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Conserved domains on  [gi|1301392927|gb|PKB60788|]
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hypothetical protein BZY64_00155 [SAR202 cluster bacterium Ae2-Chloro-G1]

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 ...
7-377 4.38e-75

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 cd01159:

Pssm-ID: 447864 [Multi-domain]  Cd Length: 370  Bit Score: 237.25  E-value: 4.38e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392927   7 QAAEKLAPVIAENVSRIDSERQLPPELAKLMADENLFGLYVPKILGGPELDPLTAFYVVEEISKIDGSAGWCcfngSTIT 86
Cdd:cd01159     1 ARAEDLAPLIRERAPEAERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSAAWV----ASIV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392927  87 SGISRV----SESAGKEIIGESGILAGSGSARPEGVSKVTPGGFLISGRWNYLSGIDHSNVLFLNsfvvdenGPMTSDNG 162
Cdd:cd01159    77 ATHSRMlaafPPEAQEEVWGDGPDTLLAGSYAPGGRAERVDGGYRVSGTWPFASGCDHADWILVG-------AIVEDDDG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392927 163 ARLTRTVIVPVESGKVIDTWDTVGMRGTASNDAEFSDVFVPVEHTYVRGDPSYHDNPLYSsqTAIH-------IGWTLAA 235
Cdd:cd01159   150 GPLPRAFVVPRAEYEIVDTWHVVGLRGTGSNTVVVDDVFVPEHRTLTAGDMMAGDGPGGS--TPVYrmplrqvFPLSFAA 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392927 236 AnSLGMARGAMNCFVEMATSRGTANSRT-LMRDRSVVQTVVGECEAIIDGARSFVIDAVASMWDCQRTG--NGDLERkaL 312
Cdd:cd01159   228 V-SLGAAEGALAEFLELAGKRVRQYGAAvKMAEAPITQLRLAEAAAELDAARAFLERATRDLWAHALAGgpIDVEER--A 304
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1301392927 313 RTRLAITHAIRQSSQAVDRLFHVAGVNAIHESLGLARFFRDLKVSVQHISGL-ENNYEFGGQSLMG 377
Cdd:cd01159   305 RIRRDAAYAAKLSAEAVDRLFHAAGGSALYTASPLQRIWRDIHAAAQHAALNpETAAEAYGRALLG 370
 
Name Accession Description Interval E-value
NcnH cd01159
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ...
7-377 4.38e-75

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: 237.25  E-value: 4.38e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392927   7 QAAEKLAPVIAENVSRIDSERQLPPELAKLMADENLFGLYVPKILGGPELDPLTAFYVVEEISKIDGSAGWCcfngSTIT 86
Cdd:cd01159     1 ARAEDLAPLIRERAPEAERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSAAWV----ASIV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392927  87 SGISRV----SESAGKEIIGESGILAGSGSARPEGVSKVTPGGFLISGRWNYLSGIDHSNVLFLNsfvvdenGPMTSDNG 162
Cdd:cd01159    77 ATHSRMlaafPPEAQEEVWGDGPDTLLAGSYAPGGRAERVDGGYRVSGTWPFASGCDHADWILVG-------AIVEDDDG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392927 163 ARLTRTVIVPVESGKVIDTWDTVGMRGTASNDAEFSDVFVPVEHTYVRGDPSYHDNPLYSsqTAIH-------IGWTLAA 235
Cdd:cd01159   150 GPLPRAFVVPRAEYEIVDTWHVVGLRGTGSNTVVVDDVFVPEHRTLTAGDMMAGDGPGGS--TPVYrmplrqvFPLSFAA 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392927 236 AnSLGMARGAMNCFVEMATSRGTANSRT-LMRDRSVVQTVVGECEAIIDGARSFVIDAVASMWDCQRTG--NGDLERkaL 312
Cdd:cd01159   228 V-SLGAAEGALAEFLELAGKRVRQYGAAvKMAEAPITQLRLAEAAAELDAARAFLERATRDLWAHALAGgpIDVEER--A 304
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1301392927 313 RTRLAITHAIRQSSQAVDRLFHVAGVNAIHESLGLARFFRDLKVSVQHISGL-ENNYEFGGQSLMG 377
Cdd:cd01159   305 RIRRDAAYAAKLSAEAVDRLFHAAGGSALYTASPLQRIWRDIHAAAQHAALNpETAAEAYGRALLG 370
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
5-356 3.99e-31

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: 121.87  E-value: 3.99e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392927   5 LLQAAEKLAP-VIAENVSRIDSERQLPPELAKLMADENLFGLYVPKILGGPELDPLTAFYVVEEISKIDGSAGWCCFNGS 83
Cdd:COG1960    12 LRDEVREFAEeEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADASLALPVGVHN 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392927  84 TITSGISRV-SE----------SAGKEIIG----ESGilAGSG------SARPEGvskvtpGGFLISGRWNYLSGIDHSN 142
Cdd:COG1960    92 GAAEALLRFgTEeqkerylprlASGEWIGAfaltEPG--AGSDaaalrtTAVRDG------DGYVLNGQKTFITNAPVAD 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392927 143 VLFLnSFVVDEngpmtsDNGARLTRTVIVPVES-G-KVIDTWDTVGMRGTASNDAEFSDVFVPVEhtYVRGDPsyhDNPL 220
Cdd:COG1960   164 VILV-LARTDP------AAGHRGISLFLVPKDTpGvTVGRIEDKMGLRGSDTGELFFDDVRVPAE--NLLGEE---GKGF 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392927 221 YSSQTAIHIGWTLAAANSLGMARGAMNCFVEMATSRgTANSRTLMRDrSVVQTVVGECEAIIDGARSFVIDAvASMWDcq 300
Cdd:COG1960   232 KIAMSTLNAGRLGLAAQALGIAEAALELAVAYARER-EQFGRPIADF-QAVQHRLADMAAELEAARALVYRA-AWLLD-- 306
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1301392927 301 rtgngdlERKALRTRLAI--THAIRQSSQAVDRLFHVAGVNAIHESLGLARFFRDLKV 356
Cdd:COG1960   307 -------AGEDAALEAAMakLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARI 357
Acyl-CoA_dh_2 pfam08028
Acyl-CoA dehydrogenase, C-terminal domain;
235-361 4.73e-23

Acyl-CoA dehydrogenase, C-terminal domain;


Pssm-ID: 429790 [Multi-domain]  Cd Length: 133  Bit Score: 93.56  E-value: 4.73e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392927 235 AANSLGMARGAMNCFVEMATSRGTANSRTLMRDRSVVQTVVGECEAIIDGARSFVIDAVASMWDCQRTGNGDLERKALRT 314
Cdd:pfam08028   3 AAAALGAARAALAEFTERARGRVRAYFGVPLAEDPATQLALAEAAARIDAARLLLERAAARIEAAAAAGKPVTPALRAEA 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1301392927 315 RLAITHAIRQSSQAVDRLFHVAGVNAIHESLGLARFFRDLKVSVQHI 361
Cdd:pfam08028  83 RRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHA 129
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
4-206 9.04e-05

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 44.10  E-value: 9.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392927   4 TLLQAAEKLAPVIAENV----SRIDSERQLPPE--LAKLMADENLFGLYVPKILGGPELDPLTAFYVVEEISKIDGSAGW 77
Cdd:PLN02519   29 TQLQFKESVQQFAQENIaphaAAIDATNSFPKDvnLWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGSVGL 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392927  78 C-------CFNGSTITSGISRVSESAGKEIIGES-GILA----GSGS------ARPEGVSkvtpGGFLISGRWNYLSGID 139
Cdd:PLN02519  109 SygahsnlCINQLVRNGTPAQKEKYLPKLISGEHvGALAmsepNSGSdvvsmkCKAERVD----GGYVLNGNKMWCTNGP 184
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1301392927 140 HSNVLFLNSfvvdengpmTSDNGARLTRTVIVPVESG----KVIDTWDTVGMRGTASNDAEFSDVFVPVEH 206
Cdd:PLN02519  185 VAQTLVVYA---------KTDVAAGSKGITAFIIEKGmpgfSTAQKLDKLGMRGSDTCELVFENCFVPEEN 246
 
Name Accession Description Interval E-value
NcnH cd01159
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ...
7-377 4.38e-75

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: 237.25  E-value: 4.38e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392927   7 QAAEKLAPVIAENVSRIDSERQLPPELAKLMADENLFGLYVPKILGGPELDPLTAFYVVEEISKIDGSAGWCcfngSTIT 86
Cdd:cd01159     1 ARAEDLAPLIRERAPEAERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSAAWV----ASIV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392927  87 SGISRV----SESAGKEIIGESGILAGSGSARPEGVSKVTPGGFLISGRWNYLSGIDHSNVLFLNsfvvdenGPMTSDNG 162
Cdd:cd01159    77 ATHSRMlaafPPEAQEEVWGDGPDTLLAGSYAPGGRAERVDGGYRVSGTWPFASGCDHADWILVG-------AIVEDDDG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392927 163 ARLTRTVIVPVESGKVIDTWDTVGMRGTASNDAEFSDVFVPVEHTYVRGDPSYHDNPLYSsqTAIH-------IGWTLAA 235
Cdd:cd01159   150 GPLPRAFVVPRAEYEIVDTWHVVGLRGTGSNTVVVDDVFVPEHRTLTAGDMMAGDGPGGS--TPVYrmplrqvFPLSFAA 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392927 236 AnSLGMARGAMNCFVEMATSRGTANSRT-LMRDRSVVQTVVGECEAIIDGARSFVIDAVASMWDCQRTG--NGDLERkaL 312
Cdd:cd01159   228 V-SLGAAEGALAEFLELAGKRVRQYGAAvKMAEAPITQLRLAEAAAELDAARAFLERATRDLWAHALAGgpIDVEER--A 304
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1301392927 313 RTRLAITHAIRQSSQAVDRLFHVAGVNAIHESLGLARFFRDLKVSVQHISGL-ENNYEFGGQSLMG 377
Cdd:cd01159   305 RIRRDAAYAAKLSAEAVDRLFHAAGGSALYTASPLQRIWRDIHAAAQHAALNpETAAEAYGRALLG 370
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
5-356 3.99e-31

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: 121.87  E-value: 3.99e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392927   5 LLQAAEKLAP-VIAENVSRIDSERQLPPELAKLMADENLFGLYVPKILGGPELDPLTAFYVVEEISKIDGSAGWCCFNGS 83
Cdd:COG1960    12 LRDEVREFAEeEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADASLALPVGVHN 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392927  84 TITSGISRV-SE----------SAGKEIIG----ESGilAGSG------SARPEGvskvtpGGFLISGRWNYLSGIDHSN 142
Cdd:COG1960    92 GAAEALLRFgTEeqkerylprlASGEWIGAfaltEPG--AGSDaaalrtTAVRDG------DGYVLNGQKTFITNAPVAD 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392927 143 VLFLnSFVVDEngpmtsDNGARLTRTVIVPVES-G-KVIDTWDTVGMRGTASNDAEFSDVFVPVEhtYVRGDPsyhDNPL 220
Cdd:COG1960   164 VILV-LARTDP------AAGHRGISLFLVPKDTpGvTVGRIEDKMGLRGSDTGELFFDDVRVPAE--NLLGEE---GKGF 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392927 221 YSSQTAIHIGWTLAAANSLGMARGAMNCFVEMATSRgTANSRTLMRDrSVVQTVVGECEAIIDGARSFVIDAvASMWDcq 300
Cdd:COG1960   232 KIAMSTLNAGRLGLAAQALGIAEAALELAVAYARER-EQFGRPIADF-QAVQHRLADMAAELEAARALVYRA-AWLLD-- 306
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1301392927 301 rtgngdlERKALRTRLAI--THAIRQSSQAVDRLFHVAGVNAIHESLGLARFFRDLKV 356
Cdd:COG1960   307 -------AGEDAALEAAMakLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARI 357
DszC cd01163
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ...
7-360 2.13e-26

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: 108.56  E-value: 2.13e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392927   7 QAAEKLAPVIAENVSRIDSERQLPPELAKLMADENLFGLYVPKILGGPELDPLTAFYVVEEISKIDGSAGWCCFNGSTIT 86
Cdd:cd01163     1 ARARPLAARIAEGAAERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALRAHFGFV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392927  87 SGISRVSESAGKE----IIGESGILAGS----GSARPEGVSKVT---PGGFLISGRWNYLSGIDHSNvlFLNSFVVDENG 155
Cdd:cd01163    81 EALLLAGPEQFRKrwfgRVLNGWIFGNAvserGSVRPGTFLTATvrdGGGYVLNGKKFYSTGALFSD--WVTVSALDEEG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392927 156 pmtsdngarltRTVIVPVESGK----VIDTWDTVGMRGTASNDAEFSDVFVPVEHTYVRGDPSYHDNPLYSSQTAIHigw 231
Cdd:cd01163   159 -----------KLVFAAVPTDRpgitVVDDWDGFGQRLTASGTVTFDNVRVEPDEVLPRPNAPDRGTLLTAIYQLVL--- 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392927 232 tlaAANSLGMARGAMNCFVEMATSRGTA---NSRTLMRDRSVVQTVVGECEAIIDGARSFVIDA---VASMWDcQRTGNG 305
Cdd:cd01163   225 ---AAVLAGIARAALDDAVAYVRSRTRPwihSGAESARDDPYVQQVVGDLAARLHAAEALVLQAaraLDAAAA-AGTALT 300
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1301392927 306 DLERKALRTRLAITHAI--RQSSQAVDRLFHVAGVNAIHESLGLARFFRDLKVSVQH 360
Cdd:cd01163   301 AEARGEAALAVAAAKVVvtRLALDATSRLFEVGGASATAREHNLDRHWRNARTHTLH 357
Acyl-CoA_dh_2 pfam08028
Acyl-CoA dehydrogenase, C-terminal domain;
235-361 4.73e-23

Acyl-CoA dehydrogenase, C-terminal domain;


Pssm-ID: 429790 [Multi-domain]  Cd Length: 133  Bit Score: 93.56  E-value: 4.73e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392927 235 AANSLGMARGAMNCFVEMATSRGTANSRTLMRDRSVVQTVVGECEAIIDGARSFVIDAVASMWDCQRTGNGDLERKALRT 314
Cdd:pfam08028   3 AAAALGAARAALAEFTERARGRVRAYFGVPLAEDPATQLALAEAAARIDAARLLLERAAARIEAAAAAGKPVTPALRAEA 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1301392927 315 RLAITHAIRQSSQAVDRLFHVAGVNAIHESLGLARFFRDLKVSVQHI 361
Cdd:pfam08028  83 RRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHA 129
ACAD cd00567
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
108-356 4.54e-17

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: 81.18  E-value: 4.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392927 108 AGSGSARPEGVSKVTPGGFLISGRWNYLSGIDHSNVLFLnsFVVdengpmTSDNGARLTRTVIVPVESG----KVIDTWD 183
Cdd:cd00567    80 AGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFIV--LAR------TDEEGPGHRGISAFLVPADtpgvTVGRIWD 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392927 184 TVGMRGTASNDAEFSDVFVPVEHtyVRGDPsyhDNPLYSSQTAIHIGWTLAAANSLGMARGAMNCFVEMATSRGTANSRt 263
Cdd:cd00567   152 KMGMRGSGTGELVFDDVRVPEDN--LLGEE---GGGFELAMKGLNVGRLLLAAVALGAARAALDEAVEYAKQRKQFGKP- 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392927 264 lMRDRSVVQTVVGECEAIIDGARSFVIDAVASMwdcqrtgngDLERKALRTRLAIT--HAIRQSSQAVDRLFHVAGVNAI 341
Cdd:cd00567   226 -LAEFQAVQFKLADMAAELEAARLLLYRAAWLL---------DQGPDEARLEAAMAklFATEAAREVADLAMQIHGGRGY 295
                         250
                  ....*....|....*
gi 1301392927 342 HESLGLARFFRDLKV 356
Cdd:cd00567   296 SREYPVERYLRDARA 310
Acyl-CoA_dh_N pfam02771
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ...
8-85 3.30e-11

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: 59.78  E-value: 3.30e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1301392927   8 AAEKLAPVIAEnvsrIDSERQLPPELAKLMADENLFGLYVPKILGGPELDPLTAFYVVEEISKIDGSAGWCCFNGSTI 85
Cdd:pfam02771  15 AEEEIAPHAAE----WDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVALALSVHSSL 88
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
8-356 4.96e-11

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: 63.44  E-value: 4.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392927   8 AAEKLAPVIAEnvsrIDSERQLPPELAKLMADENLFGLYVPKILGGPELDPLTAFYVVEEISKIDGSAG-WCCFNGSTIT 86
Cdd:cd01158    14 AEKEIAPLAAE----MDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAvIVSVHNSLGA 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392927  87 SGISRVSESAGK----------EIIG-----ESGilAGSGSARPEGVSKVTPGGFLISGRWNYLSGIDHSNVlflnsFVV 151
Cdd:cd01158    90 NPIIKFGTEEQKkkylpplatgEKIGafalsEPG--AGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADF-----YIV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392927 152 DEN-GPmtsDNGARLTRTVIVPVE-----SGKVIdtwDTVGMRGTASNDAEFSDVFVPVEHtyVRGDPSyhDNPLYSSQT 225
Cdd:cd01158   163 FAVtDP---SKGYRGITAFIVERDtpglsVGKKE---DKLGIRGSSTTELIFEDVRVPKEN--ILGEEG--EGFKIAMQT 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392927 226 --AIHIGwtlAAANSLGMARGAMNCFVEMATSR---GTAnsrtlMRDRSVVQTVVGECEAIIDGARSFVIDAvASMWDcq 300
Cdd:cd01158   233 ldGGRIG---IAAQALGIAQAALDAAVDYAKERkqfGKP-----IADFQGIQFKLADMATEIEAARLLTYKA-ARLKD-- 301
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1301392927 301 rtgNG-DLERKALRTRLAITH-AIRQSSQAVDRLfhvaGVNAIHESLGLARFFRDLKV 356
Cdd:cd01158   302 ---NGePFIKEAAMAKLFASEvAMRVTTDAVQIF----GGYGYTKDYPVERYYRDAKI 352
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
220-356 2.09e-05

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: 44.17  E-value: 2.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392927 220 LYSSQTAIHIGWTLAAANSLGMARGAMNCFVEMATSRgTANSRTLMrDRSVVQTVVGECEAIIDGARSFVIDAVASMWDC 299
Cdd:pfam00441   4 FRVAMETLNHERLAIAAMALGLARRALDEALAYARRR-KAFGRPLI-DFQLVRHKLAEMAAEIEAARLLVYRAAEALDAG 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1301392927 300 QRTGNGDLERKALRTRLAIthairqssQAVDRLFHVAGVNAIHESLGLARFFRDLKV 356
Cdd:pfam00441  82 GPDGAEASMAKLYASEAAV--------EVADLAMQLHGGYGYLREYPVERLYRDARV 130
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
4-206 9.04e-05

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 44.10  E-value: 9.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392927   4 TLLQAAEKLAPVIAENV----SRIDSERQLPPE--LAKLMADENLFGLYVPKILGGPELDPLTAFYVVEEISKIDGSAGW 77
Cdd:PLN02519   29 TQLQFKESVQQFAQENIaphaAAIDATNSFPKDvnLWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGSVGL 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392927  78 C-------CFNGSTITSGISRVSESAGKEIIGES-GILA----GSGS------ARPEGVSkvtpGGFLISGRWNYLSGID 139
Cdd:PLN02519  109 SygahsnlCINQLVRNGTPAQKEKYLPKLISGEHvGALAmsepNSGSdvvsmkCKAERVD----GGYVLNGNKMWCTNGP 184
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1301392927 140 HSNVLFLNSfvvdengpmTSDNGARLTRTVIVPVESG----KVIDTWDTVGMRGTASNDAEFSDVFVPVEH 206
Cdd:PLN02519  185 VAQTLVVYA---------KTDVAAGSKGITAFIIEKGmpgfSTAQKLDKLGMRGSDTCELVFENCFVPEEN 246
 
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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