NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1330191931|ref|WP_102367141|]
View 

MaoC/PaaZ C-terminal domain-containing protein [Vibrio breoganii]

Protein Classification

hotdog fold domain-containing protein( domain architecture ID 713432)

hotdog fold domain-containing protein belonging to the hotdog fold superfamily of thioesterases and dehydratases, with similarity to MaoC family dehydratases

CATH:  3.10.129.10
PubMed:  15307895
SCOP:  3000149

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 172-238 7.40e-13

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 pfam01575:

Pssm-ID: 469797 [Multi-domain]  Cd Length: 123  Bit Score: 63.90  E-value: 7.40e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1330191931 172 HIARLKITEQSVRGYARVSGDYNPIHLHRLTSAPFGFKKPIAHGLYLLA--RSLVsLDIAPAEVEVNFK 238
Cdd:pfam01575  12 TEKPRTVTEADIALFALVSGDHNPIHVDPEFAKKAGFGGPIAHGMLTLAivAGLV-EEWGGDNVIARFG 79
PLN02864 super family cl28571
enoyl-CoA hydratase
 101-216 7.99e-04

enoyl-CoA hydratase


The actual alignment was detected with superfamily member PLN02864:

Pssm-ID: 178455 [Multi-domain]  Cd Length: 310  Bit Score: 40.15  E-value: 7.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330191931 101 HKEIDTRANYDVTVSVG--HVESKARGIEFELCVQFFENDERVC------------GFD--SRYFSITSSQRGNKPAPIA 164
Cdd:PLN02864  104 YKPIPSSASVRNKVSIAglHDKGKAAILELETLSYEKDSGELLCmnrstiflrgagGFSnsSQPFSYSNYPTNQVSAVKI 183

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1330191931 165 DDFSAFQHIArlKITEQSVRGYARVSGDYNPIHLHRLTSAPFGFKKPIAHGL 216
Cdd:PLN02864  184 PKSQPDAVFE--DQTQPSQALLYRLSGDYNPLHSDPMFAKVAGFTRPILHGL 233
 
Name Accession Description Interval E-value
MaoC_dehydratas pfam01575
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ...
 172-238 7.40e-13

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: 63.90  E-value: 7.40e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1330191931 172 HIARLKITEQSVRGYARVSGDYNPIHLHRLTSAPFGFKKPIAHGLYLLA--RSLVsLDIAPAEVEVNFK 238
Cdd:pfam01575  12 TEKPRTVTEADIALFALVSGDHNPIHVDPEFAKKAGFGGPIAHGMLTLAivAGLV-EEWGGDNVIARFG 79
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
165-240 1.59e-10

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 57.97  E-value: 1.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330191931 165 DDFSAFQHI--ARLKITEQSVRGYARVSGDYNPIHLHRLTSAPFGFKKPIAHGLYLLA---RSLVSL--DIAPAEV---E 234
Cdd:COG2030     3 EDLEVGDVLphGGRTVTEEDIVLFAGATGDPNPIHLDEEAAAATGFGGRIAHGMLTLSlasGLLVDDlpGTAVANLglqE 82


                  ....*.
gi 1330191931 235 VNFKRP 240
Cdd:COG2030    83 VRFLRP 88
R_hydratase cd03449
(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA ...
 177-225 1.72e-09

(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: 54.47  E-value: 1.72e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1330191931 177 KITEQSVRGYARVSGDYNPIHLHRLTSAPFGFKKPIAHGlyLLARSLVS 225
Cdd:cd03449    12 TITEEDVELFAELSGDFNPIHLDEEYAKKTRFGGRIAHG--MLTASLIS 58
PRK08190 PRK08190
bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated
 179-225 7.23e-04

bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated


Pssm-ID: 236180 [Multi-domain]  Cd Length: 466  Bit Score: 40.63  E-value: 7.23e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1330191931 179 TEQSVRGYARVSGDYNPIHLHRLTSAPFGFKKPIAHGLYllARSLVS 225
Cdd:PRK08190   27 TPDDIELFAAMSGDVNPAHLDAAYAASDGFHHVVAHGMW--GGALIS 71
PLN02864 PLN02864
enoyl-CoA hydratase
 101-216 7.99e-04

enoyl-CoA hydratase


Pssm-ID: 178455 [Multi-domain]  Cd Length: 310  Bit Score: 40.15  E-value: 7.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330191931 101 HKEIDTRANYDVTVSVG--HVESKARGIEFELCVQFFENDERVC------------GFD--SRYFSITSSQRGNKPAPIA 164
Cdd:PLN02864  104 YKPIPSSASVRNKVSIAglHDKGKAAILELETLSYEKDSGELLCmnrstiflrgagGFSnsSQPFSYSNYPTNQVSAVKI 183

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1330191931 165 DDFSAFQHIArlKITEQSVRGYARVSGDYNPIHLHRLTSAPFGFKKPIAHGL 216
Cdd:PLN02864  184 PKSQPDAVFE--DQTQPSQALLYRLSGDYNPLHSDPMFAKVAGFTRPILHGL 233
 
Name Accession Description Interval E-value
MaoC_dehydratas pfam01575
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ...
 172-238 7.40e-13

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: 63.90  E-value: 7.40e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1330191931 172 HIARLKITEQSVRGYARVSGDYNPIHLHRLTSAPFGFKKPIAHGLYLLA--RSLVsLDIAPAEVEVNFK 238
Cdd:pfam01575  12 TEKPRTVTEADIALFALVSGDHNPIHVDPEFAKKAGFGGPIAHGMLTLAivAGLV-EEWGGDNVIARFG 79
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
165-240 1.59e-10

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 57.97  E-value: 1.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330191931 165 DDFSAFQHI--ARLKITEQSVRGYARVSGDYNPIHLHRLTSAPFGFKKPIAHGLYLLA---RSLVSL--DIAPAEV---E 234
Cdd:COG2030     3 EDLEVGDVLphGGRTVTEEDIVLFAGATGDPNPIHLDEEAAAATGFGGRIAHGMLTLSlasGLLVDDlpGTAVANLglqE 82


                  ....*.
gi 1330191931 235 VNFKRP 240
Cdd:COG2030    83 VRFLRP 88
R_hydratase cd03449
(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA ...
 177-225 1.72e-09

(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: 54.47  E-value: 1.72e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1330191931 177 KITEQSVRGYARVSGDYNPIHLHRLTSAPFGFKKPIAHGlyLLARSLVS 225
Cdd:cd03449    12 TITEEDVELFAELSGDFNPIHLDEEYAKKTRFGGRIAHG--MLTASLIS 58
R_hydratase_like cd03441
(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl ...
 178-240 4.14e-09

(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: 53.42  E-value: 4.14e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1330191931 178 ITEQSVRGYARVSGDYNPIHLHRLTSAPFGFKKPIAHGLYL--LARSLVSLDIAPAEV------EVNFKRP 240
Cdd:cd03441    10 VTEADIALFARLSGDPNPIHVDPEYAKAAGFGGRIAHGMLTlsLASGLLVQWLPGTDGanlgsqSVRFLAP 80
FAS_MaoC cd03447
FAS_MaoC, the MaoC-like hot dog fold of the fatty acid synthase, beta subunit. Other enzymes ...
 182-224 2.62e-08

FAS_MaoC, the MaoC-like hot dog fold of the fatty acid synthase, beta subunit. Other enzymes with this fold include MaoC dehydratase, Hydratase-Dehydrogenase-Epimerase protein (HDE), and 17-beta-hydroxysteriod dehydrogenase (HSD).


Pssm-ID: 239531 [Multi-domain]  Cd Length: 126  Bit Score: 51.13  E-value: 2.62e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1330191931 182 SVRGYARVSGDYNPIHLHRLTSAPFGFKKPIAHGLYL--LARSLV 224
Cdd:cd03447    14 SNEPYARVSGDFNPIHVSRVFASYAGLPGTITHGMYTsaAVRALV 58
HDE_HSD cd03448
HDE_HSD The R-hydratase-like hot dog fold of the 17-beta-hydroxysteriod dehydrogenase (HSD), ...
 188-256 2.96e-06

HDE_HSD The R-hydratase-like hot dog fold of the 17-beta-hydroxysteriod dehydrogenase (HSD), and Hydratase-Dehydrogenase-Epimerase (HDE) proteins. Other enzymes with this fold include MaoC dehydratase, and the fatty acid synthase beta subunit.


Pssm-ID: 239532 [Multi-domain]  Cd Length: 122  Bit Score: 45.29  E-value: 2.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330191931 188 RVSGDYNPIHLHRLTSAPFGFKKPIAHGLYLL---ARSLVS--LDIAPAEVE---VNFKRPAlLP---IETELVQTGNQA 256
Cdd:cd03448    22 RLSGDYNPLHIDPAFAKAAGFPRPILHGLCTYgfaARAVLEafADGDPARFKaikVRFSSPV-FPgetLRTEMWKEGNRV 100
MaoC_like cd03446
MoaC_like Similar to the MaoC (monoamine oxidase C) dehydratase regulatory protein but ...
 178-220 3.50e-04

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: 3.50e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1330191931 178 ITEQSVRGYARVSGDYNPIHL--HRLTSAPFGfkKPIAHGLYLLA 220
Cdd:cd03446    18 VTEADVVMFAGLSGDWNPIHTdaEYAKKTRFG--ERIAHGLLTLS 60
SAV4209_like cd03453
SAV4209_like. Similar in sequence to the Streptomyces avermitilis SAV4209 protein, with a hot ...
 178-244 3.97e-04

SAV4209_like. Similar in sequence to the Streptomyces avermitilis SAV4209 protein, with a hot dog fold that is similar to those of (R)-specific enoyl-CoA hydratase, the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit.


Pssm-ID: 239537 [Multi-domain]  Cd Length: 127  Bit Score: 39.61  E-value: 3.97e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1330191931 178 ITEQSVRGYARVSGDYNPIHLHRLTSAPFGFKKPIAHGLY---LLARSLVSLDIAPAEV---EVNFKRPALLP 244
Cdd:cd03453    12 VSRADLVRYAGASGDFNPIHYDEDFAKKVGLPGVIAHGMLtmgLLGRLVTDWVGDPGRVvsfGVRFTKPVPVP 84
PRK08190 PRK08190
bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated
 179-225 7.23e-04

bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated


Pssm-ID: 236180 [Multi-domain]  Cd Length: 466  Bit Score: 40.63  E-value: 7.23e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1330191931 179 TEQSVRGYARVSGDYNPIHLHRLTSAPFGFKKPIAHGLYllARSLVS 225
Cdd:PRK08190   27 TPDDIELFAAMSGDVNPAHLDAAYAASDGFHHVVAHGMW--GGALIS 71
PLN02864 PLN02864
enoyl-CoA hydratase
 101-216 7.99e-04

enoyl-CoA hydratase


Pssm-ID: 178455 [Multi-domain]  Cd Length: 310  Bit Score: 40.15  E-value: 7.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330191931 101 HKEIDTRANYDVTVSVG--HVESKARGIEFELCVQFFENDERVC------------GFD--SRYFSITSSQRGNKPAPIA 164
Cdd:PLN02864  104 YKPIPSSASVRNKVSIAglHDKGKAAILELETLSYEKDSGELLCmnrstiflrgagGFSnsSQPFSYSNYPTNQVSAVKI 183

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1330191931 165 DDFSAFQHIArlKITEQSVRGYARVSGDYNPIHLHRLTSAPFGFKKPIAHGL 216
Cdd:PLN02864  184 PKSQPDAVFE--DQTQPSQALLYRLSGDYNPLHSDPMFAKVAGFTRPILHGL 233
PRK13693 PRK13693
(3R)-hydroxyacyl-ACP dehydratase subunit HadB; Provisional
 176-264 1.03e-03

(3R)-hydroxyacyl-ACP dehydratase subunit HadB; Provisional


Pssm-ID: 184249 [Multi-domain]  Cd Length: 142  Bit Score: 38.66  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330191931 176 LKITEQSVRGYARVSGDYNPIHLHRLTSAPFGFKKPIAHGLYLLA------RSLVSLDIAPAEVEVNFKRPALLPIE--- 246
Cdd:PRK13693   20 YPLTRQDLVNYAGVSGDLNPIHWDDEIAKVVGLDTAIAHGMLTMGlgggyvTSWVGDPGAVTEYNVRFTAVVPVPNDgkg 99

                          90
                  ....*....|....*...
gi 1330191931 247 TELVQTGnQALLLNPESK 264
Cdd:PRK13693  100 AELVFNG-RVKSVDPESK 116
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH