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Conserved domains on  [gi|501228838|ref|WP_012271856|]
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MULTISPECIES: indole-3-acetate monooxygenase [Pseudomonas]

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 ...
21-381 1.23e-101

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: 305.43  E-value: 1.23e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501228838  21 EALLDGVRDRArlGEFDRQRHISRDVIDAFKAHGVYRALVPKRFGGLECSPAAFCEMIERIAHADGSAGWVASF-GMSPV 99
Cdd:cd01159    4 EDLAPLIRERA--PEAERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSAAWVASIvATHSR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501228838 100 YLAALPLDTIAEIYGNSPDTVFAGGIFPPQPAETVPGGFKVNGRWKYSSGSMGADIVGVGITPRNGDKLDLPRLAVLPRS 179
Cdd:cd01159   82 MLAAFPPEAQEEVWGDGPDTLLAGSYAPGGRAERVDGGYRVSGTWPFASGCDHADWILVGAIVEDDDGGPLPRAFVVPRA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501228838 180 QARIEETWDTVGLLGTGSHDLVVEDVRVGEQWTF-----VRGGKPNLDEPFFRYPSLSFATQVLSVVGLGIARAALDELS 254
Cdd:cd01159  162 EYEIVDTWHVVGLRGTGSNTVVVDDVFVPEHRTLtagdmMAGDGPGGSTPVYRMPLRQVFPLSFAAVSLGAAEGALAEFL 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501228838 255 GMASGRISVTGAPA-LADRPLAQVDVAKAEAALRSARAFFYEAIEQAWGHVLAGDPVPVEVTNLLRLSSTHAARVAAEVA 333
Cdd:cd01159  242 ELAGKRVRQYGAAVkMAEAPITQLRLAEAAAELDAARAFLERATRDLWAHALAGGPIDVEERARIRRDAAYAAKLSAEAV 321
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 501228838 334 RSAQLLSGMTGIYNESPLARCVNDAQVVTQHAFM-GDVTYQNAGAMFFG 381
Cdd:cd01159  322 DRLFHAAGGSALYTASPLQRIWRDIHAAAQHAALnPETAAEAYGRALLG 370
 
Name Accession Description Interval E-value
NcnH cd01159
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ...
21-381 1.23e-101

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: 305.43  E-value: 1.23e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501228838  21 EALLDGVRDRArlGEFDRQRHISRDVIDAFKAHGVYRALVPKRFGGLECSPAAFCEMIERIAHADGSAGWVASF-GMSPV 99
Cdd:cd01159    4 EDLAPLIRERA--PEAERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSAAWVASIvATHSR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501228838 100 YLAALPLDTIAEIYGNSPDTVFAGGIFPPQPAETVPGGFKVNGRWKYSSGSMGADIVGVGITPRNGDKLDLPRLAVLPRS 179
Cdd:cd01159   82 MLAAFPPEAQEEVWGDGPDTLLAGSYAPGGRAERVDGGYRVSGTWPFASGCDHADWILVGAIVEDDDGGPLPRAFVVPRA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501228838 180 QARIEETWDTVGLLGTGSHDLVVEDVRVGEQWTF-----VRGGKPNLDEPFFRYPSLSFATQVLSVVGLGIARAALDELS 254
Cdd:cd01159  162 EYEIVDTWHVVGLRGTGSNTVVVDDVFVPEHRTLtagdmMAGDGPGGSTPVYRMPLRQVFPLSFAAVSLGAAEGALAEFL 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501228838 255 GMASGRISVTGAPA-LADRPLAQVDVAKAEAALRSARAFFYEAIEQAWGHVLAGDPVPVEVTNLLRLSSTHAARVAAEVA 333
Cdd:cd01159  242 ELAGKRVRQYGAAVkMAEAPITQLRLAEAAAELDAARAFLERATRDLWAHALAGGPIDVEERARIRRDAAYAAKLSAEAV 321
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 501228838 334 RSAQLLSGMTGIYNESPLARCVNDAQVVTQHAFM-GDVTYQNAGAMFFG 381
Cdd:cd01159  322 DRLFHAAGGSALYTASPLQRIWRDIHAAAQHAALnPETAAEAYGRALLG 370
Acyl-CoA_dh_2 pfam08028
Acyl-CoA dehydrogenase, C-terminal domain;
237-367 1.55e-23

Acyl-CoA dehydrogenase, C-terminal domain;


Pssm-ID: 429790 [Multi-domain]  Cd Length: 133  Bit Score: 94.72  E-value: 1.55e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501228838  237 VLSVVGLGIARAALDELSGMASGRISVTGAPALADRPLAQVDVAKAEAALRSARAFFYEAIEQAWGHVLAGDPVPVEVTN 316
Cdd:pfam08028   1 GIAAAALGAARAALAEFTERARGRVRAYFGVPLAEDPATQLALAEAAARIDAARLLLERAAARIEAAAAAGKPVTPALRA 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 501228838  317 LLRLSSTHAARVAAEVARSAQLLSGMTGIYNESPLARCVNDAQVVTQHAFM 367
Cdd:pfam08028  81 EARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAV 131
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
18-362 1.85e-23

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: 100.30  E-value: 1.85e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501228838  18 PAFEALLDGVRD------RARLGEFDRQRHISRDVIDAFKAHGVYRALVPKRFGGLECSPAAFCEMIERIAHADGSAGW- 90
Cdd:COG1960    7 EEQRALRDEVREfaeeeiAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADASLALp 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501228838  91 --VASFGMSPVYLAALP------LDTIAeiygnSPDTVFAGGIFPPQP----------AETVPGGFKVNGRWKYSSGSMG 152
Cdd:COG1960   87 vgVHNGAAEALLRFGTEeqkeryLPRLA-----SGEWIGAFALTEPGAgsdaaalrttAVRDGDGYVLNGQKTFITNAPV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501228838 153 ADIVGVGITPRNGDKLDLPRLAVLPRSQA--RIEETWDTVGLLGTGSHDLVVEDVRVGEQWTFVRGGKPnldepfFRYP- 229
Cdd:COG1960  162 ADVILVLARTDPAAGHRGISLFLVPKDTPgvTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKG------FKIAm 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501228838 230 -SLSFATQVLSVVGLGIARAALDELSGMASGRIsVTGAPaLADRPLAQVDVAKAEAALRSARAFFYEAIEQawghVLAGD 308
Cdd:COG1960  236 sTLNAGRLGLAAQALGIAEAALELAVAYARERE-QFGRP-IADFQAVQHRLADMAAELEAARALVYRAAWL----LDAGE 309
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 501228838 309 PVPVEvTNLLRLSSTHAARVAAEVARsaQLLSGMtGIYNESPLARCVNDAQVVT 362
Cdd:COG1960  310 DAALE-AAMAKLFATEAALEVADEAL--QIHGGY-GYTREYPLERLYRDARILT 359
 
Name Accession Description Interval E-value
NcnH cd01159
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ...
21-381 1.23e-101

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: 305.43  E-value: 1.23e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501228838  21 EALLDGVRDRArlGEFDRQRHISRDVIDAFKAHGVYRALVPKRFGGLECSPAAFCEMIERIAHADGSAGWVASF-GMSPV 99
Cdd:cd01159    4 EDLAPLIRERA--PEAERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSAAWVASIvATHSR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501228838 100 YLAALPLDTIAEIYGNSPDTVFAGGIFPPQPAETVPGGFKVNGRWKYSSGSMGADIVGVGITPRNGDKLDLPRLAVLPRS 179
Cdd:cd01159   82 MLAAFPPEAQEEVWGDGPDTLLAGSYAPGGRAERVDGGYRVSGTWPFASGCDHADWILVGAIVEDDDGGPLPRAFVVPRA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501228838 180 QARIEETWDTVGLLGTGSHDLVVEDVRVGEQWTF-----VRGGKPNLDEPFFRYPSLSFATQVLSVVGLGIARAALDELS 254
Cdd:cd01159  162 EYEIVDTWHVVGLRGTGSNTVVVDDVFVPEHRTLtagdmMAGDGPGGSTPVYRMPLRQVFPLSFAAVSLGAAEGALAEFL 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501228838 255 GMASGRISVTGAPA-LADRPLAQVDVAKAEAALRSARAFFYEAIEQAWGHVLAGDPVPVEVTNLLRLSSTHAARVAAEVA 333
Cdd:cd01159  242 ELAGKRVRQYGAAVkMAEAPITQLRLAEAAAELDAARAFLERATRDLWAHALAGGPIDVEERARIRRDAAYAAKLSAEAV 321
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 501228838 334 RSAQLLSGMTGIYNESPLARCVNDAQVVTQHAFM-GDVTYQNAGAMFFG 381
Cdd:cd01159  322 DRLFHAAGGSALYTASPLQRIWRDIHAAAQHAALnPETAAEAYGRALLG 370
Acyl-CoA_dh_2 pfam08028
Acyl-CoA dehydrogenase, C-terminal domain;
237-367 1.55e-23

Acyl-CoA dehydrogenase, C-terminal domain;


Pssm-ID: 429790 [Multi-domain]  Cd Length: 133  Bit Score: 94.72  E-value: 1.55e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501228838  237 VLSVVGLGIARAALDELSGMASGRISVTGAPALADRPLAQVDVAKAEAALRSARAFFYEAIEQAWGHVLAGDPVPVEVTN 316
Cdd:pfam08028   1 GIAAAALGAARAALAEFTERARGRVRAYFGVPLAEDPATQLALAEAAARIDAARLLLERAAARIEAAAAAGKPVTPALRA 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 501228838  317 LLRLSSTHAARVAAEVARSAQLLSGMTGIYNESPLARCVNDAQVVTQHAFM 367
Cdd:pfam08028  81 EARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAV 131
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
18-362 1.85e-23

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: 100.30  E-value: 1.85e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501228838  18 PAFEALLDGVRD------RARLGEFDRQRHISRDVIDAFKAHGVYRALVPKRFGGLECSPAAFCEMIERIAHADGSAGW- 90
Cdd:COG1960    7 EEQRALRDEVREfaeeeiAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADASLALp 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501228838  91 --VASFGMSPVYLAALP------LDTIAeiygnSPDTVFAGGIFPPQP----------AETVPGGFKVNGRWKYSSGSMG 152
Cdd:COG1960   87 vgVHNGAAEALLRFGTEeqkeryLPRLA-----SGEWIGAFALTEPGAgsdaaalrttAVRDGDGYVLNGQKTFITNAPV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501228838 153 ADIVGVGITPRNGDKLDLPRLAVLPRSQA--RIEETWDTVGLLGTGSHDLVVEDVRVGEQWTFVRGGKPnldepfFRYP- 229
Cdd:COG1960  162 ADVILVLARTDPAAGHRGISLFLVPKDTPgvTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKG------FKIAm 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501228838 230 -SLSFATQVLSVVGLGIARAALDELSGMASGRIsVTGAPaLADRPLAQVDVAKAEAALRSARAFFYEAIEQawghVLAGD 308
Cdd:COG1960  236 sTLNAGRLGLAAQALGIAEAALELAVAYARERE-QFGRP-IADFQAVQHRLADMAAELEAARALVYRAAWL----LDAGE 309
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 501228838 309 PVPVEvTNLLRLSSTHAARVAAEVARsaQLLSGMtGIYNESPLARCVNDAQVVT 362
Cdd:COG1960  310 DAALE-AAMAKLFATEAALEVADEAL--QIHGGY-GYTREYPLERLYRDARILT 359
DszC cd01163
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ...
18-301 1.91e-19

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: 88.92  E-value: 1.91e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501228838  18 PAFEALLDGVRDRarlgefDRQRHISRDVIDAFKAHGVYRALVPKRFGGLECSPAAFCEMIERIAHADGSAGWV--ASFG 95
Cdd:cd01163    5 PLAARIAEGAAER------DRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQAlrAHFG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501228838  96 MSPVYLAALPLDTIAEIYGNSPDTVFAGGIFPPQPA----------ETVPGGFKVNGRWKYSSGSMGADIVGVGITPRNG 165
Cdd:cd01163   79 FVEALLLAGPEQFRKRWFGRVLNGWIFGNAVSERGSvrpgtfltatVRDGGGYVLNGKKFYSTGALFSDWVTVSALDEEG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501228838 166 DKLdlprLAVLPRSQARIE--ETWDTVGLLGTGSHDLVVEDVRVgeQWTFVRGGKPNLDEPFFRYPslsFATQVLSVVGL 243
Cdd:cd01163  159 KLV----FAAVPTDRPGITvvDDWDGFGQRLTASGTVTFDNVRV--EPDEVLPRPNAPDRGTLLTA---IYQLVLAAVLA 229
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501228838 244 GIARAALDELSGMASGR---ISVTGAPALADRPLAQVDVAKAEAALRSARAFFYEA---IEQAW 301
Cdd:cd01163  230 GIARAALDDAVAYVRSRtrpWIHSGAESARDDPYVQQVVGDLAARLHAAEALVLQAaraLDAAA 293
ACAD cd00567
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
131-373 2.67e-13

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: 70.01  E-value: 2.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501228838 131 AETVPGGFKVNGRWKYSSGSMGADIVGV-GITPRNGDKLDLPRLAVLPRSQA--RIEETWDTVGLLGTGSHDLVVEDVRV 207
Cdd:cd00567   91 ARKDGDGYVLNGRKIFISNGGDADLFIVlARTDEEGPGHRGISAFLVPADTPgvTVGRIWDKMGMRGSGTGELVFDDVRV 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501228838 208 GEQWTFVRGGKpnldepFFRY--PSLSFATQVLSVVGLGIARAALDELSGMASGRisVTGAPALADRPLAQVDVAKAEAA 285
Cdd:cd00567  171 PEDNLLGEEGG------GFELamKGLNVGRLLLAAVALGAARAALDEAVEYAKQR--KQFGKPLAEFQAVQFKLADMAAE 242
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501228838 286 LRSARAFFYEAieqAWGhVLAGDPVPVEVTNLLRLSSThaARVAAEVARSAQLLSGMtGIYNESPLARCVNDAQVVTQha 365
Cdd:cd00567  243 LEAARLLLYRA---AWL-LDQGPDEARLEAAMAKLFAT--EAAREVADLAMQIHGGR-GYSREYPVERYLRDARAARI-- 313

                 ....*...
gi 501228838 366 FMGDVTYQ 373
Cdd:cd00567  314 AEGTAEIQ 321
Acyl-CoA_dh_N pfam02771
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ...
21-115 4.26e-07

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: 48.23  E-value: 4.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501228838   21 EALLDGVRD------RARLGEFDRQRHISRDVIDAFKAHGVYRALVPKRFGGLECSPAAFCEMIERIAHADGSAGWVASF 94
Cdd:pfam02771   5 EALRDTVREfaeeeiAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVALALSV 84
                          90       100
                  ....*....|....*....|.
gi 501228838   95 GMSpvyLAALPLDTiaeiYGN 115
Cdd:pfam02771  85 HSS---LGAPPILR----FGT 98
Acyl-CoA_dh_M pfam02770
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ...
131-203 6.14e-03

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: 35.72  E-value: 6.14e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501228838  131 AETVPGGFKVNGRWKYSSGSMGADIVGVGITPRNGDKLDLPRLAVLPRSQA--RIEETWDTVGLLGTGSHDLVVE 203
Cdd:pfam02770  21 ADGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDDRHGGISLFLVPKDAPgvSVRRIETKLGVRGLPTGELVFD 95
 
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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