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Conserved domains on  [gi|446699019|ref|WP_000776365|]
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MULTISPECIES: enoyl-CoA hydratase [Bacillus]

Protein Classification

hotdog family protein( domain architecture ID 107)

hotdog family protein may have metabolic roles such as thioester hydrolysis in fatty acid metabolism and degradation of phenylacetic acid and the environmental pollutant 4-chlorobenzoate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
hot_dog super family cl00509
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 3-124 1.47e-32

The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase) structure and subsequently in 4HBT (4-hydroxybenzoyl-CoA thioesterase) from Pseudomonas. A number of other seemingly unrelated proteins also share the hotdog fold. These proteins have related, but distinct, catalytic activities that include metabolic roles such as thioester hydrolysis in fatty acid metabolism, and degradation of phenylacetic acid and the environmental pollutant 4-chlorobenzoate. This superfamily also includes the PaaI-like protein FapR, a non-catalytic bacterial homolog involved in transcriptional regulation of fatty acid biosynthesis.


The actual alignment was detected with superfamily member cd03449:

Pssm-ID: 469797 [Multi-domain]  Cd Length: 128  Bit Score: 110.71  E-value: 1.47e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699019   3 LQVGEKITFERTFTREDVVLFTEVSKDEGVHHVTPD--EQGRF---VVQGLLTSTLPTKVGGDY----NVLARKMDFEFL 73
Cdd:cd03449    1 LKVGDSASLTRTITEEDVELFAELSGDFNPIHLDEEyaKKTRFggrIAHGMLTASLISAVLGTLlpgpGTIYLSQSLRFL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446699019  74 RPVFSGDTIRCDVTIEKFEPDeknRTKIIAMFTCMNQLEKEVLKGSFSGII 124
Cdd:cd03449   81 RPVFIGDTVTATVTVTEKRED---KKRVTLETVCTNQNGEVVIEGEAVVLA 128
 
Name Accession Description Interval E-value
R_hydratase cd03449
(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA ...
 3-124 1.47e-32

(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA to (R)-3-hydroxyacyl-CoA as part of the PHA (polyhydroxyalkanoate) biosynthetic pathway. (R)-hydratase contains a hot-dog fold similar to those of thioesterase II, and beta-hydroxydecanoyl-ACP dehydratase, MaoC dehydratase, Hydratase-Dehydrogenase-Epimerase protein (HDE), and the fatty acid synthase beta subunit. The active site lies within a substrate-binding tunnel formed by the (R)-hydratase homodimer. A subset of the bacterial (R)-hydratases contain a C-terminal phosphotransacetylase (PTA) domain.


Pssm-ID: 239533 [Multi-domain]  Cd Length: 128  Bit Score: 110.71  E-value: 1.47e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699019   3 LQVGEKITFERTFTREDVVLFTEVSKDEGVHHVTPD--EQGRF---VVQGLLTSTLPTKVGGDY----NVLARKMDFEFL 73
Cdd:cd03449    1 LKVGDSASLTRTITEEDVELFAELSGDFNPIHLDEEyaKKTRFggrIAHGMLTASLISAVLGTLlpgpGTIYLSQSLRFL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446699019  74 RPVFSGDTIRCDVTIEKFEPDeknRTKIIAMFTCMNQLEKEVLKGSFSGII 124
Cdd:cd03449   81 RPVFIGDTVTATVTVTEKRED---KKRVTLETVCTNQNGEVVIEGEAVVLA 128
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
3-118 3.96e-17

Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 71.84  E-value: 3.96e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699019   3 LQVGEKITFE-RTFTREDVVLFTEVSKDEGVHHVTPD--EQGRF---VVQGLLTSTLPTKVGGDY---NVLA--RKMDFE 71
Cdd:COG2030    5 LEVGDVLPHGgRTVTEEDIVLFAGATGDPNPIHLDEEaaAATGFggrIAHGMLTLSLASGLLVDDlpgTAVAnlGLQEVR 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 446699019  72 FLRPVFSGDTIRCDVTIEKFEPdEKNRTKIIAMFTCMNQLEKEVLKG 118
Cdd:COG2030   85 FLRPVRVGDTLRARVEVLEKRE-SKSRGIVTLRTTVTNQDGEVVLTG 130
PRK08190 PRK08190
bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated
 3-119 6.23e-10

bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated


Pssm-ID: 236180 [Multi-domain]  Cd Length: 466  Bit Score: 55.27  E-value: 6.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699019   3 LQVGEKITFERTFTREDVVLFTEVSKDEGVHHVTPD--EQGRF---VVQGLLTSTLPTKVGGdyNVLA------RKMDFE 71
Cdd:PRK08190  14 IAIGDSASLVRTLTPDDIELFAAMSGDVNPAHLDAAyaASDGFhhvVAHGMWGGALISAVLG--TRLPgpgtiyLGQSLR 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 446699019  72 FLRPVFSGDTIRCDVTIEkfepdEKNRTKIIAMFTC--MNQLEKEVLKGS 119
Cdd:PRK08190  92 FRRPVRIGDTLTVTVTVR-----EKDPEKRIVVLDCrcTNQDGEVVITGT 136
MaoC_dehydratas pfam01575
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ...
 5-100 1.13e-05

MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the synthesis of monoamine oxidase. The MaoC protein is found to share similarity with a wide variety of enzymes; estradiol 17 beta-dehydrogenase 4, peroxisomal hydratase-dehydrogenase-epimerase, fatty acid synthase beta subunit. Several bacterial proteins that are composed solely of this domain have (R)-specific enoyl-CoA hydratase activity. This domain is also present in the NodN nodulation protein N.


Pssm-ID: 396243 [Multi-domain]  Cd Length: 123  Bit Score: 41.56  E-value: 1.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699019    5 VGEKITFE--RTFTREDVVLFTEVSKDEGVHHVTPD--EQGRF---VVQGLLTSTLPTKV----GGDYNVLARKMD-FEF 72
Cdd:pfam01575   6 PGEPPDTEkpRTVTEADIALFALVSGDHNPIHVDPEfaKKAGFggpIAHGMLTLAIVAGLveewGGDNVIARFGEIkVRF 85

                          90       100
                  ....*....|....*....|....*...
gi 446699019   73 LRPVFSGDTIRcdVTIEKFEPDEKNRTK 100
Cdd:pfam01575  86 TKPVFPGDTLR--TEAEVVGKRDGRQTK 111
 
Name Accession Description Interval E-value
R_hydratase cd03449
(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA ...
 3-124 1.47e-32

(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA to (R)-3-hydroxyacyl-CoA as part of the PHA (polyhydroxyalkanoate) biosynthetic pathway. (R)-hydratase contains a hot-dog fold similar to those of thioesterase II, and beta-hydroxydecanoyl-ACP dehydratase, MaoC dehydratase, Hydratase-Dehydrogenase-Epimerase protein (HDE), and the fatty acid synthase beta subunit. The active site lies within a substrate-binding tunnel formed by the (R)-hydratase homodimer. A subset of the bacterial (R)-hydratases contain a C-terminal phosphotransacetylase (PTA) domain.


Pssm-ID: 239533 [Multi-domain]  Cd Length: 128  Bit Score: 110.71  E-value: 1.47e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699019   3 LQVGEKITFERTFTREDVVLFTEVSKDEGVHHVTPD--EQGRF---VVQGLLTSTLPTKVGGDY----NVLARKMDFEFL 73
Cdd:cd03449    1 LKVGDSASLTRTITEEDVELFAELSGDFNPIHLDEEyaKKTRFggrIAHGMLTASLISAVLGTLlpgpGTIYLSQSLRFL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446699019  74 RPVFSGDTIRCDVTIEKFEPDeknRTKIIAMFTCMNQLEKEVLKGSFSGII 124
Cdd:cd03449   81 RPVFIGDTVTATVTVTEKRED---KKRVTLETVCTNQNGEVVIEGEAVVLA 128
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
3-118 3.96e-17

Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 71.84  E-value: 3.96e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699019   3 LQVGEKITFE-RTFTREDVVLFTEVSKDEGVHHVTPD--EQGRF---VVQGLLTSTLPTKVGGDY---NVLA--RKMDFE 71
Cdd:COG2030    5 LEVGDVLPHGgRTVTEEDIVLFAGATGDPNPIHLDEEaaAATGFggrIAHGMLTLSLASGLLVDDlpgTAVAnlGLQEVR 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 446699019  72 FLRPVFSGDTIRCDVTIEKFEPdEKNRTKIIAMFTCMNQLEKEVLKG 118
Cdd:COG2030   85 FLRPVRVGDTLRARVEVLEKRE-SKSRGIVTLRTTVTNQDGEVVLTG 130
R_hydratase_like cd03441
(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl ...
 6-118 2.15e-15

(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl CoA to (R)-3-hydroxyacyl-CoA as part of the PHA (polyhydroxyalkanoate) biosynthetic pathway. The structure of the monomer includes a five-strand antiparallel beta-sheet wrapped around a central alpha helix, referred to as a hot dog fold. The active site lies within a substrate-binding tunnel formed by the homodimer. Other enzymes with this fold include MaoC dehydratase, Hydratase-Dehydrogenase-Epimerase protein (HDE), and the fatty acid synthase beta subunit.


Pssm-ID: 239525 [Multi-domain]  Cd Length: 127  Bit Score: 66.90  E-value: 2.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699019   6 GEKITFERTFTREDVVLFTEVSKDEGVHHVTPD--EQGRF---VVQGLLTSTLPTKVGGDYN-----VLARKMDFEFLRP 75
Cdd:cd03441    1 GELDSSGRTVTEADIALFARLSGDPNPIHVDPEyaKAAGFggrIAHGMLTLSLASGLLVQWLpgtdgANLGSQSVRFLAP 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446699019  76 VFSGDTIRCDVTIEKFEPDEKNRTKIIAmFTCMNQLEKEVLKG 118
Cdd:cd03441   81 VFPGDTLRVEVEVLGKRPSKGRGVVTVR-TEARNQGGEVVLSG 122
PRK08190 PRK08190
bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated
 3-119 6.23e-10

bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated


Pssm-ID: 236180 [Multi-domain]  Cd Length: 466  Bit Score: 55.27  E-value: 6.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699019   3 LQVGEKITFERTFTREDVVLFTEVSKDEGVHHVTPD--EQGRF---VVQGLLTSTLPTKVGGdyNVLA------RKMDFE 71
Cdd:PRK08190  14 IAIGDSASLVRTLTPDDIELFAAMSGDVNPAHLDAAyaASDGFhhvVAHGMWGGALISAVLG--TRLPgpgtiyLGQSLR 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 446699019  72 FLRPVFSGDTIRCDVTIEkfepdEKNRTKIIAMFTC--MNQLEKEVLKGS 119
Cdd:PRK08190  92 FRRPVRIGDTLTVTVTVR-----EKDPEKRIVVLDCrcTNQDGEVVITGT 136
MaoC_dehydratas pfam01575
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ...
 5-100 1.13e-05

MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the synthesis of monoamine oxidase. The MaoC protein is found to share similarity with a wide variety of enzymes; estradiol 17 beta-dehydrogenase 4, peroxisomal hydratase-dehydrogenase-epimerase, fatty acid synthase beta subunit. Several bacterial proteins that are composed solely of this domain have (R)-specific enoyl-CoA hydratase activity. This domain is also present in the NodN nodulation protein N.


Pssm-ID: 396243 [Multi-domain]  Cd Length: 123  Bit Score: 41.56  E-value: 1.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699019    5 VGEKITFE--RTFTREDVVLFTEVSKDEGVHHVTPD--EQGRF---VVQGLLTSTLPTKV----GGDYNVLARKMD-FEF 72
Cdd:pfam01575   6 PGEPPDTEkpRTVTEADIALFALVSGDHNPIHVDPEfaKKAGFggpIAHGMLTLAIVAGLveewGGDNVIARFGEIkVRF 85

                          90       100
                  ....*....|....*....|....*...
gi 446699019   73 LRPVFSGDTIRcdVTIEKFEPDEKNRTK 100
Cdd:pfam01575  86 TKPVFPGDTLR--TEAEVVGKRDGRQTK 111
MaoC_C cd03452
MaoC_C The C-terminal hot dog fold of the MaoC (monoamine oxidase C) dehydratase regulatory ...
 3-93 1.63e-05

MaoC_C The C-terminal hot dog fold of the MaoC (monoamine oxidase C) dehydratase regulatory protein. Orthologs of MaoC include PaaZ [Escherichia coli] and PaaN [Pseudomonas putida], which are putative ring-opening enzymes involved in phenylacetic acid degradation. The C-terminal domain of MaoC has sequence similarity to (R)-specific enoyl-CoA hydratase,Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit. MaoC also has an N-terminal PutA domain like that found in the E. coli PutA proline dehydrogenase and other members of the aldehyde dehydrogenase family.


Pssm-ID: 239536 [Multi-domain]  Cd Length: 142  Bit Score: 41.62  E-value: 1.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699019   3 LQVGEKI-TFERTFTREDVVLFTEVSKDEGVHHVtpDE-------------QGRFVVQ---GLLTSTLPTKVGGDYNVLA 65
Cdd:cd03452    5 LRPGDSLlTHRRTVTEADIVNFACLTGDHFYAHM--DEiaakasffgkrvaHGYFVLSaaaGLFVDPAPGPVLANYGLEN 82

                         90       100
                 ....*....|....*....|....*...
gi 446699019  66 rkmdFEFLRPVFSGDTIRCDVTIEKFEP 93
Cdd:cd03452   83 ----LRFLEPVYPGDTIQVRLTCKRKIP 106
MaoC_like cd03446
MoaC_like Similar to the MaoC (monoamine oxidase C) dehydratase regulatory protein but ...
 3-124 6.45e-05

MoaC_like Similar to the MaoC (monoamine oxidase C) dehydratase regulatory protein but without the N-terminal PutA domain. This protein family has a hot-dog fold similar to that of (R)-specific enoyl-CoA hydratase, the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit.


Pssm-ID: 239530 [Multi-domain]  Cd Length: 140  Bit Score: 39.98  E-value: 6.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699019   3 LQVGEKI-TFERTFTREDVVLFTEVSKDEGVHHVtpDEQ-------GRFVVQGLLTSTLPT----KVGG-DYNVLA---- 65
Cdd:cd03446    5 FEIGQVFeSVGRTVTEADVVMFAGLSGDWNPIHT--DAEyakktrfGERIAHGLLTLSIATgllqRLGVfERTVVAfygi 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699019  66 RKMDFefLRPVFSGDTIRCDVTI-EKFEPDEKNRTKIIAMFTCMNQLEKEVLKGSFSGII 124
Cdd:cd03446   83 DNLRF--LNPVFIGDTIRAEAEVvEKEEKDGEDAGVVTRRIEVVNQRGEVVQSGEMSLLV 140
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 29-121 1.78e-03

The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase) structure and subsequently in 4HBT (4-hydroxybenzoyl-CoA thioesterase) from Pseudomonas. A number of other seemingly unrelated proteins also share the hotdog fold. These proteins have related, but distinct, catalytic activities that include metabolic roles such as thioester hydrolysis in fatty acid metabolism, and degradation of phenylacetic acid and the environmental pollutant 4-chlorobenzoate. This superfamily also includes the PaaI-like protein FapR, a non-catalytic bacterial homolog involved in transcriptional regulation of fatty acid biosynthesis.


Pssm-ID: 239524 [Multi-domain]  Cd Length: 100  Bit Score: 35.14  E-value: 1.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699019  29 DEGVHHVTPDEQGRF-VVQGLLTSTL---------PTKVGGDYNVLARKMDFEFLRPVFSGDTIRCDVTIEKfepdeKNR 98
Cdd:cd03440    1 FVLRLTVTPEDIDGGgIVHGGLLLALadeaagaaaARLGGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVR-----VGR 75

                         90       100
                 ....*....|....*....|...
gi 446699019  99 TKIIAMFTCMNQLEKEVLKGSFS 121
Cdd:cd03440   76 SSVTVEVEVRNEDGKLVATATAT 98
 
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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