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Conserved domains on  [gi|281363737|ref|NP_611409|]
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uncharacterized protein Dmel_CG7461, isoform B [Drosophila melanogaster]

Protein Classification

acyl-CoA dehydrogenase family protein( domain architecture ID 10100190)

acyl-CoA dehydrogenase (ACAD) family protein similar to mitochondrial very long-chain specific acyl-CoA dehydrogenase (VLCAD), which is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats

CATH:  1.10.540.10
EC:  1.3.8.-
Gene Ontology:  GO:0016627|GO:0006631|GO:0050660
PubMed:  10760462|12504675
SCOP:  3001580|3001701

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
VLCAD cd01161
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ...
 45-454 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: 756.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737  45 SFMANIFRGSLVSSQVFPYPDVLTAEQKELTNSLIDPFERFFSDVNDAARNDANSKIDDTTSTALWELGAFGIQVPSEFG 124
Cdd:cd01161    1 SFALNMFLGDIVTKQVFPYPSVLTEEQTEELNMLVGPVEKFFEEVNDPAKNDQLEKIPRKTLTQLKELGLFGLQVPEEYG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 125 GLGLNNTQYGRLCAIVGVnDLGLGITIGAHQSIGFKGILLYGTPEQKEKYLPKVAAEQVYAAFALTEPSSGSDAGSIRCR 204
Cdd:cd01161   81 GLGLNNTQYARLAEIVGM-DLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 205 AVKSADGKHYVLNGSKIWISNGGIAEIMTVFAQTEQVDPkTGEKKDKVTAFIVERSFGGVTNGPPEKKMGIKASNTAEVY 284
Cdd:cd01161  160 AVLSEDGKHYVLNGSKIWITNGGIADIFTVFAKTEVKDA-TGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVY 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 285 FEDVKIPIENVLGKEGDGFKVAMNILNNGRFGMGATLSGTMKKCIEQATEHANNRVQFGQKLKNYGSIQEKLAQMNILQY 364
Cdd:cd01161  239 FEDVKIPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQY 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 365 ATESMAFTISQNMDAGSK-DYHLEAAISKIYASESAWYVCDEAIQILGGMGYMVDNGLERVLRDLRIFRIFEGTNDILRL 443
Cdd:cd01161  319 ATESMAYMTSGNMDRGLKaEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRL 398

                        410
                 ....*....|.
gi 281363737 444 FIALTGIQYAG 454
Cdd:cd01161  399 FIALTGLQHAG 409
 
Name Accession Description Interval E-value
VLCAD cd01161
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ...
 45-454 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: 756.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737  45 SFMANIFRGSLVSSQVFPYPDVLTAEQKELTNSLIDPFERFFSDVNDAARNDANSKIDDTTSTALWELGAFGIQVPSEFG 124
Cdd:cd01161    1 SFALNMFLGDIVTKQVFPYPSVLTEEQTEELNMLVGPVEKFFEEVNDPAKNDQLEKIPRKTLTQLKELGLFGLQVPEEYG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 125 GLGLNNTQYGRLCAIVGVnDLGLGITIGAHQSIGFKGILLYGTPEQKEKYLPKVAAEQVYAAFALTEPSSGSDAGSIRCR 204
Cdd:cd01161   81 GLGLNNTQYARLAEIVGM-DLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 205 AVKSADGKHYVLNGSKIWISNGGIAEIMTVFAQTEQVDPkTGEKKDKVTAFIVERSFGGVTNGPPEKKMGIKASNTAEVY 284
Cdd:cd01161  160 AVLSEDGKHYVLNGSKIWITNGGIADIFTVFAKTEVKDA-TGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVY 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 285 FEDVKIPIENVLGKEGDGFKVAMNILNNGRFGMGATLSGTMKKCIEQATEHANNRVQFGQKLKNYGSIQEKLAQMNILQY 364
Cdd:cd01161  239 FEDVKIPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQY 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 365 ATESMAFTISQNMDAGSK-DYHLEAAISKIYASESAWYVCDEAIQILGGMGYMVDNGLERVLRDLRIFRIFEGTNDILRL 443
Cdd:cd01161  319 ATESMAYMTSGNMDRGLKaEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRL 398

                        410
                 ....*....|.
gi 281363737 444 FIALTGIQYAG 454
Cdd:cd01161  399 FIALTGLQHAG 409
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 67-446 1.24e-136

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: 403.84  E-value: 1.24e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737  67 LTAEQKELtnslIDPFERFFSDVND--AARNDANSKIDDTTSTALWELGAFGIQVPSEFGGLGLNNTQYGRLCAIVGVND 144
Cdd:COG1960    5 LTEEQRAL----RDEVREFAEEEIApeAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARAD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 145 LGLGITIGAHQSIGfKGILLYGTPEQKEKYLPKVAAEQVYAAFALTEPSSGSDAGSIRCRAVKsaDGKHYVLNGSKIWIS 224
Cdd:COG1960   81 ASLALPVGVHNGAA-EALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVR--DGDGYVLNGQKTFIT 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 225 NGGIAEIMTVFAQTeqvDPKTGEKKdkVTAFIVERSFGGVTNGPPEKKMGIKASNTAEVYFEDVKIPIENVLGKEGDGFK 304
Cdd:COG1960  158 NAPVADVILVLART---DPAAGHRG--ISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFK 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 305 VAMNILNNGRFGMGATLSGTMKKCIEQATEHANNRVQFGQKLKNYGSIQEKLAQMNILQYATESMAFTISQNMDAGsKDY 384
Cdd:COG1960  233 IAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAG-EDA 311

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281363737 385 HLEAAISKIYASESAWYVCDEAIQILGGMGYMVDNGLERVLRDLRIFRIFEGTNDILRLFIA 446
Cdd:COG1960  312 ALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIA 373
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 99-445 9.47e-67

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 223.60  E-value: 9.47e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737  99 SKIDDT----TSTALWEL-GAF---GIQVPSEFGGLGLnntqyGRLCAIVGVNDL-----GLGITIGAHQSIGFKGILLY 165
Cdd:PLN02519  50 AAIDATnsfpKDVNLWKLmGDFnlhGITAPEEYGGLGL-----GYLYHCIAMEEIsrasgSVGLSYGAHSNLCINQLVRN 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 166 GTPEQKEKYLPKVAAEQVYAAFALTEPSSGSDAGSIRCRAVKSADGkhYVLNGSKIWISNGGIAEIMTVFAQTeqvDPKT 245
Cdd:PLN02519 125 GTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGG--YVLNGNKMWCTNGPVAQTLVVYAKT---DVAA 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 246 GEKKdkVTAFIVERSFGGVTNGPPEKKMGIKASNTAEVYFEDVKIPIENVLGKEGDGFKVAMNILNNGRFGMGATLSGTM 325
Cdd:PLN02519 200 GSKG--ITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSGLDLERLVLAAGPLGLM 277

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 326 KKCIEQATEHANNRVQFGQKLKNYGSIQEKLAQMNILQYATESMAFTISQNMDAGSKDYHlEAAISKIYASESAWYVCDE 405
Cdd:PLN02519 278 QACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRK-DCAGVILCAAERATQVALQ 356

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 281363737 406 AIQILGGMGYMVDNGLERVLRDLRIFRIFEGTNDILRLFI 445
Cdd:PLN02519 357 AIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLI 396
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 300-446 3.98e-43

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: 151.64  E-value: 3.98e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737  300 GDGFKVAMNILNNGRFGMGATLSGTMKKCIEQATEHANNRVQFGQKLKNYGSIQEKLAQMNILQYATESMAFTISQNMDA 379
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281363737  380 GSKDyHLEAAISKIYASESAWYVCDEAIQILGGMGYMVDNGLERVLRDLRIFRIFEGTNDILRLFIA 446
Cdd:pfam00441  81 GGPD-GAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIA 146
 
Name Accession Description Interval E-value
VLCAD cd01161
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ...
 45-454 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: 756.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737  45 SFMANIFRGSLVSSQVFPYPDVLTAEQKELTNSLIDPFERFFSDVNDAARNDANSKIDDTTSTALWELGAFGIQVPSEFG 124
Cdd:cd01161    1 SFALNMFLGDIVTKQVFPYPSVLTEEQTEELNMLVGPVEKFFEEVNDPAKNDQLEKIPRKTLTQLKELGLFGLQVPEEYG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 125 GLGLNNTQYGRLCAIVGVnDLGLGITIGAHQSIGFKGILLYGTPEQKEKYLPKVAAEQVYAAFALTEPSSGSDAGSIRCR 204
Cdd:cd01161   81 GLGLNNTQYARLAEIVGM-DLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 205 AVKSADGKHYVLNGSKIWISNGGIAEIMTVFAQTEQVDPkTGEKKDKVTAFIVERSFGGVTNGPPEKKMGIKASNTAEVY 284
Cdd:cd01161  160 AVLSEDGKHYVLNGSKIWITNGGIADIFTVFAKTEVKDA-TGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVY 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 285 FEDVKIPIENVLGKEGDGFKVAMNILNNGRFGMGATLSGTMKKCIEQATEHANNRVQFGQKLKNYGSIQEKLAQMNILQY 364
Cdd:cd01161  239 FEDVKIPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQY 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 365 ATESMAFTISQNMDAGSK-DYHLEAAISKIYASESAWYVCDEAIQILGGMGYMVDNGLERVLRDLRIFRIFEGTNDILRL 443
Cdd:cd01161  319 ATESMAYMTSGNMDRGLKaEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRL 398

                        410
                 ....*....|.
gi 281363737 444 FIALTGIQYAG 454
Cdd:cd01161  399 FIALTGLQHAG 409
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 67-446 1.24e-136

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: 403.84  E-value: 1.24e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737  67 LTAEQKELtnslIDPFERFFSDVND--AARNDANSKIDDTTSTALWELGAFGIQVPSEFGGLGLNNTQYGRLCAIVGVND 144
Cdd:COG1960    5 LTEEQRAL----RDEVREFAEEEIApeAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARAD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 145 LGLGITIGAHQSIGfKGILLYGTPEQKEKYLPKVAAEQVYAAFALTEPSSGSDAGSIRCRAVKsaDGKHYVLNGSKIWIS 224
Cdd:COG1960   81 ASLALPVGVHNGAA-EALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVR--DGDGYVLNGQKTFIT 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 225 NGGIAEIMTVFAQTeqvDPKTGEKKdkVTAFIVERSFGGVTNGPPEKKMGIKASNTAEVYFEDVKIPIENVLGKEGDGFK 304
Cdd:COG1960  158 NAPVADVILVLART---DPAAGHRG--ISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFK 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 305 VAMNILNNGRFGMGATLSGTMKKCIEQATEHANNRVQFGQKLKNYGSIQEKLAQMNILQYATESMAFTISQNMDAGsKDY 384
Cdd:COG1960  233 IAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAG-EDA 311

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281363737 385 HLEAAISKIYASESAWYVCDEAIQILGGMGYMVDNGLERVLRDLRIFRIFEGTNDILRLFIA 446
Cdd:COG1960  312 ALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIA 373
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
 92-446 1.07e-114

Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA dehydrogenases; Short chain acyl-CoA dehydrogenase (SCAD). SCAD is a mitochondrial beta-oxidation enzyme. It catalyzes the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of SCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. This subgroup also contains the eukaryotic short/branched chain acyl-CoA dehydrogenase(SBCAD), the bacterial butyryl-CoA dehydorgenase(BCAD) and 2-methylbutyryl-CoA dehydrogenase, which is involved in isoleucine catabolism. These enzymes are homotetramers.


Pssm-ID: 173847 [Multi-domain]  Cd Length: 373  Bit Score: 347.33  E-value: 1.07e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737  92 AARNDANSKIDDTTSTALWELGAFGIQVPSEFGGLGLNNTQYGRLCAIVGVNDLGLGITIGAHQSIGFKGILLYGTPEQK 171
Cdd:cd01158   22 AAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVIVSVHNSLGANPIIKFGTEEQK 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 172 EKYLPKVAAEQVYAAFALTEPSSGSDAGSIRCRAVKsaDGKHYVLNGSKIWISNGGIAEIMTVFAQTeqvDPKTGEKKdk 251
Cdd:cd01158  102 KKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKK--DGDDYVLNGSKMWITNGGEADFYIVFAVT---DPSKGYRG-- 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 252 VTAFIVERSFGGVTNGPPEKKMGIKASNTAEVYFEDVKIPIENVLGKEGDGFKVAMNILNNGRFGMGATLSGTMKKCIEQ 331
Cdd:cd01158  175 ITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGIAAQALGIAQAALDA 254

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 332 ATEHANNRVQFGQKLKNYGSIQEKLAQMNILQYATESMAFTISQNMDAGsKDYHLEAAISKIYASESAWYVCDEAIQILG 411
Cdd:cd01158  255 AVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNG-EPFIKEAAMAKLFASEVAMRVTTDAVQIFG 333

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 281363737 412 GMGYMVDNGLERVLRDLRIFRIFEGTNDILRLFIA 446
Cdd:cd01158  334 GYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIA 368
ACAD cd00567
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
 146-446 2.73e-108

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: 329.24  E-value: 2.73e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 146 GLGITIGAHQsigfkgILLYGTPEQKEKYLPKVAAEQVYAAFALTEPSSGSDAGSIRCRAVKsaDGKHYVLNGSKIWISN 225
Cdd:cd00567   38 ELGLLLGAAL------LLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARK--DGDGYVLNGRKIFISN 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 226 GGIAEIMTVFAQTEQVDPKTGekkdKVTAFIVERSFGGVTNGPPEKKMGIKASNTAEVYFEDVKIPIENVLGKEGDGFKV 305
Cdd:cd00567  110 GGDADLFIVLARTDEEGPGHR----GISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFEL 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 306 AMNILNNGRFGMGATLSGTMKKCIEQATEHANNRVQFGQKLKNYGSIQEKLAQMNILQYATESMAFTISQNMDAGSKDYH 385
Cdd:cd00567  186 AMKGLNVGRLLLAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEAR 265

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281363737 386 LEAAISKIYASESAWYVCDEAIQILGGMGYMVDNGLERVLRDLRIFRIFEGTNDILRLFIA 446
Cdd:cd00567  266 LEAAMAKLFATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIA 326
IVD cd01156
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ...
 99-446 4.39e-88

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: 278.91  E-value: 4.39e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737  99 SKIDDTTS--TALW----ELGAFGIQVPSEFGGLGLnntqyGRLCAIVGVNDL-----GLGITIGAHQSIGFKGILLYGT 167
Cdd:cd01156   26 AKIDRDNEfpRDLWrkmgKLGLLGITAPEEYGGSGM-----GYLAHVIIMEEIsrasgSVALSYGAHSNLCINQIYRNGS 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 168 PEQKEKYLPKVAAEQVYAAFALTEPSSGSDAGSIRCRAVKsaDGKHYVLNGSKIWISNGGIAEIMTVFAQTeqvDPKTGe 247
Cdd:cd01156  101 AAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEK--KGDRYVLNGSKMWITNGPDADTLVVYAKT---DPSAG- 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 248 kKDKVTAFIVERSFGGVTNGPPEKKMGIKASNTAEVYFEDVKIPIENVLGKEGDGFKVAMNILNNGRFGMGATLSGTMKK 327
Cdd:cd01156  175 -AHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGLDYERLVLAGGPIGIMQA 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 328 CIEQATEHANNRVQFGQKLKNYGSIQEKLAQMNILQYATESMAFTISQNMDAGSKDyHLEAAISKIYASESAWYVCDEAI 407
Cdd:cd01156  254 ALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMD-PKDAAGVILYAAEKATQVALDAI 332

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 281363737 408 QILGGMGYMVDNGLERVLRDLRIFRIFEGTNDILRLFIA 446
Cdd:cd01156  333 QILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIG 371
IBD cd01162
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ...
 111-446 8.70e-79

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: 254.68  E-value: 8.70e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 111 ELGAFGIQVPSEFGGLGLnntqyGRLCAIVGVNDLGLG-ITIGAHQSIGFKG---ILLYGTPEQKEKYLPKVAAEQVYAA 186
Cdd:cd01162   43 ELGFGGIYIRDDVGGSGL-----SRLDASIIFEALSTGcVSTAAYISIHNMCawmIDSFGNDEQRERFLPDLCTMEKLAS 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 187 FALTEPSSGSDAGSIRCRAVKsaDGKHYVLNGSKIWISNGGIAEIMTVFAQTEQVDPKtgekkdKVTAFIVERSFGGVTN 266
Cdd:cd01162  118 YCLTEPGSGSDAAALRTRAVR--EGDHYVLNGSKAFISGAGDSDVYVVMARTGGEGPK------GISCFVVEKGTPGLSF 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 267 GPPEKKMGIKASNTAEVYFEDVKIPIENVLGKEGDGFKVAMNILNNGRFGMGATLSGTMKKCIEQATEHANNRVQFGQKL 346
Cdd:cd01162  190 GANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRLNIASCSLGAAQAALDLARAYLEERKQFGKPL 269

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 347 KNYGSIQEKLAQMNILQYATESMAFTISQNMDAGSKDYHLEAAISKIYASESAWYVCDEAIQILGGMGYMVDNGLERVLR 426
Cdd:cd01162  270 ADFQALQFKLADMATELVASRLMVRRAASALDRGDPDAVKLCAMAKRFATDECFDVANQALQLHGGYGYLKDYPVEQYVR 349

                        330       340
                 ....*....|....*....|
gi 281363737 427 DLRIFRIFEGTNDILRLFIA 446
Cdd:cd01162  350 DLRVHQILEGTNEIMRLIIA 369
LCAD cd01160
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ...
 106-446 7.96e-71

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: 233.55  E-value: 7.96e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 106 STALW----ELGAFGIQVPSEFGGLGLNntqygRLCAIVGVNDL----GLGITIGAHQSIGFKGILLYGTPEQKEKYLPK 177
Cdd:cd01160   32 PREVWrkagEQGLLGVGFPEEYGGIGGD-----LLSAAVLWEELaragGSGPGLSLHTDIVSPYITRAGSPEQKERVLPQ 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 178 VAAEQVYAAFALTEPSSGSDAGSIRCRAVKsaDGKHYVLNGSKIWISNGGIAEIMTVFAQTeqvdpkTGEKKDK--VTAF 255
Cdd:cd01160  107 MVAGKKIGAIAMTEPGAGSDLQGIRTTARK--DGDHYVLNGSKTFITNGMLADVVIVVART------GGEARGAggISLF 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 256 IVERSFGGVTNGPPEKKMGIKASNTAEVYFEDVKIPIENVLGKEGDGFKVAMNILNNGRFGMGATLSGTMKKCIEQATEH 335
Cdd:cd01160  179 LVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLLIAAGALAAAEFMLEETRNY 258

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 336 ANNRVQFGQKLKNYGSIQEKLAQMNILQYATESMAFTISQNMDAGSKDYhLEAAISKIYASESAWYVCDEAIQILGGMGY 415
Cdd:cd01160  259 VKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDV-AEASMAKYWATELQNRVAYECVQLHGGWGY 337

                        330       340       350
                 ....*....|....*....|....*....|.
gi 281363737 416 MVDNGLERVLRDLRIFRIFEGTNDILRLFIA 446
Cdd:cd01160  338 MREYPIARAYRDARVQPIYGGTTEIMKELIS 368
MCAD cd01157
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ...
 110-446 1.97e-69

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: 230.17  E-value: 1.97e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 110 WELGAFGIQVPSEFGGLGLnntqyGRLCAIVGVNDLGLGIT-----IGAHqSIGFKGILLYGTPEQKEKYLPKVAAEQVY 184
Cdd:cd01157   42 WELGLMNTHIPEDCGGLGL-----GTFDTCLITEELAYGCTgvqtaIEAN-SLGQMPVIISGNDEQKKKYLGRMTEEPLM 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 185 AAFALTEPSSGSDAGSIRCRAVKSADgkHYVLNGSKIWISNGGIAEIMTVFAQTEQvDPKTGEKKdKVTAFIVERSFGGV 264
Cdd:cd01157  116 CAYCVTEPGAGSDVAGIKTKAEKKGD--EYIINGQKMWITNGGKANWYFLLARSDP-DPKCPASK-AFTGFIVEADTPGI 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 265 TNGPPEKKMGIKASNTAEVYFEDVKIPIENVLGKEGDGFKVAMNILNNGRFGMGATLSGTMKKCIEQATEHANNRVQFGQ 344
Cdd:cd01157  192 QPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGK 271

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 345 KLKNYGSIQEKLAQMNIlQYATESMAFTISQN-MDAGSKDYHlEAAISKIYASESAWYVCDEAIQILGGMGYMVDNGLER 423
Cdd:cd01157  272 LIAEHQAVSFMLADMAM-KVELARLAYQRAAWeVDSGRRNTY-YASIAKAFAADIANQLATDAVQIFGGNGFNSEYPVEK 349

                        330       340
                 ....*....|....*....|...
gi 281363737 424 VLRDLRIFRIFEGTNDILRLFIA 446
Cdd:cd01157  350 LMRDAKIYQIYEGTSQIQRLIIS 372
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 99-445 9.47e-67

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 223.60  E-value: 9.47e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737  99 SKIDDT----TSTALWEL-GAF---GIQVPSEFGGLGLnntqyGRLCAIVGVNDL-----GLGITIGAHQSIGFKGILLY 165
Cdd:PLN02519  50 AAIDATnsfpKDVNLWKLmGDFnlhGITAPEEYGGLGL-----GYLYHCIAMEEIsrasgSVGLSYGAHSNLCINQLVRN 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 166 GTPEQKEKYLPKVAAEQVYAAFALTEPSSGSDAGSIRCRAVKSADGkhYVLNGSKIWISNGGIAEIMTVFAQTeqvDPKT 245
Cdd:PLN02519 125 GTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGG--YVLNGNKMWCTNGPVAQTLVVYAKT---DVAA 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 246 GEKKdkVTAFIVERSFGGVTNGPPEKKMGIKASNTAEVYFEDVKIPIENVLGKEGDGFKVAMNILNNGRFGMGATLSGTM 325
Cdd:PLN02519 200 GSKG--ITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSGLDLERLVLAAGPLGLM 277

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 326 KKCIEQATEHANNRVQFGQKLKNYGSIQEKLAQMNILQYATESMAFTISQNMDAGSKDYHlEAAISKIYASESAWYVCDE 405
Cdd:PLN02519 278 QACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRK-DCAGVILCAAERATQVALQ 356

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 281363737 406 AIQILGGMGYMVDNGLERVLRDLRIFRIFEGTNDILRLFI 445
Cdd:PLN02519 357 AIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLI 396
GCD cd01151
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ...
 111-451 1.71e-63

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: 214.53  E-value: 1.71e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 111 ELGAFGIQvPSEFGGLGLNNTQYGRLCAIVGVNDLGLGITIGAHQSIGFKGILLYGTPEQKEKYLPKVAAEQVYAAFALT 190
Cdd:cd01151   55 ELGLLGAT-IKGYGCAGLSSVAYGLIAREVERVDSGYRSFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLT 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 191 EPSSGSDAGSIRCRAVKsaDGKHYVLNGSKIWISNGGIAEIMTVFAQTEQvdpktgekKDKVTAFIVERSFGGVTNGPPE 270
Cdd:cd01151  134 EPNHGSDPGGMETRARK--DGGGYKLNGSKTWITNSPIADVFVVWARNDE--------TGKIRGFILERGMKGLSAPKIQ 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 271 KKMGIKASNTAEVYFEDVKIPIENVLgKEGDGFKVAMNILNNGRFGMGATLSGTMKKCIEQATEHANNRVQFGQKLKNYG 350
Cdd:cd01151  204 GKFSLRASITGEIVMDNVFVPEENLL-PGAEGLRGPFKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQ 282

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 351 SIQEKLAQMNILQYATESMAFTISQNMDAGsKDYHLEAAISKIYASESAWYVCDEAIQILGGMGYMVDNGLERVLRDLRI 430
Cdd:cd01151  283 LVQKKLADMLTEIALGLLACLRVGRLKDQG-KATPEQISLLKRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLES 361

                        330       340
                 ....*....|....*....|...
gi 281363737 431 FRIFEGTNDILRLFI--ALTGIQ 451
Cdd:cd01151  362 VNTYEGTHDIHALILgrAITGIQ 384
PTZ00461 PTZ00461
isovaleryl-CoA dehydrogenase; Provisional
 68-437 2.39e-62

isovaleryl-CoA dehydrogenase; Provisional


Pssm-ID: 185640 [Multi-domain]  Cd Length: 410  Bit Score: 212.10  E-value: 2.39e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737  68 TAEQKELTNSLidpfERFFSDVND--AARNDANSKIDDTTSTALWELGAFGIQVPSEFGGLGLNNTQYGRLCAIVGVNDL 145
Cdd:PTZ00461  38 TPEHAALRETV----AKFSREVVDkhAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDP 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 146 GLGITIGAHQSIGFKGILLYGTPEQKEKYLPKVAAEQVYAAFALTEPSSGSDAGSIRCRAVKSADGKhYVLNGSKIWISN 225
Cdd:PTZ00461 114 GFCLAYLAHSMLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNGN-YVLNGSKIWITN 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 226 GGIAEIMTVFAQTEqvdpktgekkDKVTAFIVERSFGGVTNGPPEKKMGIKASNTAEVYFEDVKIPIENVLGKEGDGFKV 305
Cdd:PTZ00461 193 GTVADVFLIYAKVD----------GKITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVG 262

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 306 AMNILNNGRFGMGATLSGTMKKCIEQATEHANNRVQFGQKLKNYGSIQEKLAQMNILQYATESMAFTISQNMDAGSKDyH 385
Cdd:PTZ00461 263 MMRNLELERVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKN-R 341

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 281363737 386 LEAAISKIYASESAWYVCDEAIQILGGMGYMVDNGLERVLRDLRIFRIFEGT 437
Cdd:PTZ00461 342 LGSDAAKLFATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGT 393
ACAD_fadE5 cd01153
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ...
 111-440 5.10e-54

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: 189.91  E-value: 5.10e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 111 ELGAFGIQVPSEFGGLGLNNTQYGRLCAIVGVNDLGLGITIGAHQsiGFKGILLYGTPEQKEKYLPKVAAEQVYAAFALT 190
Cdd:cd01153   47 EAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDAPLMYASGTQG--AAATLLAHGTEAQREKWIPRLAEGEWTGTMCLT 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 191 EPSSGSDAGSIRCRAVKSADGKhYVLNGSKIWISNG--GIAE--IMTVFAQTEqvDPKTGEKKDK---VTAFIVERSFGG 263
Cdd:cd01153  125 EPDAGSDLGALRTKAVYQADGS-WRINGVKRFISAGehDMSEniVHLVLARSE--GAPPGVKGLSlflVPKFLDDGERNG 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 264 VTNGPPEKKMGIKASNTAEVYFEDVKIPIenvLGKEGDGFKVAMNILNNGRFGMGATLSGTMKKCIEQATEHANNRVQFG 343
Cdd:cd01153  202 VTVARIEEKMGLHGSPTCELVFDNAKGEL---IGEEGMGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGG 278

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 344 QKLKN--------YGSIQEKLAQMNILQYATESMA-----FTISQNMDAGSKDY--HLEA------AISKIYASESAWYV 402
Cdd:cd01153  279 DLIKAapavtiihHPDVRRSLMTQKAYAEGSRALDlytatVQDLAERKATEGEDrkALSAladlltPVVKGFGSEAALEA 358

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 281363737 403 CDEAIQILGGMGYMVDNGLERVLRDLRIFRIFEGTNDI 440
Cdd:cd01153  359 VSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGI 396
PRK12341 PRK12341
acyl-CoA dehydrogenase;
67-441 4.16e-52

acyl-CoA dehydrogenase;


Pssm-ID: 183454 [Multi-domain]  Cd Length: 381  Bit Score: 183.78  E-value: 4.16e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737  67 LTAEQKELTNSLIDPFERFFSDvNDAARNDANSKIDDTTSTALWELGAFGIQVPSEFGGLGLNNT-------QYGRLCAI 139
Cdd:PRK12341   5 LTEEQELLLASIRELITRNFPE-EYFRTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVtqmlvleEVSKCGAP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 140 VGVndlglgitIGAHQSIgfKGILLYGTPEQKEKYLPKVAAEQVYA-AFALTEPSSGSDAGSIRCRAVKSaDGKHYvLNG 218
Cdd:PRK12341  84 AFL--------ITNGQCI--HSMRRFGSAEQLRKTAESTLETGDPAyALALTEPGAGSDNNSATTTYTRK-NGKVY-LNG 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 219 SKIWISNGGIAEIMTVFAQteqvDPKTGEKKDKVTAFIVERSFGGVTNGPPEKkMGIKASNTAEVYFEDVKIPIENVLGK 298
Cdd:PRK12341 152 QKTFITGAKEYPYMLVLAR----DPQPKDPKKAFTLWWVDSSKPGIKINPLHK-IGWHMLSTCEVYLDNVEVEESDLVGE 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 299 EGDGFKVAMNILNNGRFGMGATLSGTMKKCIEQATEHANNRVQFGQKLKNYGSIQEKLAQMNIlqyATESMaftisQNM- 377
Cdd:PRK12341 227 EGMGFLNVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAI---KIENM-----RNMv 298

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 378 --DAGSKDYHL----EAAISKIYASESAWYVCDEAIQILGGMGYMVDNGLERVLRDLRIFRIFEGTNDIL 441
Cdd:PRK12341 299 ykVAWQADNGQslrtSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIM 368
PRK03354 PRK03354
crotonobetainyl-CoA dehydrogenase; Validated
 67-443 1.15e-49

crotonobetainyl-CoA dehydrogenase; Validated


Pssm-ID: 179566 [Multi-domain]  Cd Length: 380  Bit Score: 177.33  E-value: 1.15e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737  67 LTAEQ-------KELTNSliDPFERFFsdvndaARNDANSKIDDTTSTALWELGAFGIQVPSEFGGLGLNNTQYGRLCAI 139
Cdd:PRK03354   5 LNDEQelfvagiRELMAS--ENWEAYF------AECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWME 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 140 VGvnDLGLGITIGAHQSIGFKGILLYGTPEQKEKYLPKVAA-EQVYAaFALTEPSSGSDAGSIRCrAVKSADGKHYvLNG 218
Cdd:PRK03354  77 LG--RLGAPTYVLYQLPGGFNTFLREGTQEQIDKIMAFRGTgKQMWN-SAITEPGAGSDVGSLKT-TYTRRNGKVY-LNG 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 219 SKIWISNGGIAEIMTVFAQTEqvdpkTGEKKDKVTAFIVERSFGGVTNGPPEKkMGIKASNTAEVYFEDVKIPIENVLGK 298
Cdd:PRK03354 152 SKCFITSSAYTPYIVVMARDG-----ASPDKPVYTEWFVDMSKPGIKVTKLEK-LGLRMDSCCEITFDDVELDEKDMFGR 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 299 EGDGFKVAMNILNNGRFGMGATLSGTMKKCIEQATEHANNRVQFGQKLKNYGSIQEKLAQMNILQYATESMAFTISQNMD 378
Cdd:PRK03354 226 EGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKAD 305

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281363737 379 AGSKDYHlEAAISKIYASESAWYVCDEAIQILGGMGYMVDNGLERVLRDLRIFRIFEGTNDILRL 443
Cdd:PRK03354 306 NGTITSG-DAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQIL 369
ACAD_fadE6_17_26 cd01152
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ...
 108-446 4.38e-45

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: 164.44  E-value: 4.38e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 108 ALWELGAFGIQVPSEFGGLGLNNTQ-------YGRLCAIVGVNDLGLGiTIGAhqsigfkGILLYGTPEQKEKYLPKVAA 180
Cdd:cd01152   43 ALAAAGWAAPGWPKEYGGRGASLMEqlifreeMAAAGAPVPFNQIGID-LAGP-------TILAYGTDEQKRRFLPPILS 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 181 EQVYAAFALTEPSSGSDAGSIRCRAVKsaDGKHYVLNGSKIWISNGGIAEIMTVFAQTeqvDPkTGEKKDKVTAFIVERS 260
Cdd:cd01152  115 GEEIWCQGFSEPGAGSDLAGLRTRAVR--DGDDWVVNGQKIWTSGAHYADWAWLLVRT---DP-EAPKHRGISILLVDMD 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 261 FGGVTNGPPEKKMGikASNTAEVYFEDVKIPIENVLGKEGDGFKVAMNILNNGRFGMGatlsGTMKKCIEQATEHANNRV 340
Cdd:cd01152  189 SPGVTVRPIRSING--GEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTLNFERVSIG----GSAATFFELLLARLLLLT 262

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 341 QFGQKLKNYGSIQEKLAQMNILQYATESMAFTISQNMDAGsKDYHLEAAISKIYASESAWYVCDEAIQILGGMGYMVDNG 420
Cdd:cd01152  263 RDGRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAG-KPPGAEASIAKLFGSELAQELAELALELLGTAALLRDPA 341

                        330       340       350
                 ....*....|....*....|....*....|....
gi 281363737 421 L--------ERVLRDLRIFRIFEGTNDILRLFIA 446
Cdd:cd01152  342 PgaelagrwEADYLRSRATTIYGGTSEIQRNIIA 375
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 300-446 3.98e-43

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: 151.64  E-value: 3.98e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737  300 GDGFKVAMNILNNGRFGMGATLSGTMKKCIEQATEHANNRVQFGQKLKNYGSIQEKLAQMNILQYATESMAFTISQNMDA 379
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281363737  380 GSKDyHLEAAISKIYASESAWYVCDEAIQILGGMGYMVDNGLERVLRDLRIFRIFEGTNDILRLFIA 446
Cdd:pfam00441  81 GGPD-GAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIA 146
ACAD_FadE2 cd01155
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ...
 81-451 7.01e-35

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: 136.37  E-value: 7.01e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737  81 PFERFFSD---VNDAARNDANSKIDDTTSTALwELGAFGIQVPSEFGGLGLNNTQYGRLCAIVGVNDLGLGITIGAHQSI 157
Cdd:cd01155   20 PAEQEFLEyyaEGGDRWWTPPPIIEKLKAKAK-AEGLWNLFLPEVSGLSGLTNLEYAYLAEETGRSFFAPEVFNCQAPDT 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 158 GFKGIL-LYGTPEQKEKYLPKVAAEQVYAAFALTEPS-SGSDAGSIRCRAVKsaDGKHYVLNGSKIWISNGG--IAEIMT 233
Cdd:cd01155   99 GNMEVLhRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIER--DGDDYVINGRKWWSSGAGdpRCKIAI 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 234 VFAQTeqvDPkTGEKKDKVTAFI-VERSFGGVTNGPPEKKMGIKAS--NTAEVYFEDVKIPIENVLGKEGDGFKVAMNIL 310
Cdd:cd01155  177 VMGRT---DP-DGAPRHRQQSMIlVPMDTPGVTIIRPLSVFGYDDAphGHAEITFDNVRVPASNLILGEGRGFEIAQGRL 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 311 NNGRFGMGATLSGTMKKCIEQATEHANNRVQFGQKLKNYGSIQEKLAQMNI----LQYATESMAFTISQnmdAGSKDYHL 386
Cdd:cd01155  253 GPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIeieqARLLVLKAAHMIDT---VGNKAARK 329

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281363737 387 EAAISKIYASESAWYVCDEAIQILGGMGYMVDNGLERVLRDLRIFRIFEGTNDILRLFIALTGIQ 451
Cdd:cd01155  330 EIAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIARMELK 394
AidB cd01154
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ...
 160-443 1.82e-33

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: 132.88  E-value: 1.82e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 160 KGILLYGTPEQKEKYLPKVAAEQ---VYAAFALTEPSSGSDAGSIRCRAVKSADGKhYVLNGSKiWISNGGIAEIMTVFA 236
Cdd:cd01154  121 YALRKYGPEELKQYLPGLLSDRYktgLLGGTWMTEKQGGSDLGANETTAERSGGGV-YRLNGHK-WFASAPLADAALVLA 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 237 QTEQVDPKTGekkdKVTAFIVERSF-GGVTNGPP----EKKMGIKASNTAEVYFEDVkipIENVLGKEGDGFKVAMNILN 311
Cdd:cd01154  199 RPEGAPAGAR----GLSLFLVPRLLeDGTRNGYRirrlKDKLGTRSVATGEVEFDDA---EAYLIGDEGKGIYYILEMLN 271

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 312 NGRFGMGATLSGTMKKCIEQATEHANNRVQFGQKLKNYGSIQEKLAQMNILQYATESMAFTISQNMDAGSKDYHLEA--- 388
Cdd:cd01154  272 ISRLDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDRAAADKPVEAhma 351

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 281363737 389 ----AISKIYASESAWYVCDEAIQILGGMGYMVDNGLERVLRDLRIFRIFEGTNDILRL 443
Cdd:cd01154  352 rlatPVAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQAL 410
Acyl-CoA_dh_M pfam02770
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ...
 186-286 3.98e-28

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: 108.14  E-value: 3.98e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737  186 AFALTEPSSGSDAGSIRCRAVKsADGKHYVLNGSKIWISNGGIAEIMTVFAQTEQVDPKTGekkdkVTAFIVERSFGGVT 265
Cdd:pfam02770   1 AFALTEPGAGSDVASLKTTAAD-GDGGGWVLNGTKWWITNAGIADLFLVLARTGGDDRHGG-----ISLFLVPKDAPGVS 74

                          90       100
                  ....*....|....*....|.
gi 281363737  266 NGPPEKKMGIKASNTAEVYFE 286
Cdd:pfam02770  75 VRRIETKLGVRGLPTGELVFD 95
PLN02876 PLN02876
acyl-CoA dehydrogenase
 125-463 3.56e-27

acyl-CoA dehydrogenase


Pssm-ID: 215473 [Multi-domain]  Cd Length: 822  Bit Score: 117.20  E-value: 3.56e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 125 GLGLNNTQYGRLCAIVGVNDLGLGI-TIGAHQSIGFKGILLYGTPEQKEKYLPKVAAEQVYAAFALTEPS-SGSDAGSIR 202
Cdd:PLN02876 491 GAGLSNLEYGYLCEIMGRSVWAPQVfNCGAPDTGNMEVLLRYGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDATNIE 570

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 203 CRAVKSADgkHYVLNGSKIWISnGGI---AEIMTVFAQTeqvDPKTGEKKDKvTAFIVERSFGGVTNGPPEKKMGIKAS- 278
Cdd:PLN02876 571 CSIRRQGD--SYVINGTKWWTS-GAMdprCRVLIVMGKT---DFNAPKHKQQ-SMILVDIQTPGVQIKRPLLVFGFDDAp 643

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 279 -NTAEVYFEDVKIPIENVLGKEGDGFKVAMNILNNGRFGMGATLSGTMKKCIEQATEHANNRVQFGQKLKNYGSIQEKLA 357
Cdd:PLN02876 644 hGHAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHHCMRLIGAAERGMQLMVQRALSRKAFGKLIAQHGSFLSDLA 723

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 358 QMNILQYATESMAFTISQNMDA-GSKDYHLEAAISKIYASESAWYVCDEAIQILGGMGYMVDNGLERVLRDLRIFRIFEG 436
Cdd:PLN02876 724 KCRVELEQTRLLVLEAADQLDRlGNKKARGIIAMAKVAAPNMALKVLDMAMQVHGAAGVSSDTVLAHLWATARTLRIADG 803

                        330       340
                 ....*....|....*....|....*...
gi 281363737 437 TNDIlrlfialtgiqYAGSHLK-ELQRA 463
Cdd:PLN02876 804 PDEV-----------HLGTIAKlELQRA 820
PLN02526 PLN02526
acyl-coenzyme A oxidase
 48-450 6.55e-27

acyl-coenzyme A oxidase


Pssm-ID: 178141 [Multi-domain]  Cd Length: 412  Bit Score: 113.41  E-value: 6.55e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737  48 ANIFRGSLvsSQVFPYPDVLTAEQKELTNSLIDPFERFFSDVndaarndanskiddttSTALWELGAFGIQVPSEFGGL- 126
Cdd:PLN02526  12 ASIFPPSV--SDYYQFDDLLTPEEQALRKRVRECMEKEVAPI----------------MTEYWEKAEFPFHIIPKLGSLg 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 127 ------------GLNNTQYGRLCAIVGVNDLGLGITIGAHQSIGFKGILLYGTPEQKEKYLPKVAAEQVYAAFALTEPSS 194
Cdd:PLN02526  74 iaggtikgygcpGLSITASAIATAEVARVDASCSTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDY 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 195 GSDAGSIRCRAVKSADGkhYVLNGSKIWISNGGIAEIMTVFAQTEQVdpktgekkDKVTAFIVERSFGGVTNGPPEKKMG 274
Cdd:PLN02526 154 GSDASSLNTTATKVEGG--WILNGQKRWIGNSTFADVLVIFARNTTT--------NQINGFIVKKGAPGLKATKIENKIG 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 275 IKASNTAEVYFEDVKIPIENVLgKEGDGFKVAMNILNNGRFGMGATLSGTMKKCIEQATEHANNRVQFGQKLKNYGSIQE 354
Cdd:PLN02526 224 LRMVQNGDIVLKDVFVPDEDRL-PGVNSFQDTNKVLAVSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQE 302

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 355 KLAQM--NIlqyatESMAFT--------ISQNMDAGskdyhlEAAISKIYASESAWYVCDEAIQILGGMGYMVDNGLERV 424
Cdd:PLN02526 303 KLVRMlgNI-----QAMFLVgwrlcklyESGKMTPG------HASLGKAWITKKARETVALGRELLGGNGILADFLVAKA 371

                        410       420
                 ....*....|....*....|....*...
gi 281363737 425 LRDLRIFRIFEGTNDILRLFIA--LTGI 450
Cdd:PLN02526 372 FCDLEPIYTYEGTYDINALVTGreITGI 399
PTZ00456 PTZ00456
acyl-CoA dehydrogenase; Provisional
 108-440 1.74e-25

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185635 [Multi-domain]  Cd Length: 622  Bit Score: 111.50  E-value: 1.74e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 108 ALWELGAFGIQVPSEFGGLGLNNTQYGRLCAIVGVNDLGLGITIGahQSIG-FKGILLYGTPEQKEKYLPKVAAEQVYAA 186
Cdd:PTZ00456 107 ALKAGGWTGISEPEEYGGQALPLSVGFITRELMATANWGFSMYPG--LSIGaANTLMAWGSEEQKEQYLTKLVSGEWSGT 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 187 FALTEPSSGSDAGSIRCRAVKSADGKhYVLNGSKIWISNG--GIAE--IMTVFAQTEQVDPKTgekKDkVTAFIVER--- 259
Cdd:PTZ00456 185 MCLTEPQCGTDLGQVKTKAEPSADGS-YKITGTKIFISAGdhDLTEniVHIVLARLPNSLPTT---KG-LSLFLVPRhvv 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 260 -------SFGGVTNGPPEKKMGIKASNTAEVYFEDVKipiENVLGKEGDGFKVAMNILNNGRfgMGATLSG------TMK 326
Cdd:PTZ00456 260 kpdgsleTAKNVKCIGLEKKMGIKGSSTCQLSFENSV---GYLIGEPNAGMKQMFTFMNTAR--VGTALEGvchaelAFQ 334

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 327 KCIEQATEHANNRVQFGQK--------LKNYGSIQEKLAQMNILQYATESMAFTISQNMD--AGSKDYHLEAA------- 389
Cdd:PTZ00456 335 NALRYARERRSMRALSGTKepekpadrIICHANVRQNILFAKAVAEGGRALLLDVGRLLDihAAAKDAATREAldheigf 414

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 281363737 390 ---ISKIYASESAWYVCDEAIQILGGMGYMVDNGLERVLRDLRIFRIFEGTNDI 440
Cdd:PTZ00456 415 ytpIAKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGI 468
PTZ00457 PTZ00457
acyl-CoA dehydrogenase; Provisional
 45-587 1.10e-23

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185636 [Multi-domain]  Cd Length: 520  Bit Score: 104.96  E-value: 1.10e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737  45 SFMANIFRGSLVSSQVFPYPD-VLTAEQKELTNSLIDPFERFFSDVNDAArndanskiddttstalwelgafGIQVPSEF 123
Cdd:PTZ00457  17 SYAAGLFNFKIVPEEMFPYPCrKLDGDEAENLQSLLEQIRSNDKILGNLY----------------------GARIATEY 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 124 GGLGLNNTQYGRLCAIVGVNdlGLGITIGAHQSIGFKGILL--YGTPEQKEKYLPKVAAEQVYAAFAlTEPSSGSDAGSI 201
Cdd:PTZ00457  75 GGLGLGHTAHALIYEEVGTN--CDSKLLSTIQHSGFCTYLLstVGSKELKGKYLTAMSDGTIMMGWA-TEEGCGSDISMN 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 202 RCRAVKSADGKhYVLNGSKIWISNGGIAEIMTVFAQTEQVDPKTGEKK-DKVTAFIVERSFGGVTngppekkmgikaSNT 280
Cdd:PTZ00457 152 TTKASLTDDGS-YVLTGQKRCEFAASATHFLVLAKTLTQTAAEEGATEvSRNSFFICAKDAKGVS------------VNG 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 281 AEVYFEDVkiPIENVLGKEGDGFKVAMNILNNGRFGMGATLSGTMKKCIEQATEHANNRvqfgqklknygSIQEKLAQMN 360
Cdd:PTZ00457 219 DSVVFENT--PAADVVGVVGEGFKDAMITLFTEQYLYAASLLGIMKRVVQELRGSNAEE-----------GATDTVASFA 285

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 361 ILQYATESMAFTISQNMDAGSKDYHLEAAISKIYASESawyvcdeaiqilggmgymvdnglerVLRDLRIFRIFEGTNDI 440
Cdd:PTZ00457 286 CAMYAMESTLYALTANLDLPTEDSLLECTLVSAFVQST-------------------------TNQLLSILETATPPSTT 340

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 441 LRLFIAltgiqYAGSHLKEL-QRAFKNPSA------NLGLIFKEASR------RAASTVGlggtdLSGHVVGELLPYAKK 507
Cdd:PTZ00457 341 LEKCFA-----NARLFLSMMeSRDFLYSSAvccgveDYGLFFQRASTlqmmqaRTLRSLG-----VRDRVPIKNLPDCSL 410

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 508 TAHCIDLFGQSVEELLLRYNKNIVNEQILLTRLANAAIDIYAMVVTQSRSSRAVNLNLPTAQHELNMTKALTIQASDRVI 587
Cdd:PTZ00457 411 IDEAVVAFGNAVEATFVRSGSQVPYQQLLLNRLGEAASLLYAASAVASRASMCVSKGLPSAKVEGELASAFIAMAVSRAR 490
Acyl-CoA_dh_N pfam02771
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ...
 68-180 2.20e-20

Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is an all-alpha domain.


Pssm-ID: 460686 [Multi-domain]  Cd Length: 113  Bit Score: 86.75  E-value: 2.20e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737   68 TAEQKELtnslIDPFERFFSDV--NDAARNDANSKIDDTTSTALWELGAFGIQVPSEFGGLGLNNTQYGRLCAIVGVNDL 145
Cdd:pfam02771   1 TEEQEAL----RDTVREFAEEEiaPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADA 76

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 281363737  146 GLGITIGAHQSIGFKGILLYGTPEQKEKYLPKVAA 180
Cdd:pfam02771  77 SVALALSVHSSLGAPPILRFGTEEQKERYLPKLAS 111
PRK13026 PRK13026
acyl-CoA dehydrogenase; Reviewed
 113-414 5.65e-20

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 237277 [Multi-domain]  Cd Length: 774  Bit Score: 94.25  E-value: 5.65e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 113 GAFGIQVPSEFGGLGLNNTQYGRLCAIVGVNDLGLGITIGAHQSIGfKGILL--YGTPEQKEKYLPKVAAEQVYAAFALT 190
Cdd:PRK13026 121 GFFALIIPKEYGGKGFSAYANSTIVSKIATRSVSAAVTVMVPNSLG-PGELLthYGTQEQKDYWLPRLADGTEIPCFALT 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 191 EPSSGSDAGSIR-----CRavKSADGKHYV---LNGSKIWISnggIAEIMTVFAQTEQV-DPK--TGEKKD-KVTAFIVE 258
Cdd:PRK13026 200 GPEAGSDAGAIPdtgivCR--GEFEGEEVLglrLTWDKRYIT---LAPVATVLGLAFKLrDPDglLGDKKElGITCALIP 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 259 RSFGGVTNGPPEKKMGIKASNtAEVYFEDVKIPIENVLG---KEGDGFKVAMNILNNGRfGMG----ATLSGTMkkCIEQ 331
Cdd:PRK13026 275 TDHPGVEIGRRHNPLGMAFMN-GTTRGKDVFIPLDWIIGgpdYAGRGWRMLVECLSAGR-GISlpalGTASGHM--ATRT 350

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 332 ATEHANNRVQFGQKLKNYGSIQEKLAQMNILQYATESMAFTISQNMDAGSKDyHLEAAISKIYASESAWYVCDEAIQILG 411
Cdd:PRK13026 351 TGAYAYVRRQFGMPIGQFEGVQEALARIAGNTYLLEAARRLTTTGLDLGVKP-SVVTAIAKYHMTELARDVVNDAMDIHA 429


                 ...
gi 281363737 412 GMG 414
Cdd:PRK13026 430 GKG 432
AXO cd01150
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ...
 140-465 1.75e-19

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: 92.39  E-value: 1.75e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 140 VGVNDLGLGITIGAHQSIGFKGILLYGTPEQKEKYLPKVAAEQVYAAFALTEPSSGSDAGSIRCRAVKSADGKHYVLN-- 217
Cdd:cd01150   91 LGGYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATYDPLTQEFVINtp 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 218 ---GSKIWISNGGI-AEIMTVFAQTeqvdpKTGEKKDKVTAFIVE-------RSFGGVTNGPPEKKMGIKASNTAEVYFE 286
Cdd:cd01150  171 dftATKWWPGNLGKtATHAVVFAQL-----ITPGKNHGLHAFIVPirdpkthQPLPGVTVGDIGPKMGLNGVDNGFLQFR 245

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 287 DVKIPIENVLGKEGD----------------GFKVAMNILNNGRFGMGATLSGTMKKCIEQATEHANNRVQFGQKLK--- 347
Cdd:cd01150  246 NVRIPRENLLNRFGDvspdgtyvspfkdpnkRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQFGPKPSdpe 325

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 348 ----NYGSIQEK----LAQMNILQYATESMAFTISQNMDAGS-------KDYHLEAAISKIYASesaWYvCDEAIQIL-- 410
Cdd:cd01150  326 vqilDYQLQQYRlfpqLAAAYAFHFAAKSLVEMYHEIIKELLqgnsellAELHALSAGLKAVAT---WT-AAQGIQECre 401

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 281363737 411 --GGMGYMVDNGLERVLRDLRIFRIFEGTNDILRLfialtgiQYAGSHLKELQRAFK 465
Cdd:cd01150  402 acGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQ-------QTANYLLKKYAQAFS 451
fadE PRK09463
acyl-CoA dehydrogenase; Reviewed
 113-414 3.19e-19

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 236528 [Multi-domain]  Cd Length: 777  Bit Score: 92.19  E-value: 3.19e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 113 GAFGIQVPSEFGGLGLNNTQYGRLCAIVGVNDLGLGITIGAHQSIGfKGILL--YGTPEQKEKYLPKVAAEQVYAAFALT 190
Cdd:PRK09463 122 GFFGMIIPKEYGGLEFSAYAHSRVLQKLASRSGTLAVTVMVPNSLG-PGELLlhYGTDEQKDHYLPRLARGEEIPCFALT 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 191 EPSSGSDAGSIR-----CRAVKSADGKHYV-LNGSKIWISNGGIAeimTVFAQTEQV-DPK--TGEKKD-KVTAFIVERS 260
Cdd:PRK09463 201 SPEAGSDAGSIPdtgvvCKGEWQGEEVLGMrLTWNKRYITLAPIA---TVLGLAFKLyDPDglLGDKEDlGITCALIPTD 277

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 261 FGGVT-------------NGPPEKKmgikasntaevyfeDVKIPIENVLGKE---GDGFKVAMNILNNGRfgmGATL--S 322
Cdd:PRK09463 278 TPGVEigrrhfplnvpfqNGPTRGK--------------DVFIPLDYIIGGPkmaGQGWRMLMECLSVGR---GISLpsN 340

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 323 GT-MKKCIEQAT-EHANNRVQFGQKLKNYGSIQEKLAQMNILQYATESMAFTISQNMDAGSKDYHLeAAISKIYASESAW 400
Cdd:PRK09463 341 STgGAKLAALATgAYARIRRQFKLPIGKFEGIEEPLARIAGNAYLMDAARTLTTAAVDLGEKPSVL-SAIAKYHLTERGR 419

                        330
                 ....*....|....
gi 281363737 401 YVCDEAIQILGGMG 414
Cdd:PRK09463 420 QVINDAMDIHGGKG 433
PLN02636 PLN02636
acyl-coenzyme A oxidase
 140-465 1.09e-16

acyl-coenzyme A oxidase


Pssm-ID: 215342 [Multi-domain]  Cd Length: 686  Bit Score: 83.75  E-value: 1.09e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 140 VGVNDLGLGITIGAHQSIGFKGILLYGTPEQKEKYLPKVAAEQVYAAFALTEPSSGSDAGSIRCRAVKSADGKHYVLN-- 217
Cdd:PLN02636 130 VGSVDMSLGIKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFDPLTDEFVINtp 209

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 218 ---GSKIWISNGGI-AEIMTVFAQTEQVDPKTGEKKDK-VTAFIV-------ERSFGGVTNGPPEKKMGIKASNTAEVYF 285
Cdd:PLN02636 210 ndgAIKWWIGNAAVhGKFATVFARLKLPTHDSKGVSDMgVHAFIVpirdmktHQVLPGVEIRDCGHKVGLNGVDNGALRF 289

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 286 EDVKIPIENVLGKEGD----------------GFKVAMNILNNGRFGMGATLSGTMKKCIEQATEHANNRVQFGQKLK-- 347
Cdd:PLN02636 290 RSVRIPRDNLLNRFGDvsrdgkytsslptinkRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQFGPPKQpe 369

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 348 ----NYGSIQEKLAQM----NILQYATESMAFTISQ----NMDAGSKDYHLEAAISKIYASE---SAWYVCDEAIqilGG 412
Cdd:PLN02636 370 isilDYQSQQHKLMPMlastYAFHFATEYLVERYSEmkktHDDQLVADVHALSAGLKAYITSytaKALSTCREAC---GG 446

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 281363737 413 MGYMVDNGLERVLRDLRIFRIFEGTNDILRLfialtgiQYAGSHLKELQRAFK 465
Cdd:PLN02636 447 HGYAAVNRFGSLRNDHDIFQTFEGDNTVLLQ-------QVAADLLKQYKEKFQ 492
PRK11561 PRK11561
isovaleryl CoA dehydrogenase; Provisional
 189-451 3.96e-12

isovaleryl CoA dehydrogenase; Provisional


Pssm-ID: 183199 [Multi-domain]  Cd Length: 538  Bit Score: 69.01  E-value: 3.96e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 189 LTEPSSGSDAGSIRCRAVKSADGKhYVLNGSKiWISNGGIAEIMTVFAQTEQvdpktgekkdKVTAFIVERSF-GGVTNG 267
Cdd:PRK11561 184 MTEKQGGSDVLSNTTRAERLADGS-YRLVGHK-WFFSVPQSDAHLVLAQAKG----------GLSCFFVPRFLpDGQRNA 251

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 268 PP----EKKMGIKASNTAEVYFEDVkipIENVLGKEGDGFKvamNILNNG---RFGMGATLSGTMKKCIEQATEHANNRV 340
Cdd:PRK11561 252 IRlerlKDKLGNRSNASSEVEFQDA---IGWLLGEEGEGIR---LILKMGgmtRFDCALGSHGLMRRAFSVAIYHAHQRQ 325

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 341 QFGQKLKNYGSIQEKLAQMNILQYATESMAFTISQNMDAgSKDYHlEAAISKIYASESAWYVCD-------EAIQILGGM 413
Cdd:PRK11561 326 VFGKPLIEQPLMRQVLSRMALQLEGQTALLFRLARAWDR-RADAK-EALWARLFTPAAKFVICKrgipfvaEAMEVLGGI 403

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 281363737 414 GYMVDNGLERVLRDLRIFRIFEGTN-----DILRLFIALTGIQ 451
Cdd:PRK11561 404 GYCEESELPRLYREMPVNSIWEGSGnimclDVLRVLNKQPGVY 446
DszC cd01163
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ...
 108-298 1.49e-07

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: 53.87  E-value: 1.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 108 ALWELGAFGIQVPSEFGGLGLNNTQYGRLCAIVGVNDLGLGITIGAHqsIGF-KGILLYGTPEQKEKYLPKVAAEQVYAA 186
Cdd:cd01163   30 LLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALRAH--FGFvEALLLAGPEQFRKRWFGRVLNGWIFGN 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 187 fALTEPSSGSDAGSIRcraVKSADGKHYVLNGSKIWISNGGIAEIMTVFAQTEQvdpktgekkDKVTAFIVERSFGGVT- 265
Cdd:cd01163  108 -AVSERGSVRPGTFLT---ATVRDGGGYVLNGKKFYSTGALFSDWVTVSALDEE---------GKLVFAAVPTDRPGITv 174

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 281363737 266 ----NGppekkMGIK--ASNTAEvyFEDVKIPIENVLGK 298
Cdd:cd01163  175 vddwDG-----FGQRltASGTVT--FDNVRVEPDEVLPR 206
Acyl-CoA_dh_2 pfam08028
Acyl-CoA dehydrogenase, C-terminal domain;
323-438 1.79e-07

Acyl-CoA dehydrogenase, C-terminal domain;


Pssm-ID: 429790 [Multi-domain]  Cd Length: 133  Bit Score: 50.42  E-value: 1.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737  323 GTMKKCIEQATEHANNRVQ--FGQKLKNYGSIQEKLAQMNI----LQYATESMAFTISQNMDAGSK---DYHLEAAISKI 393
Cdd:pfam08028   8 GAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAAridaARLLLERAAARIEAAAAAGKPvtpALRAEARRAAA 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 281363737  394 YASESAWYVCDEAIQILGGMGYMVDNGLERVLRDLRIFRIFEGTN 438
Cdd:pfam08028  88 FATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVN 132
PTZ00460 PTZ00460
acyl-CoA dehydrogenase; Provisional
 166-469 2.70e-06

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185639 [Multi-domain]  Cd Length: 646  Bit Score: 50.61  E-value: 2.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 166 GTPEQKEKYLPKVAAEQVYAAFALTEPSSGSDAGSIRCRAVKSADGKHYVLN-----GSKIWISN-GGIAEIMTVFAQTe 239
Cdd:PTZ00460 110 GTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATYDKQTNEFVIHtpsveAVKFWPGElGFLCNFALVYAKL- 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 240 QVDPKTgekkDKVTAFIVE-------RSFGGVTNGPPEKKMGIKASNTAEVYFEDVKIPIENVLGKegdgfkvAMNILNN 312
Cdd:PTZ00460 189 IVNGKN----KGVHPFMVRirdkethKPLQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLAR-------YIKVSED 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 313 GRF--------GMGATL----------SGTMKKCIEQATEHANNRVQFGQKLKNYGSIQE-KLAQMNILQYATE--SMAF 371
Cdd:PTZ00460 258 GQVerqgnpkvSYASMMymrnliidqyPRFAAQALTVAIRYSIYRQQFTNDNKQENSVLEyQTQQQKLLPLLAEfyACIF 337

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 372 T---ISQNMDAG-----SKDYHL----EAAISKIYASESAWYV-CDEAIQI-LGGMGYMVDNGLERVLRDLRIFRIFEGT 437
Cdd:PTZ00460 338 GglkIKELVDDNfnrvqKNDFSLlqltHAILSAAKANYTYFVSnCAEWCRLsCGGHGYAHYSGLPAIYFDMSPNITLEGE 417

                        330       340       350
                 ....*....|....*....|....*....|..
gi 281363737 438 NDILRLfialtgiQYAGSHLKELQRAFKNPSA 469
Cdd:PTZ00460 418 NQIMYL-------QLARYLLKQLQHAVQKPEK 442
NcnH cd01159
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ...
 92-429 7.91e-06

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: 48.50  E-value: 7.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737  92 AARNDANSKIDDTTSTALWELGAFGIQVPSEFGGLGLNNTQYGRLCAIVGvndlglgitiGAHQSIGFkGILLYGTPEQK 171
Cdd:cd01159   14 APEAERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLA----------EACGSAAW-VASIVATHSRM 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 172 EKYLPKVAAEQVYAafaltEPSSGSDAGSIR--CRAVKSADGkhYVLNGSKIWISNGGIAEIMTVFAQTEqvdpKTGEKK 249
Cdd:cd01159   83 LAAFPPEAQEEVWG-----DGPDTLLAGSYApgGRAERVDGG--YRVSGTWPFASGCDHADWILVGAIVE----DDDGGP 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 250 DkVTAFIVERSfgGVTNGPPEKKMGIKASNTAEVYFEDVKIPIENVL-----------GKEGDGFKVAMNILNNgrFGMG 318
Cdd:cd01159  152 L-PRAFVVPRA--EYEIVDTWHVVGLRGTGSNTVVVDDVFVPEHRTLtagdmmagdgpGGSTPVYRMPLRQVFP--LSFA 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 319 ATLSGTMKKCIEQATEHANNRVQ---FGQKLKNYGSIQEKLAQMNILQYATESMAFTISQNMDAGSKDYHLEAAISKIYA 395
Cdd:cd01159  227 AVSLGAAEGALAEFLELAGKRVRqygAAVKMAEAPITQLRLAEAAAELDAARAFLERATRDLWAHALAGGPIDVEERARI 306

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 281363737 396 SESAWYV---CDEAIQIL----GGMGYMVDNGLERVLRDLR 429
Cdd:cd01159  307 RRDAAYAaklSAEAVDRLfhaaGGSALYTASPLQRIWRDIH 347
PLN02443 PLN02443
acyl-coenzyme A oxidase
 126-446 4.52e-05

acyl-coenzyme A oxidase


Pssm-ID: 178062 [Multi-domain]  Cd Length: 664  Bit Score: 46.37  E-value: 4.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 126 LGLNNTQYGRLCAIV---GVNDLGLGITIGAhqsigFKGillYGTPEQKEKYLPKVAAEQVYAAFALTEPSSGSDAGSIR 202
Cdd:PLN02443  79 LRLTEEEAGKLRSFVdepGYTDLHWGMFVPA-----IKG---QGTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLE 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 203 CRAVKSADGKHYVLN-----GSKIWisNGGIAEIMT---VFAQTeqvdpKTGEKKDKVTAFIVE-RSFG------GVTNG 267
Cdd:PLN02443 151 TTATFDPKTDEFVIHsptltSSKWW--PGGLGKVSThavVYARL-----ITNGKDHGIHGFIVQlRSLDdhsplpGVTVG 223

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 268 PPEKKMGIKASNTAE---VYFEDVKIPIENVLGKEG----DGFKVAMNI---LNNG-----RFGMGATLSGTMKKCIEQA 332
Cdd:PLN02443 224 DIGMKFGNGAYNTMDngfLRFDHVRIPRDQMLMRLSkvtrEGKYVQSDVprqLVYGtmvyvRQTIVADASTALSRAVCIA 303

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 333 TEHANNRVQFGQK-------LKNYGSIQEKLAQMNILQYATESMAF-------TISQNMDAgsKDY------HLEAAISK 392
Cdd:PLN02443 304 TRYSAVRRQFGSQdggpetqVIDYKTQQSRLFPLLASAYAFRFVGEwlkwlytDVTQRLEA--NDFstlpeaHACTAGLK 381

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 281363737 393 IYASESAWYVCDEAIQILGGMGYMVDNGLERVLRDLRIFRIFEGTNDILRLFIA 446
Cdd:PLN02443 382 SLTTSATADGIEECRKLCGGHGYLCSSGLPELFAVYVPACTYEGDNVVLLLQVA 435
PLN02312 PLN02312
acyl-CoA oxidase
 136-301 7.44e-05

acyl-CoA oxidase


Pssm-ID: 215178 [Multi-domain]  Cd Length: 680  Bit Score: 45.92  E-value: 7.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 136 LCAIVGVNDLGLGITIGAHQSIGFKGILLYGTPEQKEKYLPKVAAEQVYAAFALTEPSSGSDAGSIRCRAVKSADGKHYV 215
Cdd:PLN02312 138 LLEVIGIYDHSLAIKLGVHFFLWGGAIKFLGTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTTYDPKTEEFV 217

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363737 216 LN-----GSKIWIsnGGIAEIMT---VFAQTEqvdpkTGEKKDKVTAFIVE------RSFGGVTNGPPEKKMGIKASNTA 281
Cdd:PLN02312 218 INtpcesAQKYWI--GGAANHAThtiVFSQLH-----INGKNEGVHAFIAQirdqdgNICPNIRIADCGHKIGLNGVDNG 290

                        170       180
                 ....*....|....*....|
gi 281363737 282 EVYFEDVKIPIENVLGKEGD 301
Cdd:PLN02312 291 RIWFDNLRIPRENLLNSVAD 310
 
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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