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Conserved domains on  [gi|872680174|ref|WP_048543230|]
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MULTISPECIES: MaoC family dehydratase [Bacillus]

Protein Classification

MaoC family dehydratase( domain architecture ID 10130975)

MaoC family dehydratase similar to Aeromonas caviae (R)-specific enoyl-CoA hydratase that is involved in polyhydroxyalkanoate biosynthesis, and Methylorubrum extorquens 3-hydroxybutyryl-CoA dehydratase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
R_hydratase cd03449
(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA ...
 5-131 3.86e-56

(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: 171.19  E-value: 3.86e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872680174   5 STGQQASCSKTITETDFVLFAGLSGDFNPIHIDHEYAKQTRFNQRIAHGLLTSSLLSQLLGIHLPGKGSVYMEQTIKFTA 84
Cdd:cd03449    2 KVGDSASLTRTITEEDVELFAELSGDFNPIHLDEEYAKKTRFGGRIAHGMLTASLISAVLGTLLPGPGTIYLSQSLRFLR 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 872680174  85 PVFIGDTITATATVQEFMIEKRVLKLLTECHNQKGDLVLTGVATMMV 131
Cdd:cd03449   82 PVFIGDTVTATVTVTEKREDKKRVTLETVCTNQNGEVVIEGEAVVLA 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 ...
 5-131 3.86e-56

(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: 171.19  E-value: 3.86e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872680174   5 STGQQASCSKTITETDFVLFAGLSGDFNPIHIDHEYAKQTRFNQRIAHGLLTSSLLSQLLGIHLPGKGSVYMEQTIKFTA 84
Cdd:cd03449    2 KVGDSASLTRTITEEDVELFAELSGDFNPIHLDEEYAKKTRFGGRIAHGMLTASLISAVLGTLLPGPGTIYLSQSLRFLR 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 872680174  85 PVFIGDTITATATVQEFMIEKRVLKLLTECHNQKGDLVLTGVATMMV 131
Cdd:cd03449   82 PVFIGDTVTATVTVTEKREDKKRVTLETVCTNQNGEVVIEGEAVVLA 128
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
13-135 1.59e-40

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 131.93  E-value: 1.59e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872680174  13 SKTITETDFVLFAGLSGDFNPIHIDHEYAKQTRFNQRIAHGLLTSSLLSQLLGIHLPGKGSV-YMEQTIKFTAPVFIGDT 91
Cdd:COG2030   15 GRTVTEEDIVLFAGATGDPNPIHLDEEAAAATGFGGRIAHGMLTLSLASGLLVDDLPGTAVAnLGLQEVRFLRPVRVGDT 94

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 872680174  92 ITATATVqefmIEKR------VLKLLTECHNQKGDLVLTGVATMMVPKEG 135
Cdd:COG2030   95 LRARVEV----LEKResksrgIVTLRTTVTNQDGEVVLTGEATVLVPRRP 140
PRK08190 PRK08190
bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated
 7-134 7.56e-39

bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated


Pssm-ID: 236180 [Multi-domain]  Cd Length: 466  Bit Score: 135.78  E-value: 7.56e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872680174   7 GQQASCSKTITETDFVLFAGLSGDFNPIHIDHEYAKQTRFNQRIAHGLLTSSLLSQLLGIHLPGKGSVYMEQTIKFTAPV 86
Cdd:PRK08190  17 GDSASLVRTLTPDDIELFAAMSGDVNPAHLDAAYAASDGFHHVVAHGMWGGALISAVLGTRLPGPGTIYLGQSLRFRRPV 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 872680174  87 FIGDTITATATVQEFMIEKRVLKLLTECHNQKGDLVLTGVATMMVPKE 134
Cdd:PRK08190  97 RIGDTLTVTVTVREKDPEKRIVVLDCRCTNQDGEVVITGTAEVIAPTE 144
MaoC_dehydratas pfam01575
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ...
 13-106 1.62e-20

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: 80.46  E-value: 1.62e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872680174   13 SKTITETDFVLFAGLSGDFNPIHIDHEYAKQTRFNQRIAHGLLTSSLLSQLLGIHLPGKG-SVYMEQTIKFTAPVFIGDT 91
Cdd:pfam01575  15 PRTVTEADIALFALVSGDHNPIHVDPEFAKKAGFGGPIAHGMLTLAIVAGLVEEWGGDNViARFGEIKVRFTKPVFPGDT 94

                          90
                  ....*....|....*
gi 872680174   92 ITATATVQEfMIEKR 106
Cdd:pfam01575  95 LRTEAEVVG-KRDGR 108
 
Name Accession Description Interval E-value
R_hydratase cd03449
(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA ...
 5-131 3.86e-56

(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: 171.19  E-value: 3.86e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872680174   5 STGQQASCSKTITETDFVLFAGLSGDFNPIHIDHEYAKQTRFNQRIAHGLLTSSLLSQLLGIHLPGKGSVYMEQTIKFTA 84
Cdd:cd03449    2 KVGDSASLTRTITEEDVELFAELSGDFNPIHLDEEYAKKTRFGGRIAHGMLTASLISAVLGTLLPGPGTIYLSQSLRFLR 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 872680174  85 PVFIGDTITATATVQEFMIEKRVLKLLTECHNQKGDLVLTGVATMMV 131
Cdd:cd03449   82 PVFIGDTVTATVTVTEKREDKKRVTLETVCTNQNGEVVIEGEAVVLA 128
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
13-135 1.59e-40

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 131.93  E-value: 1.59e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872680174  13 SKTITETDFVLFAGLSGDFNPIHIDHEYAKQTRFNQRIAHGLLTSSLLSQLLGIHLPGKGSV-YMEQTIKFTAPVFIGDT 91
Cdd:COG2030   15 GRTVTEEDIVLFAGATGDPNPIHLDEEAAAATGFGGRIAHGMLTLSLASGLLVDDLPGTAVAnLGLQEVRFLRPVRVGDT 94

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 872680174  92 ITATATVqefmIEKR------VLKLLTECHNQKGDLVLTGVATMMVPKEG 135
Cdd:COG2030   95 LRARVEV----LEKResksrgIVTLRTTVTNQDGEVVLTGEATVLVPRRP 140
PRK08190 PRK08190
bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated
 7-134 7.56e-39

bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated


Pssm-ID: 236180 [Multi-domain]  Cd Length: 466  Bit Score: 135.78  E-value: 7.56e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872680174   7 GQQASCSKTITETDFVLFAGLSGDFNPIHIDHEYAKQTRFNQRIAHGLLTSSLLSQLLGIHLPGKGSVYMEQTIKFTAPV 86
Cdd:PRK08190  17 GDSASLVRTLTPDDIELFAAMSGDVNPAHLDAAYAASDGFHHVVAHGMWGGALISAVLGTRLPGPGTIYLGQSLRFRRPV 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 872680174  87 FIGDTITATATVQEFMIEKRVLKLLTECHNQKGDLVLTGVATMMVPKE 134
Cdd:PRK08190  97 RIGDTLTVTVTVREKDPEKRIVVLDCRCTNQDGEVVITGTAEVIAPTE 144
R_hydratase_like cd03441
(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl ...
 7-130 1.80e-35

(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: 118.91  E-value: 1.80e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872680174   7 GQQASCSKTITETDFVLFAGLSGDFNPIHIDHEYAKQTRFNQRIAHGLLTSSLLSQLLGIHLPGK-GSVYMEQTIKFTAP 85
Cdd:cd03441    1 GELDSSGRTVTEADIALFARLSGDPNPIHVDPEYAKAAGFGGRIAHGMLTLSLASGLLVQWLPGTdGANLGSQSVRFLAP 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 872680174  86 VFIGDTITATATVQEFMIEK--RVLKLLTECHNQKGDLVLTGVATMM 130
Cdd:cd03441   81 VFPGDTLRVEVEVLGKRPSKgrGVVTVRTEARNQGGEVVLSGEATVL 127
MaoC_like cd03446
MoaC_like Similar to the MaoC (monoamine oxidase C) dehydratase regulatory protein but ...
 14-131 6.72e-28

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: 100.07  E-value: 6.72e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872680174  14 KTITETDFVLFAGLSGDFNPIHIDHEYAKQTRFNQRIAHGLLTSSLLS---QLLGIHLPGKGSVYMEQTIKFTAPVFIGD 90
Cdd:cd03446   16 RTVTEADVVMFAGLSGDWNPIHTDAEYAKKTRFGERIAHGLLTLSIATgllQRLGVFERTVVAFYGIDNLRFLNPVFIGD 95

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 872680174  91 TITATATV---QEFMIEKR-VLKLLTECHNQKGDLVLTGVATMMV 131
Cdd:cd03446   96 TIRAEAEVvekEEKDGEDAgVVTRRIEVVNQRGEVVQSGEMSLLV 140
FkbR2 cd03451
FkbR2 is a Streptomyces hygroscopicus protein with a hot dog fold that belongs to a conserved ...
 14-135 7.59e-22

FkbR2 is a Streptomyces hygroscopicus protein with a hot dog fold that belongs to a conserved family of proteins found in prokaryotes and archaea but not in eukaryotes. FkbR2 has sequence similarity to (R)-specific enoyl-CoA hydratase, the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit. The function of FkbR2 is unknown.


Pssm-ID: 239535 [Multi-domain]  Cd Length: 146  Bit Score: 84.56  E-value: 7.59e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872680174  14 KTITETDFVLFAGLSGDFNPIHIDHEYAKQTRFNQRIAHGLLTSSLLS--QLLGIHLPGKGSVYMEQtIKFTAPVFIGDT 91
Cdd:cd03451   19 RTVTEADNVLFTLLTMNTAPLHFDAAYAAKTEFGRRLVNSLFTLSLALglSVNDTSLTAVANLGYDE-VRFPAPVFHGDT 97

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 872680174  92 ITATATVqefmIEKR---------VLKLLTECHNQKGDLVLTGVATMMVPKEG 135
Cdd:cd03451   98 LYAESEV----LSKResksrpdagIVTVRTVGYNQDGEPVLSFERTALVPKRG 146
MaoC_dehydratas pfam01575
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ...
 13-106 1.62e-20

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: 80.46  E-value: 1.62e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872680174   13 SKTITETDFVLFAGLSGDFNPIHIDHEYAKQTRFNQRIAHGLLTSSLLSQLLGIHLPGKG-SVYMEQTIKFTAPVFIGDT 91
Cdd:pfam01575  15 PRTVTEADIALFALVSGDHNPIHVDPEFAKKAGFGGPIAHGMLTLAIVAGLVEEWGGDNViARFGEIKVRFTKPVFPGDT 94

                          90
                  ....*....|....*
gi 872680174   92 ITATATVQEfMIEKR 106
Cdd:pfam01575  95 LRTEAEVVG-KRDGR 108
SAV4209_like cd03453
SAV4209_like. Similar in sequence to the Streptomyces avermitilis SAV4209 protein, with a hot ...
 16-127 1.08e-14

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: 65.81  E-value: 1.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872680174  16 ITETDFVLFAGLSGDFNPIHIDHEYAKQTRFNQRIAHGLLTSSLLSQLLGIHLPGKGSVyMEQTIKFTAPVFIGDTITAT 95
Cdd:cd03453   12 VSRADLVRYAGASGDFNPIHYDEDFAKKVGLPGVIAHGMLTMGLLGRLVTDWVGDPGRV-VSFGVRFTKPVPVPDTLTCT 90

                         90       100       110
                 ....*....|....*....|....*....|....
gi 872680174  96 ATVQE--FMIEKRVLKLLTECHNQKGDLVLTGVA 127
Cdd:cd03453   91 GIVVEktVADGEDALTVTVDATDQAGGKKVLGRA 124
MaoC_C cd03452
MaoC_C The C-terminal hot dog fold of the MaoC (monoamine oxidase C) dehydratase regulatory ...
 13-135 3.23e-13

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: 62.42  E-value: 3.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872680174  13 SKTITETDFVLFAGLSGDFNPIHIDHEYAKQTRFNQRIAHGlltSSLLSQLLGIHL-PGKGSV---YMEQTIKFTAPVFI 88
Cdd:cd03452   15 RRTVTEADIVNFACLTGDHFYAHMDEIAAKASFFGKRVAHG---YFVLSAAAGLFVdPAPGPVlanYGLENLRFLEPVYP 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 872680174  89 GDTITATATVQEFMIEKR----VLKLLTECHNQKGDLVLTGVATMMVPKEG 135
Cdd:cd03452   92 GDTIQVRLTCKRKIPRDGqdygVVRWDAEVTNQNGELVASYDILTLVAKKG 142
YdeM cd03454
YdeM is a Bacillus subtilis protein that belongs to a family of prokaryotic proteins of unkown ...
 13-132 2.27e-11

YdeM is a Bacillus subtilis protein that belongs to a family of prokaryotic proteins of unkown function. YdeM has sequence similarity to the hot-dog fold of (R)-specific enoyl-CoA hydratase. Other enzymes with this fold include the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit.


Pssm-ID: 239538 [Multi-domain]  Cd Length: 140  Bit Score: 57.19  E-value: 2.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872680174  13 SKTITETDFVLFAGlsgDFNP--IHIDHEYAKQTRFNQRIA---HGLLTSSLLSQLLGIHLP-GKGSVYMEQtIKFTAPV 86
Cdd:cd03454   14 SYTVTEEEIIAFAR---EFDPqpFHLDEEAAKESLFGGLAAsgwHTAAITMRLLVDAGLSGSaSGGSPGIDE-LRWPRPV 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 872680174  87 FIGDTITATATVqefmIEKR---------VLKLLTECHNQKGDLVLTGVATMMVP 132
Cdd:cd03454   90 RPGDTLSVEVEV----LDKRpsrsrpdrgIVTLRSETLNQRGEVVLTFEATVLVR 140
PRK13693 PRK13693
(3R)-hydroxyacyl-ACP dehydratase subunit HadB; Provisional
 15-88 9.06e-09

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


Pssm-ID: 184249 [Multi-domain]  Cd Length: 142  Bit Score: 50.60  E-value: 9.06e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 872680174  15 TITETDFVLFAGLSGDFNPIHIDHEYAKQTRFNQRIAHGLLTSSLLSQLLGIHLPGKGSVyMEQTIKFTAPVFI 88
Cdd:PRK13693  21 PLTRQDLVNYAGVSGDLNPIHWDDEIAKVVGLDTAIAHGMLTMGLGGGYVTSWVGDPGAV-TEYNVRFTAVVPV 93
SAV4209 cd03455
SAV4209 is a Streptomyces avermitilis protein with a hot dog fold that is similar to those of ...
 13-128 2.10e-08

SAV4209 is a Streptomyces avermitilis 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. The alpha- and gamma-proteobacterial members of this CD have, in addition to a hot dog fold, an N-terminal extension.


Pssm-ID: 239539 [Multi-domain]  Cd Length: 123  Bit Score: 49.24  E-value: 2.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872680174  13 SKTITETDFVLFAGLSGDFNPIHIDHEYAKQTRFNQRIAHGLLTSSLLSQLLGIHLPGKGSVymeQTIKF--TAPVFIGD 90
Cdd:cd03455    8 SIPPDPTLLFRYSAATRDFHRIHHDRDYARAVGYPDLYVNGPTLAGLVIRYVTDWAGPDARV---KSFAFrlGAPLYAGD 84

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 872680174  91 TITATATVQEFMIEKRVlKLLTECHNQKGDLVLTGVAT 128
Cdd:cd03455   85 TLRFGGRVTAKRDDEVV-TVELWARNSEGDHVMAGTAT 121
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 67-130 4.44e-08

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: 47.86  E-value: 4.44e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 872680174  67 HLPGKGSVYMEQTIKFTAPVFIGDTITATATVQEfmIEKRVLKLLTECHNQKGDLVLTGVATMM 130
Cdd:cd03440   39 GGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVR--VGRSSVTVEVEVRNEDGKLVATATATFV 100
HDE_HSD cd03448
HDE_HSD The R-hydratase-like hot dog fold of the 17-beta-hydroxysteriod dehydrogenase (HSD), ...
 27-93 1.18e-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: 44.52  E-value: 1.18e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 872680174  27 LSGDFNPIHIDHEYAKQTRFNQRIAHGlltssllSQLLGI-------HLpGKGSVYMEQTIK--FTAPVFIGDTIT 93
Cdd:cd03448   23 LSGDYNPLHIDPAFAKAAGFPRPILHG-------LCTYGFaaravleAF-ADGDPARFKAIKvrFSSPVFPGETLR 90
MaoC_dehydrat_N pfam13452
N-terminal half of MaoC dehydratase; It is clear from the structures of bacterial members of ...
 15-124 1.66e-06

N-terminal half of MaoC dehydratase; It is clear from the structures of bacterial members of MaoC dehydratase, pfam01575, that the full-length functional dehydratase enzyme is made up of two structures that dimerize to form a whole. Divergence of the N- and C- monomers in higher eukaryotes has led to two distinct domains, this one and MaoC_dehydratas. However, in order to function as an enzyme both are required together.


Pssm-ID: 433220 [Multi-domain]  Cd Length: 132  Bit Score: 44.22  E-value: 1.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872680174   15 TITETDFVLFAGLSGDFNPIHIDHEYAKQTRFNQRIAH----GLLTSSLLSQLLGIHLPGKGSVYMEQTIKFTAPVFIGD 90
Cdd:pfam13452  13 EVERGAIREFARAIGETNPAYWDEAAARAAGYGDLPAPptflFVLGWDAPGFMEQLGIDLSRLLHGEQRFTYHRPLRAGD 92

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 872680174   91 TITATATVQEFMIEKRV--LKLL---TECHNQKGDLVLT 124
Cdd:pfam13452  93 ELTCRSQIADVYDKKGNgaLCFVvveTEVTNQRGEPVAT 131
FAS_MaoC cd03447
FAS_MaoC, the MaoC-like hot dog fold of the fatty acid synthase, beta subunit. Other enzymes ...
 24-127 1.05e-05

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: 41.88  E-value: 1.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872680174  24 FAGLSGDFNPIHIDHEYAKQTRFNQRIAHGLLTSSLLSQLLGiHLPGKGSVY--MEQTIKFTAPVFIGDTItaTATVQEF 101
Cdd:cd03447   18 YARVSGDFNPIHVSRVFASYAGLPGTITHGMYTSAAVRALVE-TWAADNDRSrvRSFTASFVGMVLPNDEL--EVRLEHV 94

                         90       100
                 ....*....|....*....|....*....
gi 872680174 102 -MIEKR-VLKLltECHNQK-GDLVLTGVA 127
Cdd:cd03447   95 gMVDGRkVIKV--EARNEEtGELVLRGEA 121
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 79-134 9.05e-05

Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 39.54  E-value: 9.05e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 872680174  79 TIKFTAPVFIGDTITATATVQEfmIEKRVLKLLTECHNQKGDLVLTGVATMMVPKE 134
Cdd:COG2050   83 NINFLRPARLGDRLTAEARVVR--RGRRLAVVEVEVTDEDGKLVATATGTFAVLPK 136
PLN02864 PLN02864
enoyl-CoA hydratase
 27-53 1.11e-03

enoyl-CoA hydratase


Pssm-ID: 178455 [Multi-domain]  Cd Length: 310  Bit Score: 37.46  E-value: 1.11e-03
                         10        20
                 ....*....|....*....|....*..
gi 872680174  27 LSGDFNPIHIDHEYAKQTRFNQRIAHG 53
Cdd:PLN02864 206 LSGDYNPLHSDPMFAKVAGFTRPILHG 232
NodN cd03450
NodN (nodulation factor N) contains a single hot dog fold similar to those of the peroxisomal ...
 15-100 9.65e-03

NodN (nodulation factor N) contains a single hot dog fold similar to those of the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit. Rhizobium and related species form nodules on the roots of their legume hosts, a symbiotic process that requires production of Nod factors, which are signal molecules involved in root hair deformation and meristematic cell division. The nodulation gene products, including NodN, are involved in producing the Nod factors, however the role played by NodN is unclear.


Pssm-ID: 239534 [Multi-domain]  Cd Length: 149  Bit Score: 34.08  E-value: 9.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872680174  15 TITETDFVLFAGLSGDFNPIHIDHEYAKQTRFNQRIAHGLLT--SSLLSQLLGIHLPG-KGSV-YMEQTIKFTAPVFIGD 90
Cdd:cd03450   23 TVDQERIDQFADATGDHQWIHVDPERAAAEPFGGTIAHGFLTlsLLPALTPQLFRVEGvKMGVnYGLDKVRFPAPVPVGS 102

                         90
                 ....*....|
gi 872680174  91 TITATATVQE 100
Cdd:cd03450  103 RVRGRFTLLS 112
 
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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