVDMSKPGIKV-TKLEKLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKE 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 242 TLDHTRVTIGAQAVGIAQGALDYALGYVKERKQFGKAIADFQGIQFMLADMAMKLEAARQMVYVAAAKSERDDADlsfYG 321
Cdd:PRK03354  236 EFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTIT---SG 312

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1605303532 322 AAAKC--FASDVAMHITTDAVQLLGGYGYTRDYPVERMMRDAKITQIYEGTNQIQRVVMARQLLKK 385
Cdd:PRK03354  313 DAAMCkyFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAVLKQ 378
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 233-382 4.55e-51

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: 167.82  E-value: 4.55e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 233 GEGLRTALRTLDHTRVTIGAQAVGIAQGALDYALGYVKERKQFGKAIADFQGIQFMLADMAMKLEAARQMVYVAAAKSER 312
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 313 DDADlSFYGAAAKCFASDVAMHITTDAVQLLGGYGYTRDYPVERMMRDAKITQIYEGTNQIQRVVMARQL 382
Cdd:pfam00441  81 GGPD-GAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
PLN02526 PLN02526
acyl-coenzyme A oxidase
 10-382 6.65e-50

acyl-coenzyme A oxidase


Pssm-ID: 178141 [Multi-domain]  Cd Length: 412  Bit Score: 173.11  E-value: 6.65e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532  10 TEEHEALREAIRSVAEDKIAPHAADVDEQSRFPQEAYEALRASDFhAPHVAEEYGGVGADALATCIVIEEIARVCAS-SS 88
Cdd:PLN02526   30 TPEEQALRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLGSLGI-AGGTIKGYGCPGLSITASAIATAEVARVDAScST 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532  89 LIPAVNKLGSMPLILSGSDEVKQRYLPELASGEAMFSYGLSEREAGSDTASMRTRAVRDGDDWILNGQKSWITNAGISKY 168
Cdd:PLN02526  109 FILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIGNSTFADV 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 169 YTVMAvtdpdgprgRN-----ISAFVVHIDDPGFSFGEPERKLGIKGSPTRELIFDNVRIPG-DRLVGKvgEGLRTALRT 242
Cdd:PLN02526  189 LVIFA---------RNtttnqINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDeDRLPGV--NSFQDTNKV 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 243 LDHTRVTIGAQAVGIAQGALDYALGYVKERKQFGKAIADFQGIQFMLADM-----AMKLEAARQMVYVAAAKSERDDADL 317
Cdd:PLN02526  258 LAVSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMlgniqAMFLVGWRLCKLYESGKMTPGHASL 337

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1605303532 318 sfygaaAKCFASDVAMHITTDAVQLLGGYGYTRDYPVERMMRDAKITQIYEGTNQIQRVVMARQL 382
Cdd:PLN02526  338 ------GKAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGREI 396
AidB cd01154
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ...
 13-384 2.05e-41

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: 150.60  E-value: 2.05e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532  13 HEALREAIRSVAEDKIAPHAADVDEQSRfpqeaYEALRASDFHaphVAEEYGGVGadalatCIVIEEIARVCAssslipa 92
Cdd:cd01154    64 HPAWHALMRRLIEEGVINIEDGPAGEGR-----RHVHFAAGYL---LSDAAAGLL------CPLTMTDAAVYA------- 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532  93 vnklgsmpLILSGSDEVKQRYLPELASG--EAMFS-YGLSEREAGSDTASMRTRAVRDGDD-WILNGQKsWITNAGISKY 168
Cdd:cd01154   123 --------LRKYGPEELKQYLPGLLSDRykTGLLGgTWMTEKQGGSDLGANETTAERSGGGvYRLNGHK-WFASAPLADA 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 169 YTVMA--VTDPDGPRGrnISAFVVHIDDP-----GFSFGEPERKLGIKGSPTRELIFDNVRipgDRLVGKVGEGLRTALR 241
Cdd:cd01154   194 ALVLArpEGAPAGARG--LSLFLVPRLLEdgtrnGYRIRRLKDKLGTRSVATGEVEFDDAE---AYLIGDEGKGIYYILE 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 242 TLDHTRVTIGAQAVGIAQGALDYALGYVKERKQFGKAIADFQGIQFMLADMAMKLEAARQMVYVAAA---KSERDDADLS 318
Cdd:cd01154   269 MLNISRLDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARafdRAAADKPVEA 348

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 319 FYG----AAAKCFASDVAMHITTDAVQLLGGYGYTRDYPVERMMRDAKITQIYEGTNQIQRVVMARQLLK 384
Cdd:cd01154   349 HMArlatPVAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQALDVLRVLVK 418
Acyl-CoA_dh_N pfam02771
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ...
 10-121 2.74e-41

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: 141.06  E-value: 2.74e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532  10 TEEHEALREAIRSVAEDKIAPHAADVDEQSRFPQEAYEALRASDFHAPHVAEEYGGVGADALATCIVIEEIARVCASSSL 89
Cdd:pfam02771   1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVAL 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1605303532  90 IPAV-NKLGSMPLILSGSDEVKQRYLPELASGE 121
Cdd:pfam02771  81 ALSVhSSLGAPPILRFGTEEQKERYLPKLASGE 113
PTZ00456 PTZ00456
acyl-CoA dehydrogenase; Provisional
 43-384 2.57e-37

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185635 [Multi-domain]  Cd Length: 622  Bit Score: 142.31  E-value: 2.57e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532  43 QEAYEALRASDFHAPHVAEEYGGVGADALATCIVIEEIARVCASSSLIPAVNkLGSM-PLILSGSDEVKQRYLPELASGE 121
Cdd:PTZ00456  102 KEAYQALKAGGWTGISEPEEYGGQALPLSVGFITRELMATANWGFSMYPGLS-IGAAnTLMAWGSEEQKEQYLTKLVSGE 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 122 AMFSYGLSEREAGSDTASMRTRAVRDGD-DWILNGQKSWITnAGISKY-----YTVMAVTDPDGPRGRNISAFVV--HID 193
Cdd:PTZ00456  181 WSGTMCLTEPQCGTDLGQVKTKAEPSADgSYKITGTKIFIS-AGDHDLtenivHIVLARLPNSLPTTKGLSLFLVprHVV 259

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 194 DPGFSF--------GEPERKLGIKGSPTRELIFDNVRipgDRLVGKVGEGLRTALRTLDHTRVTIGAQAVGIAQGALDYA 265
Cdd:PTZ00456  260 KPDGSLetaknvkcIGLEKKMGIKGSSTCQLSFENSV---GYLIGEPNAGMKQMFTFMNTARVGTALEGVCHAELAFQNA 336

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 266 LGYVKERKQ----------------------------FGKAIAdfQGIQFMLADMAMKLEaarqmvYVAAAK--SERD-- 313
Cdd:PTZ00456  337 LRYARERRSmralsgtkepekpadriichanvrqnilFAKAVA--EGGRALLLDVGRLLD------IHAAAKdaATREal 408

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1605303532 314 DADLSFYGAAAKCFASDVAMHITTDAVQLLGGYGYTRDYPVERMMRDAKITQIYEGTNQIQRV-VMARQLLK 384
Cdd:PTZ00456  409 DHEIGFYTPIAKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQALdFIGRKVLS 480
ACAD_FadE2 cd01155
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ...
 97-384 3.11e-36

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: 135.98  E-value: 3.11e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532  97 GSMP-LILSGSDEVKQRYLPELASGEAMFSYGLSERE-AGSDTASMRTRAVRDGDDWILNGQKSWITNAG--ISKYYTVM 172
Cdd:cd01155    99 GNMEvLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERDGDDYVINGRKWWSSGAGdpRCKIAIVM 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 173 AVTDPDG-PRGRNISAFVVHIDDPGFSFGEPERKLGIKGSPT--RELIFDNVRIPGDRLVGKVGEGLRTALRTLDHTRVT 249
Cdd:cd01155   179 GRTDPDGaPRHRQQSMILVPMDTPGVTIIRPLSVFGYDDAPHghAEITFDNVRVPASNLILGEGRGFEIAQGRLGPGRIH 258

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 250 IGAQAVGIAQGALDYALGYVKERKQFGKAIADFQGIQFMLADMAMKLEAARQMVYVAA----------AKSERddadlsf 319
Cdd:cd01155   259 HCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAhmidtvgnkaARKEI------- 331

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1605303532 320 ygAAAKCFASDVAMHITTDAVQLLGGYGYTRDYPVERMMRDAKITQIYEGTNQIQRVVMARQLLK 384
Cdd:cd01155   332 --AMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIARMELK 394
Acyl-CoA_dh_M pfam02770
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ...
 125-219 1.07e-31

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: 115.46  E-value: 1.07e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 125 SYGLSEREAGSDTASMRTRAV-RDGDDWILNGQKSWITNAGISKYYTVMAVTDPDGPRGRnISAFVVHIDDPGFSFGEPE 203
Cdd:pfam02770   1 AFALTEPGAGSDVASLKTTAAdGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDDRHGG-ISLFLVPKDAPGVSVRRIE 79

                          90
                  ....*....|....*.
gi 1605303532 204 RKLGIKGSPTRELIFD 219
Cdd:pfam02770  80 TKLGVRGLPTGELVFD 95
DszC cd01163
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ...
 18-362 1.38e-24

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: 103.56  E-value: 1.38e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532  18 EAIRSVAEdKIAPHAADVDEQSRFPQEAYEALRASDFHAPHVAEEYGGVGADALATCIVIEEIARVCASSSLIPAVNKLG 97
Cdd:cd01163     1 ARARPLAA-RIAEGAAERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALRAHFGF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532  98 SMPLILSGSDEVKQRYLPELASGeAMFSYGLSEREaGSDTASMRTRAVRDGDDWILNGQKSWITNAGISKYYTVMAVtDP 177
Cdd:cd01163    80 VEALLLAGPEQFRKRWFGRVLNG-WIFGNAVSERG-SVRPGTFLTATVRDGGGYVLNGKKFYSTGALFSDWVTVSAL-DE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 178 DGPrgrnISAFVVHIDDPGFSFGEPERKLGIKGSPTRELIFDNVRIPGDRLVGKVG----EGLRTALRTLDHTrvtigAQ 253
Cdd:cd01163   157 EGK----LVFAAVPTDRPGITVVDDWDGFGQRLTASGTVTFDNVRVEPDEVLPRPNapdrGTLLTAIYQLVLA-----AV 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 254 AVGIAQGALDYALGYVKERKQ------FGKAIADFQGIQfMLADMAMKLEAARQMVYVAA-----------AKSERDDAD 316
Cdd:cd01163   228 LAGIARAALDDAVAYVRSRTRpwihsgAESARDDPYVQQ-VVGDLAARLHAAEALVLQAAraldaaaaagtALTAEARGE 306

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1605303532 317 LSFYGAAAKCFASDVAMHITTDAVQLLGGYGYTRDYPVERMMRDAK 362
Cdd:cd01163   307 AALAVAAAKVVVTRLALDATSRLFEVGGASATAREHNLDRHWRNAR 352
Acyl-CoA_dh_2 pfam08028
Acyl-CoA dehydrogenase, C-terminal domain;
249-372 2.24e-22

Acyl-CoA dehydrogenase, C-terminal domain;


Pssm-ID: 429790 [Multi-domain]  Cd Length: 133  Bit Score: 91.64  E-value: 2.24e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 249 TIGAQAVGIAQGALDYALGYVKERKQ--FGKAIADFQGIQFMLADMAMKLEAARQMVYVAAAKSERDDADLSFY------ 320
Cdd:pfam08028   1 GIAAAALGAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAARIDAARLLLERAAARIEAAAAAGKPVtpalra 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1605303532 321 -GAAAKCFASDVAMHITTDAVQLLGGYGYTRDYPVERMMRDAKITQIYEGTNQ 372
Cdd:pfam08028  81 eARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
PRK13026 PRK13026
acyl-CoA dehydrogenase; Reviewed
 42-303 2.33e-21

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 237277 [Multi-domain]  Cd Length: 774  Bit Score: 96.18  E-value: 2.33e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532  42 PQEAYEALRASDFHAPHVAEEYGGVGADALATCIVIEEIArvcaSSSLIPAV-----NKLGSMPLILS-GSDEVKQRYLP 115
Cdd:PRK13026  110 PPEVWDYLKKEGFFALIIPKEYGGKGFSAYANSTIVSKIA----TRSVSAAVtvmvpNSLGPGELLTHyGTQEQKDYWLP 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 116 ELASGEAMFSYGLSEREAGSDTASMR-----TRAVRDGDDWI---LNGQKSWITNAGISkyyTVMA----VTDPDG---- 179
Cdd:PRK13026  186 RLADGTEIPCFALTGPEAGSDAGAIPdtgivCRGEFEGEEVLglrLTWDKRYITLAPVA---TVLGlafkLRDPDGllgd 262

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 180 PRGRNISAFVVHIDDPGFSFGEPERKLGIK--GSPTRElifDNVRIPGDRLVG---KVGEGLRTALRTLDHTRvTIGAQA 254
Cdd:PRK13026  263 KKELGITCALIPTDHPGVEIGRRHNPLGMAfmNGTTRG---KDVFIPLDWIIGgpdYAGRGWRMLVECLSAGR-GISLPA 338

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1605303532 255 VGIAQGALDY----ALGYVkeRKQFGKAIADFQGIQFMLADMAMK---LEAARQMV 303
Cdd:PRK13026  339 LGTASGHMATrttgAYAYV--RRQFGMPIGQFEGVQEALARIAGNtylLEAARRLT 392
PLN02876 PLN02876
acyl-CoA dehydrogenase
 97-373 5.53e-20

acyl-CoA dehydrogenase


Pssm-ID: 215473 [Multi-domain]  Cd Length: 822  Bit Score: 91.78  E-value: 5.53e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532  97 GSMPLILS-GSDEVKQRYLPELASGEAMFSYGLSERE-AGSDTASMRTRAVRDGDDWILNGQKSWITNA--GISKYYTVM 172
Cdd:PLN02876  524 GNMEVLLRyGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDATNIECSIRRQGDSYVINGTKWWTSGAmdPRCRVLIVM 603

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 173 AVTDPDGPRGRNISAFVVHIDDPGFSFGEPERKLGIKGSP--TRELIFDNVRIPGDRLVGKVGEGLRTALRTLDHTRVTI 250
Cdd:PLN02876  604 GKTDFNAPKHKQQSMILVDIQTPGVQIKRPLLVFGFDDAPhgHAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHH 683

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 251 GAQAVGIAQGALDYALGYVKERKQFGKAIADFQGIQFMLADMAMKLEAARQMVYVAAAKSERddadlsfYG--------A 322
Cdd:PLN02876  684 CMRLIGAAERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAADQLDR-------LGnkkargiiA 756

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1605303532 323 AAKCFASDVAMHITTDAVQLLGGYGYTRDYPVERMMRDAKITQIYEGTNQI 373
Cdd:PLN02876  757 MAKVAAPNMALKVLDMAMQVHGAAGVSSDTVLAHLWATARTLRIADGPDEV 807
fadE PRK09463
acyl-CoA dehydrogenase; Reviewed
 42-347 1.86e-19

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 236528 [Multi-domain]  Cd Length: 777  Bit Score: 90.26  E-value: 1.86e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532  42 PQEAYEALRASDFHAPHVAEEYGGVGADALATCIVIEEIARVC---ASSSLIPavNKLGSMPLILS-GSDEVKQRYLPEL 117
Cdd:PRK09463  111 PPEVWQFIKEHGFFGMIIPKEYGGLEFSAYAHSRVLQKLASRSgtlAVTVMVP--NSLGPGELLLHyGTDEQKDHYLPRL 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 118 ASGEAMFSYGLSEREAGSDTASMR-----TRAVRDGDDWI---LNGQKSWITNAGISkyyTVMA----VTDPDGPRGRN- 184
Cdd:PRK09463  189 ARGEEIPCFALTSPEAGSDAGSIPdtgvvCKGEWQGEEVLgmrLTWNKRYITLAPIA---TVLGlafkLYDPDGLLGDKe 265

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 185 ---ISAFVVHIDDPGFSFGEPERKLGI--KGSPTRElifDNVRIPGDRLVG---KVGEGLRTALRTLDHTR-VTIGAQAV 255
Cdd:PRK09463  266 dlgITCALIPTDTPGVEIGRRHFPLNVpfQNGPTRG---KDVFIPLDYIIGgpkMAGQGWRMLMECLSVGRgISLPSNST 342

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 256 GIAQGALDYALGYVKERKQFGKAIADFQGIQFMLADMAMK---LEAARQMVYVAAAKSERDdadlSFYGAAAKCFASDVA 332
Cdd:PRK09463  343 GGAKLAALATGAYARIRRQFKLPIGKFEGIEEPLARIAGNaylMDAARTLTTAAVDLGEKP----SVLSAIAKYHLTERG 418

                         330
                  ....*....|....*
gi 1605303532 333 MHITTDAVQLLGGYG 347
Cdd:PRK09463  419 RQVINDAMDIHGGKG 433
NcnH cd01159
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ...
 18-361 1.71e-18

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: 85.86  E-value: 1.71e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532  18 EAIRSVAeDKIAPHAADVDEQSRFPQEAYEALRASDFHAPHVAEEYGGVGADALATCIVIEEIARVCASSSLIPAVnkLG 97
Cdd:cd01159     1 ARAEDLA-PLIRERAPEAERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSAAWVASI--VA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532  98 SMPLILSgsdevkqrYLPELASGEaMFSYGLSEREAGSdTASMRtRAVRDGDDWILNGQKSWITNAGISKYYTVMA-VTD 176
Cdd:cd01159    78 THSRMLA--------AFPPEAQEE-VWGDGPDTLLAGS-YAPGG-RAERVDGGYRVSGTWPFASGCDHADWILVGAiVED 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 177 PDGprGRNISAFVV-----HIDDPGFSfgeperkLGIKGSPTRELIFDNVRIPGDR-LVGKVGEGLRTALRTLDHTRV-- 248
Cdd:cd01159   147 DDG--GPLPRAFVVpraeyEIVDTWHV-------VGLRGTGSNTVVVDDVFVPEHRtLTAGDMMAGDGPGGSTPVYRMpl 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 249 ------TIGAQAVGIAQGALDYALGYVKERKQFGKA---IADFQGIQFMLADMAMKLEAARQMVYVA-------AAKSER 312
Cdd:cd01159   218 rqvfplSFAAVSLGAAEGALAEFLELAGKRVRQYGAavkMAEAPITQLRLAEAAAELDAARAFLERAtrdlwahALAGGP 297

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1605303532 313 DDADLSFYGAAAKCFASDVAMHITTDAVQLLGGYGYTRDYPVERMMRDA 361
Cdd:cd01159   298 IDVEERARIRRDAAYAAKLSAEAVDRLFHAAGGSALYTASPLQRIWRDI 346
PRK11561 PRK11561
isovaleryl CoA dehydrogenase; Provisional
 112-373 2.97e-14

isovaleryl CoA dehydrogenase; Provisional


Pssm-ID: 183199 [Multi-domain]  Cd Length: 538  Bit Score: 74.02  E-value: 2.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 112 RYLPELASGEA----MFSYGLSEREAGSDTASMRTRAVR-DGDDWILNGQKsWITNAGISKYYTVMAVTD---------- 176
Cdd:PRK11561  164 RYDSHLLPGGQkrglLIGMGMTEKQGGSDVLSNTTRAERlADGSYRLVGHK-WFFSVPQSDAHLVLAQAKgglscffvpr 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 177 --PDGPRGrnisafVVHIddpgfsfgepER---KLGIKGSPTRELIFDNVRipgDRLVGKVGEGLRTALRTLDHTRVTIG 251
Cdd:PRK11561  243 flPDGQRN------AIRL----------ERlkdKLGNRSNASSEVEFQDAI---GWLLGEEGEGIRLILKMGGMTRFDCA 303

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 252 AQAVGIAQGALDYALGYVKERKQFGKAIADFQGIQFMLADMAMKLEAARQMVY-VAAAKSERDDADLSFYG----AAAKC 326
Cdd:PRK11561  304 LGSHGLMRRAFSVAIYHAHQRQVFGKPLIEQPLMRQVLSRMALQLEGQTALLFrLARAWDRRADAKEALWArlftPAAKF 383

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1605303532 327 FASDVAMHITTDAVQLLGGYGYTRDYPVERMMRDAKITQIYEGTNQI 373
Cdd:PRK11561  384 VICKRGIPFVAEAMEVLGGIGYCEESELPRLYREMPVNSIWEGSGNI 430
AXO cd01150
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ...
 92-385 6.88e-12

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: 66.97  E-value: 6.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532  92 AVNKLGSMPLILS-GSDEVKQRYLPELASGEAMFSYGLSEREAGSDTASMRTRAVRD--GDDWILN-----GQKSWITNA 163
Cdd:cd01150   103 GLHLGLFGNAIKNlGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATYDplTQEFVINtpdftATKWWPGNL 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 164 GIS-KYYTVMAVTDPDGPRgRNISAFVVHIDD-------PGFSFGEPERKLGIKGSPTRELIFDNVRIPGDRLVGKVGE- 234
Cdd:cd01150   183 GKTaTHAVVFAQLITPGKN-HGLHAFIVPIRDpkthqplPGVTVGDIGPKMGLNGVDNGFLQFRNVRIPRENLLNRFGDv 261

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 235 ---------------GLRTALRTLDHTRVTIGAQAVGIAQGALDYALGYVKERKQFGK-------AIADFQGIQFML--- 289
Cdd:cd01150   262 spdgtyvspfkdpnkRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQFGPkpsdpevQILDYQLQQYRLfpq 341

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 290 --ADMAMKLEAA--RQMVYVAAAKSERDDADLSFYGAAAKCFASDVAMHITTDAVQLL----GGYGYTRDYPVERMMRDA 361
Cdd:cd01150   342 laAAYAFHFAAKslVEMYHEIIKELLQGNSELLAELHALSAGLKAVATWTAAQGIQECreacGGHGYLAMNRLPTLRDDN 421

                         330       340
                  ....*....|....*....|....
gi 1605303532 362 KITQIYEGTNQIQRVVMARQLLKK 385
Cdd:cd01150   422 DPFCTYEGDNTVLLQQTANYLLKK 445
PLN02636 PLN02636
acyl-coenzyme A oxidase
 105-385 2.27e-11

acyl-coenzyme A oxidase


Pssm-ID: 215342 [Multi-domain]  Cd Length: 686  Bit Score: 65.26  E-value: 2.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 105 GSDEVKQRYLPELASGEAMFSYGLSEREAGSDTASMRTRAVRD--GDDWILN-----GQKSWITNAGI-SKYYTVMA--- 173
Cdd:PLN02636  156 GTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFDplTDEFVINtpndgAIKWWIGNAAVhGKFATVFArlk 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 174 --VTDPDGPRGRNISAFVVHIDD-------PGFSFGEPERKLGIKGSPTRELIFDNVRIPGDRLVGKVGEGLR-----TA 239
Cdd:PLN02636  236 lpTHDSKGVSDMGVHAFIVPIRDmkthqvlPGVEIRDCGHKVGLNGVDNGALRFRSVRIPRDNLLNRFGDVSRdgkytSS 315

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 240 LRTLDHT-----------RVTIGAQAVGIAQGALDYALGYVKERKQFGK------AIADFQGIQFMLADMAMKLEAAR-Q 301
Cdd:PLN02636  316 LPTINKRfaatlgelvggRVGLAYGSVGVLKASNTIAIRYSLLRQQFGPpkqpeiSILDYQSQQHKLMPMLASTYAFHfA 395

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 302 MVYVAAAKSE----RDD---ADLSFYGAAAKCFASDVAMHITTDAVQLLGGYGYTRDYPVERMMRDAKITQIYEGTNQIQ 374
Cdd:PLN02636  396 TEYLVERYSEmkktHDDqlvADVHALSAGLKAYITSYTAKALSTCREACGGHGYAAVNRFGSLRNDHDIFQTFEGDNTVL 475

                         330
                  ....*....|.
gi 1605303532 375 RVVMARQLLKK 385
Cdd:PLN02636  476 LQQVAADLLKQ 486
PTZ00457 PTZ00457
acyl-CoA dehydrogenase; Provisional
 34-243 2.89e-08

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185636 [Multi-domain]  Cd Length: 520  Bit Score: 55.27  E-value: 2.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532  34 DVDEQSRFpQEAYEALRASD-----FHAPHVAEEYGGVGADALATCIVIEEIARVCASSSLiPAVNKLGSMPLILS--GS 106
Cdd:PTZ00457   41 DGDEAENL-QSLLEQIRSNDkilgnLYGARIATEYGGLGLGHTAHALIYEEVGTNCDSKLL-STIQHSGFCTYLLStvGS 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 107 DEVKQRYLPELASGEAMFSYGLSErEAGSDTASMRTRAV-RDGDDWILNGQKSWITNAGISKYY----TVMAVTDPDGPR 181
Cdd:PTZ00457  119 KELKGKYLTAMSDGTIMMGWATEE-GCGSDISMNTTKASlTDDGSYVLTGQKRCEFAASATHFLvlakTLTQTAAEEGAT 197

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1605303532 182 --GRNiSAFVVHIDDPGFSfgeperklgIKGSptrELIFDNVriPGDRLVGKVGEGLRTALRTL 243
Cdd:PTZ00457  198 evSRN-SFFICAKDAKGVS---------VNGD---SVVFENT--PAADVVGVVGEGFKDAMITL 246
PTZ00460 PTZ00460
acyl-CoA dehydrogenase; Provisional
 90-384 1.93e-06

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185639 [Multi-domain]  Cd Length: 646  Bit Score: 49.84  E-value: 1.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532  90 IPAVNKLGSmplilsgsDEVKQRYLPELASGEAMFSYGLSEREAGSDTASMRTRAVRD--GDDWILN-----GQKSWITN 162
Cdd:PTZ00460  103 IPAFQVLGT--------DEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATYDkqTNEFVIHtpsveAVKFWPGE 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 163 AG-ISKYYTVMAVTDPDGpRGRNISAFVVHIDD-------PGFSFGEPERKLGIKGSPTRELIFDNVRIPGDRLVG---- 230
Cdd:PTZ00460  175 LGfLCNFALVYAKLIVNG-KNKGVHPFMVRIRDkethkplQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLAryik 253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 231 -------------KVGEGLRTALRTLdhtrvtIGAQAVGIAQGALDYALGYVKERKQFGK------AIADFQGIQF---- 287
Cdd:PTZ00460  254 vsedgqverqgnpKVSYASMMYMRNL------IIDQYPRFAAQALTVAIRYSIYRQQFTNdnkqenSVLEYQTQQQkllp 327

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 288 MLADM-AMKLEAARQMVYVAAAKSERDDADLSFYG------AAAKCFASDVAMHiTTDAVQL-LGGYGYTRDYPVERMMR 359
Cdd:PTZ00460  328 LLAEFyACIFGGLKIKELVDDNFNRVQKNDFSLLQlthailSAAKANYTYFVSN-CAEWCRLsCGGHGYAHYSGLPAIYF 406

                         330       340
                  ....*....|....*....|....*
gi 1605303532 360 DAKITQIYEGTNQIQRVVMARQLLK 384
Cdd:PTZ00460  407 DMSPNITLEGENQIMYLQLARYLLK 431
PLN02443 PLN02443
acyl-coenzyme A oxidase
 105-384 2.19e-04

acyl-coenzyme A oxidase


Pssm-ID: 178062 [Multi-domain]  Cd Length: 664  Bit Score: 43.29  E-value: 2.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 105 GSDEVKQRYLPELASGEAMFSYGLSEREAGSDTASMRTRAVRD--GDDWILN-----GQKSWITNAG-ISKYYTVMAVTD 176
Cdd:PLN02443  114 GTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFDpkTDEFVIHsptltSSKWWPGGLGkVSTHAVVYARLI 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 177 PDGpRGRNISAFVVHI---DD----PGFSFGEPERKLGIKGSPTRE---LIFDNVRIPGDRL------VGKVGEGLRT-- 238
Cdd:PLN02443  194 TNG-KDHGIHGFIVQLrslDDhsplPGVTVGDIGMKFGNGAYNTMDngfLRFDHVRIPRDQMlmrlskVTREGKYVQSdv 272

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 239 ----ALRTLDHTRVTIGAQAVGIAQGALDYALGYVKERKQFGkaiADFQGIQFMLADmaMKLEAARQMVYVAAAKSER-- 312
Cdd:PLN02443  273 prqlVYGTMVYVRQTIVADASTALSRAVCIATRYSAVRRQFG---SQDGGPETQVID--YKTQQSRLFPLLASAYAFRfv 347

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 313 ---------------DDADLSFYGAAAKCFA--SDVAMHITTDAVQ----LLGGYGYTRDYPVERMMRDAKITQIYEGTN 371
Cdd:PLN02443  348 gewlkwlytdvtqrlEANDFSTLPEAHACTAglKSLTTSATADGIEecrkLCGGHGYLCSSGLPELFAVYVPACTYEGDN 427

                         330
                  ....*....|...
gi 1605303532 372 QIQRVVMARQLLK 384
Cdd:PLN02443  428 VVLLLQVARFLMK 440
PLN02312 PLN02312
acyl-CoA oxidase
 126-275 3.66e-04

acyl-CoA oxidase


Pssm-ID: 215178 [Multi-domain]  Cd Length: 680  Bit Score: 42.45  E-value: 3.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 126 YGLSEREAGSDTASMRTRAVRD--GDDWILN-----GQKSWITNAGISKYYT-VMAVTDPDGpRGRNISAFVVHIDD--- 194
Cdd:PLN02312  189 FAMTELGHGSNVRGIETVTTYDpkTEEFVINtpcesAQKYWIGGAANHATHTiVFSQLHING-KNEGVHAFIAQIRDqdg 267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605303532 195 ---PGFSFGEPERKLGIKGSPTRELIFDNVRIPGDRLVGKVGEGL--------------RTA--LRTLDHTRVTIGAQAV 255
Cdd:PLN02312  268 nicPNIRIADCGHKIGLNGVDNGRIWFDNLRIPRENLLNSVADVSpdgkyvsaikdpdqRFGafLAPLTSGRVTIAVSAI 347

                         170       180
                  ....*....|....*....|
gi 1605303532 256 GIAQGALDYALGYVKERKQF 275
Cdd:PLN02312  348 YSSKVGLAIAIRYSLSRRAF 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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