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Conserved domains on  [gi|516458025|ref|WP_017846865|]
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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 ...
19-382 5.38e-84

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: 260.36  E-value: 5.38e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458025  19 QAFSALLVDIKKRArsGEFDRLGYIAQDVIDAFKTLGVYRALVPRRFGGDQCSPGEFCAMVEEISRADGSAGWVASF-GM 97
Cdd:cd01159    1 ARAEDLAPLIRERA--PEAERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSAAWVASIvAT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458025  98 SPVYLASLPLDTIRQVYANGPDVVFAGGIFPPQPAEAVPGGFKVNGRWKYSSGCMGASLVGVGIAPKNGDKLDLPRLAVM 177
Cdd:cd01159   79 HSRMLAAFPPEAQEEVWGDGPDTLLAGSYAPGGRAERVDGGYRVSGTWPFASGCDHADWILVGAIVEDDDGGPLPRAFVV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458025 178 PQSKVRIEQTWDTVGLLGTGSHDLVVEDVVVSEEWTFVRGGAANLDEP-----FFRYPSLSFATQVLSVVGLGVARAALD 252
Cdd:cd01159  159 PRAEYEIVDTWHVVGLRGTGSNTVVVDDVFVPEHRTLTAGDMMAGDGPggstpVYRMPLRQVFPLSFAAVSLGAAEGALA 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458025 253 ELRDMAAGRISVTGAPA-VADRPLAQVEIAKAEAALRAARAFFFESIEDAWQTVLRGDSLSVEKTNLLRLSSTHATRVAA 331
Cdd:cd01159  239 EFLELAGKRVRQYGAAVkMAEAPITQLRLAEAAAELDAARAFLERATRDLWAHALAGGPIDVEERARIRRDAAYAAKLSA 318
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 516458025 332 EVARTAQMLSGMTGVYNSSPLARCVNDAQVVTQHAFM-GDITYQNAGAVFFG 382
Cdd:cd01159  319 EAVDRLFHAAGGSALYTASPLQRIWRDIHAAAQHAALnPETAAEAYGRALLG 370
 
Name Accession Description Interval E-value
NcnH cd01159
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ...
19-382 5.38e-84

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: 260.36  E-value: 5.38e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458025  19 QAFSALLVDIKKRArsGEFDRLGYIAQDVIDAFKTLGVYRALVPRRFGGDQCSPGEFCAMVEEISRADGSAGWVASF-GM 97
Cdd:cd01159    1 ARAEDLAPLIRERA--PEAERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSAAWVASIvAT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458025  98 SPVYLASLPLDTIRQVYANGPDVVFAGGIFPPQPAEAVPGGFKVNGRWKYSSGCMGASLVGVGIAPKNGDKLDLPRLAVM 177
Cdd:cd01159   79 HSRMLAAFPPEAQEEVWGDGPDTLLAGSYAPGGRAERVDGGYRVSGTWPFASGCDHADWILVGAIVEDDDGGPLPRAFVV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458025 178 PQSKVRIEQTWDTVGLLGTGSHDLVVEDVVVSEEWTFVRGGAANLDEP-----FFRYPSLSFATQVLSVVGLGVARAALD 252
Cdd:cd01159  159 PRAEYEIVDTWHVVGLRGTGSNTVVVDDVFVPEHRTLTAGDMMAGDGPggstpVYRMPLRQVFPLSFAAVSLGAAEGALA 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458025 253 ELRDMAAGRISVTGAPA-VADRPLAQVEIAKAEAALRAARAFFFESIEDAWQTVLRGDSLSVEKTNLLRLSSTHATRVAA 331
Cdd:cd01159  239 EFLELAGKRVRQYGAAVkMAEAPITQLRLAEAAAELDAARAFLERATRDLWAHALAGGPIDVEERARIRRDAAYAAKLSA 318
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 516458025 332 EVARTAQMLSGMTGVYNSSPLARCVNDAQVVTQHAFM-GDITYQNAGAVFFG 382
Cdd:cd01159  319 EAVDRLFHAAGGSALYTASPLQRIWRDIHAAAQHAALnPETAAEAYGRALLG 370
Acyl-CoA_dh_2 pfam08028
Acyl-CoA dehydrogenase, C-terminal domain;
238-368 8.35e-18

Acyl-CoA dehydrogenase, C-terminal domain;


Pssm-ID: 429790 [Multi-domain]  Cd Length: 133  Bit Score: 78.93  E-value: 8.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458025  238 VLSVVGLGVARAALDELRDMAAGRISVTGAPAVADRPLAQVEIAKAEAALRAARAFFFESIEDAWQTVLRGDSLSVEKTN 317
Cdd:pfam08028   1 GIAAAALGAARAALAEFTERARGRVRAYFGVPLAEDPATQLALAEAAARIDAARLLLERAAARIEAAAAAGKPVTPALRA 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 516458025  318 LLRLSSTHATRVAAEVARTAQMLSGMTGVYNSSPLARCVNDAQVVTQHAFM 368
Cdd:pfam08028  81 EARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAV 131
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
36-363 2.58e-14

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: 73.72  E-value: 2.58e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458025  36 EFDRLGYIAQDVIDAFKTLGVYRALVPRRFGGDQCSPGEFCAMVEEISRADGSAGWVASFGMSPVY-LASLPLDTIRQVY 114
Cdd:COG1960   30 EWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADASLALPVGVHNGAAEaLLRFGTEEQKERY 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458025 115 ----ANGpDVVFAGGIFPPQP----------AEAVPGGFKVNGRWKYSSGCMGASLVGVG--IAPKNGDKLdlPRLAVMP 178
Cdd:COG1960  110 lprlASG-EWIGAFALTEPGAgsdaaalrttAVRDGDGYVLNGQKTFITNAPVADVILVLarTDPAAGHRG--ISLFLVP 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458025 179 QSK--VRIEQTWDTVGLLGTGSHDLvvedvvvseewTF--VRGGAANL--DEPF-FRYP--SLSFATQVLSVVGLGVARA 249
Cdd:COG1960  187 KDTpgVTVGRIEDKMGLRGSDTGEL-----------FFddVRVPAENLlgEEGKgFKIAmsTLNAGRLGLAAQALGIAEA 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458025 250 ALDELRDMAAGRIsVTGAPAVAD----RPLAQVEIAkaeaalraarafffesIEDAWQTVLR-------GDSLSVEkTNL 318
Cdd:COG1960  256 ALELAVAYARERE-QFGRPIADFqavqHRLADMAAE----------------LEAARALVYRaawlldaGEDAALE-AAM 317
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 516458025 319 LRLsstHATRVAAEVARTAQMLSGMTGVYNSSPLARCVNDAQVVT 363
Cdd:COG1960  318 AKL---FATEAALEVADEALQIHGGYGYTREYPLERLYRDARILT 359
 
Name Accession Description Interval E-value
NcnH cd01159
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ...
19-382 5.38e-84

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: 260.36  E-value: 5.38e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458025  19 QAFSALLVDIKKRArsGEFDRLGYIAQDVIDAFKTLGVYRALVPRRFGGDQCSPGEFCAMVEEISRADGSAGWVASF-GM 97
Cdd:cd01159    1 ARAEDLAPLIRERA--PEAERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSAAWVASIvAT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458025  98 SPVYLASLPLDTIRQVYANGPDVVFAGGIFPPQPAEAVPGGFKVNGRWKYSSGCMGASLVGVGIAPKNGDKLDLPRLAVM 177
Cdd:cd01159   79 HSRMLAAFPPEAQEEVWGDGPDTLLAGSYAPGGRAERVDGGYRVSGTWPFASGCDHADWILVGAIVEDDDGGPLPRAFVV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458025 178 PQSKVRIEQTWDTVGLLGTGSHDLVVEDVVVSEEWTFVRGGAANLDEP-----FFRYPSLSFATQVLSVVGLGVARAALD 252
Cdd:cd01159  159 PRAEYEIVDTWHVVGLRGTGSNTVVVDDVFVPEHRTLTAGDMMAGDGPggstpVYRMPLRQVFPLSFAAVSLGAAEGALA 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458025 253 ELRDMAAGRISVTGAPA-VADRPLAQVEIAKAEAALRAARAFFFESIEDAWQTVLRGDSLSVEKTNLLRLSSTHATRVAA 331
Cdd:cd01159  239 EFLELAGKRVRQYGAAVkMAEAPITQLRLAEAAAELDAARAFLERATRDLWAHALAGGPIDVEERARIRRDAAYAAKLSA 318
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 516458025 332 EVARTAQMLSGMTGVYNSSPLARCVNDAQVVTQHAFM-GDITYQNAGAVFFG 382
Cdd:cd01159  319 EAVDRLFHAAGGSALYTASPLQRIWRDIHAAAQHAALnPETAAEAYGRALLG 370
Acyl-CoA_dh_2 pfam08028
Acyl-CoA dehydrogenase, C-terminal domain;
238-368 8.35e-18

Acyl-CoA dehydrogenase, C-terminal domain;


Pssm-ID: 429790 [Multi-domain]  Cd Length: 133  Bit Score: 78.93  E-value: 8.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458025  238 VLSVVGLGVARAALDELRDMAAGRISVTGAPAVADRPLAQVEIAKAEAALRAARAFFFESIEDAWQTVLRGDSLSVEKTN 317
Cdd:pfam08028   1 GIAAAALGAARAALAEFTERARGRVRAYFGVPLAEDPATQLALAEAAARIDAARLLLERAAARIEAAAAAGKPVTPALRA 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 516458025  318 LLRLSSTHATRVAAEVARTAQMLSGMTGVYNSSPLARCVNDAQVVTQHAFM 368
Cdd:pfam08028  81 EARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAV 131
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
36-363 2.58e-14

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: 73.72  E-value: 2.58e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458025  36 EFDRLGYIAQDVIDAFKTLGVYRALVPRRFGGDQCSPGEFCAMVEEISRADGSAGWVASFGMSPVY-LASLPLDTIRQVY 114
Cdd:COG1960   30 EWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADASLALPVGVHNGAAEaLLRFGTEEQKERY 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458025 115 ----ANGpDVVFAGGIFPPQP----------AEAVPGGFKVNGRWKYSSGCMGASLVGVG--IAPKNGDKLdlPRLAVMP 178
Cdd:COG1960  110 lprlASG-EWIGAFALTEPGAgsdaaalrttAVRDGDGYVLNGQKTFITNAPVADVILVLarTDPAAGHRG--ISLFLVP 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458025 179 QSK--VRIEQTWDTVGLLGTGSHDLvvedvvvseewTF--VRGGAANL--DEPF-FRYP--SLSFATQVLSVVGLGVARA 249
Cdd:COG1960  187 KDTpgVTVGRIEDKMGLRGSDTGEL-----------FFddVRVPAENLlgEEGKgFKIAmsTLNAGRLGLAAQALGIAEA 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458025 250 ALDELRDMAAGRIsVTGAPAVAD----RPLAQVEIAkaeaalraarafffesIEDAWQTVLR-------GDSLSVEkTNL 318
Cdd:COG1960  256 ALELAVAYARERE-QFGRPIADFqavqHRLADMAAE----------------LEAARALVYRaawlldaGEDAALE-AAM 317
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 516458025 319 LRLsstHATRVAAEVARTAQMLSGMTGVYNSSPLARCVNDAQVVT 363
Cdd:COG1960  318 AKL---FATEAALEVADEALQIHGGYGYTREYPLERLYRDARILT 359
DszC cd01163
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ...
19-277 2.58e-09

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: 58.49  E-value: 2.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458025  19 QAFSALLVDIKKRARsgEFDRLGYIAQDVIDAFKTLGVYRALVPRRFGGDQCSPGEFCAMVEEISRADGSAGWV--ASFG 96
Cdd:cd01163    1 ARARPLAARIAEGAA--ERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQAlrAHFG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458025  97 MSPVYLASLP-------LDTIRQVYANGPDVVFAGGIFPPQPAEAV---PGGFKVNGRWKYSSGCMGASLVGVGIAPKNG 166
Cdd:cd01163   79 FVEALLLAGPeqfrkrwFGRVLNGWIFGNAVSERGSVRPGTFLTATvrdGGGYVLNGKKFYSTGALFSDWVTVSALDEEG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458025 167 DKLdlprLAVMP--QSKVRIEQTWDTVGLLGTGSHdlVVEDVVVSEEWTFVRGGAANLDEPFFRYPslsFATQVLSVVGL 244
Cdd:cd01163  159 KLV----FAAVPtdRPGITVVDDWDGFGQRLTASG--TVTFDNVRVEPDEVLPRPNAPDRGTLLTA---IYQLVLAAVLA 229
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 516458025 245 GVARAALDELRDMAAGR---ISVTGAPAVADRPLAQ 277
Cdd:cd01163  230 GIARAALDDAVAYVRSRtrpWIHSGAESARDDPYVQ 265
Acyl-CoA_dh_N pfam02771
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ...
36-107 3.89e-05

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: 42.45  E-value: 3.89e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516458025   36 EFDRLGYIAQDVIDAFKTLGVYRALVPRRFGGDQCSPGEFCAMVEEISRADGSAGWVASFGMSpvyLASLPL 107
Cdd:pfam02771  25 EWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVALALSVHSS---LGAPPI 93
 
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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