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Conserved domains on  [gi|488258055|ref|WP_002329263|]
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MULTISPECIES: MaoC/PaaZ C-terminal domain-containing protein [Enterococcus]

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 ...
 16-141 2.07e-23

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: 88.76  E-value: 2.07e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258055  16 IEEGDSLSLTESIEDNQLLLYLGLTNDANPLYIQHDFAQKTEYHQPIVPSVMLMGIITSAISKHLPGPGSHVVNFSVNFI 95
Cdd:cd03449    1 LKVGDSASLTRTITEEDVELFAELSGDFNPIHLDEEYAKKTRFGGRIAHGMLTASLISAVLGTLLPGPGTIYLSQSLRFL 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 488258055  96 EPVFHYETLTFQFDVIKVDKMKDVVTISVEAENTNEDRVLD--AVVMV 141
Cdd:cd03449   81 RPVFIGDTVTATVTVTEKREDKKRVTLETVCTNQNGEVVIEgeAVVLA 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 ...
 16-141 2.07e-23

(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: 88.76  E-value: 2.07e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258055  16 IEEGDSLSLTESIEDNQLLLYLGLTNDANPLYIQHDFAQKTEYHQPIVPSVMLMGIITSAISKHLPGPGSHVVNFSVNFI 95
Cdd:cd03449    1 LKVGDSASLTRTITEEDVELFAELSGDFNPIHLDEEYAKKTRFGGRIAHGMLTASLISAVLGTLLPGPGTIYLSQSLRFL 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 488258055  96 EPVFHYETLTFQFDVIKVDKMKDVVTISVEAENTNEDRVLD--AVVMV 141
Cdd:cd03449   81 RPVFIGDTVTATVTVTEKREDKKRVTLETVCTNQNGEVVIEgeAVVLA 128
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
15-144 1.34e-22

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 87.25  E-value: 1.34e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258055  15 EIEEGDSLSL-TESIEDNQLLLYLGLTNDANPLYIQHDFAQKTEYHQPIVPSVMLMGIITSAISKHLPGPGS-HVVNFSV 92
Cdd:COG2030    4 DLEVGDVLPHgGRTVTEEDIVLFAGATGDPNPIHLDEEAAAATGFGGRIAHGMLTLSLASGLLVDDLPGTAVaNLGLQEV 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488258055  93 NFIEPVFHYETLTFQFDVIKVDKMKD--VVTISVEAENTNEDRVLDAVVMVQPP 144
Cdd:COG2030   84 RFLRPVRVGDTLRARVEVLEKRESKSrgIVTLRTTVTNQDGEVVLTGEATVLVP 137
PRK08190 PRK08190
bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated
 11-147 1.14e-10

bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated


Pssm-ID: 236180 [Multi-domain]  Cd Length: 466  Bit Score: 58.74  E-value: 1.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258055  11 KTINEIEEGDSLSLTESIEDNQLLLYLGLTNDANPLYIQHDFAQKTEYHQPIVPSVMLMGIITSAISKHLPGPGSHVVNF 90
Cdd:PRK08190   9 RTFDEIAIGDSASLVRTLTPDDIELFAAMSGDVNPAHLDAAYAASDGFHHVVAHGMWGGALISAVLGTRLPGPGTIYLGQ 88

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488258055  91 SVNFIEPVFHYETLTFQFDVIKVDKMKDVVTISVEAENTNEDRVLDAVVMVQPPQVP 147
Cdd:PRK08190  89 SLRFRRPVRIGDTLTVTVTVREKDPEKRIVVLDCRCTNQDGEVVITGTAEVIAPTEK 145
MaoC_dehydratas pfam01575
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ...
 2-129 1.40e-07

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: 47.72  E-value: 1.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258055    2 NIGKPRKLGKTIneieegdslSLTESiednQLLLYLGLTNDANPLYIQHDFAQKTEYHQPIVPSVMLMGIITSAISKHLP 81
Cdd:pfam01575   5 APGEPPDTEKPR---------TVTEA----DIALFALVSGDHNPIHVDPEFAKKAGFGGPIAHGMLTLAIVAGLVEEWGG 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 488258055   82 GPG-SHVVNFSVNFIEPVFHYETLTFQ---FDVIKVDKMKDVVTISVEAENT 129
Cdd:pfam01575  72 DNViARFGEIKVRFTKPVFPGDTLRTEaevVGKRDGRQTKVVEVTVEVTEVA 123
 
Name Accession Description Interval E-value
R_hydratase cd03449
(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA ...
 16-141 2.07e-23

(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: 88.76  E-value: 2.07e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258055  16 IEEGDSLSLTESIEDNQLLLYLGLTNDANPLYIQHDFAQKTEYHQPIVPSVMLMGIITSAISKHLPGPGSHVVNFSVNFI 95
Cdd:cd03449    1 LKVGDSASLTRTITEEDVELFAELSGDFNPIHLDEEYAKKTRFGGRIAHGMLTASLISAVLGTLLPGPGTIYLSQSLRFL 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 488258055  96 EPVFHYETLTFQFDVIKVDKMKDVVTISVEAENTNEDRVLD--AVVMV 141
Cdd:cd03449   81 RPVFIGDTVTATVTVTEKREDKKRVTLETVCTNQNGEVVIEgeAVVLA 128
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
15-144 1.34e-22

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 87.25  E-value: 1.34e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258055  15 EIEEGDSLSL-TESIEDNQLLLYLGLTNDANPLYIQHDFAQKTEYHQPIVPSVMLMGIITSAISKHLPGPGS-HVVNFSV 92
Cdd:COG2030    4 DLEVGDVLPHgGRTVTEEDIVLFAGATGDPNPIHLDEEAAAATGFGGRIAHGMLTLSLASGLLVDDLPGTAVaNLGLQEV 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488258055  93 NFIEPVFHYETLTFQFDVIKVDKMKD--VVTISVEAENTNEDRVLDAVVMVQPP 144
Cdd:COG2030   84 RFLRPVRVGDTLRARVEVLEKRESKSrgIVTLRTTVTNQDGEVVLTGEATVLVP 137
R_hydratase_like cd03441
(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl ...
 19-141 4.81e-16

(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: 69.99  E-value: 4.81e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258055  19 GDSLSLTESIEDNQLLLYLGLTNDANPLYIQHDFAQKTEYHQPIVPSVMLMGIITSAISKHLPG-PGSHVVNFSVNFIEP 97
Cdd:cd03441    1 GELDSSGRTVTEADIALFARLSGDPNPIHVDPEYAKAAGFGGRIAHGMLTLSLASGLLVQWLPGtDGANLGSQSVRFLAP 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 488258055  98 VFHYETLTFQFDVIKVDKMKD--VVTISVEAENTNEDRVLDAVVMV 141
Cdd:cd03441   81 VFPGDTLRVEVEVLGKRPSKGrgVVTVRTEARNQGGEVVLSGEATV 126
PRK08190 PRK08190
bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated
 11-147 1.14e-10

bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated


Pssm-ID: 236180 [Multi-domain]  Cd Length: 466  Bit Score: 58.74  E-value: 1.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258055  11 KTINEIEEGDSLSLTESIEDNQLLLYLGLTNDANPLYIQHDFAQKTEYHQPIVPSVMLMGIITSAISKHLPGPGSHVVNF 90
Cdd:PRK08190   9 RTFDEIAIGDSASLVRTLTPDDIELFAAMSGDVNPAHLDAAYAASDGFHHVVAHGMWGGALISAVLGTRLPGPGTIYLGQ 88

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488258055  91 SVNFIEPVFHYETLTFQFDVIKVDKMKDVVTISVEAENTNEDRVLDAVVMVQPPQVP 147
Cdd:PRK08190  89 SLRFRRPVRIGDTLTVTVTVREKDPEKRIVVLDCRCTNQDGEVVITGTAEVIAPTEK 145
SAV4209_like cd03453
SAV4209_like. Similar in sequence to the Streptomyces avermitilis SAV4209 protein, with a hot ...
 18-139 1.79e-08

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: 50.01  E-value: 1.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258055  18 EGDSL-SLTESIEDNQLLLYLGLTNDANPLYIQHDFAQKTEYHQPIVPSVMLMGIITSAISKHLPGPGShVVNFSVNF-- 94
Cdd:cd03453    1 VGDELpPLTPPVSRADLVRYAGASGDFNPIHYDEDFAKKVGLPGVIAHGMLTMGLLGRLVTDWVGDPGR-VVSFGVRFtk 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 488258055  95 IEPVFHYETLTFQFDVIKVDKMKDVVTISVEAENTNEDRVL--DAVV 139
Cdd:cd03453   80 PVPVPDTLTCTGIVVEKTVADGEDALTVTVDATDQAGGKKVlgRAIV 126
MaoC_like cd03446
MoaC_like Similar to the MaoC (monoamine oxidase C) dehydratase regulatory protein but ...
 15-141 8.57e-08

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: 48.45  E-value: 8.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258055  15 EIEEGDSL-SLTESIEDNQLLLYLGLTNDANPLYIQHDFAQKTEYHQPIVPSVMLMGIITSAISKhLPGPGSHVVNF--- 90
Cdd:cd03446    4 DFEIGQVFeSVGRTVTEADVVMFAGLSGDWNPIHTDAEYAKKTRFGERIAHGLLTLSIATGLLQR-LGVFERTVVAFygi 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488258055  91 -SVNFIEPVFHYETLTFQFDVI-KVDKMKD---VVTISVEAENTNEDRVLDAVVMV 141
Cdd:cd03446   83 dNLRFLNPVFIGDTIRAEAEVVeKEEKDGEdagVVTRRIEVVNQRGEVVQSGEMSL 138
MaoC_dehydratas pfam01575
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ...
 2-129 1.40e-07

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: 47.72  E-value: 1.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258055    2 NIGKPRKLGKTIneieegdslSLTESiednQLLLYLGLTNDANPLYIQHDFAQKTEYHQPIVPSVMLMGIITSAISKHLP 81
Cdd:pfam01575   5 APGEPPDTEKPR---------TVTEA----DIALFALVSGDHNPIHVDPEFAKKAGFGGPIAHGMLTLAIVAGLVEEWGG 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 488258055   82 GPG-SHVVNFSVNFIEPVFHYETLTFQ---FDVIKVDKMKDVVTISVEAENT 129
Cdd:pfam01575  72 DNViARFGEIKVRFTKPVFPGDTLRTEaevVGKRDGRQTKVVEVTVEVTEVA 123
FkbR2 cd03451
FkbR2 is a Streptomyces hygroscopicus protein with a hot dog fold that belongs to a conserved ...
 23-142 3.30e-06

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: 44.12  E-value: 3.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258055  23 SLTESieDNQLllYLGLTNDANPLYIQHDFAQKTEYHQPIVPSVMLMGIitsAISKHLPGPGSHVV-NF---SVNFIEPV 98
Cdd:cd03451   20 TVTEA--DNVL--FTLLTMNTAPLHFDAAYAAKTEFGRRLVNSLFTLSL---ALGLSVNDTSLTAVaNLgydEVRFPAPV 92

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488258055  99 FHYETLTFQFDVIKVDKMKD-----VVTISVEAENTNEDRVLDAV--VMVQ 142
Cdd:cd03451   93 FHGDTLYAESEVLSKRESKSrpdagIVTVRTVGYNQDGEPVLSFErtALVP 143
SAV4209 cd03455
SAV4209 is a Streptomyces avermitilis protein with a hot dog fold that is similar to those of ...
 28-142 3.82e-05

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: 41.15  E-value: 3.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258055  28 IEDNQLLLYLGLTNDANPLYIQHDFAQKTEYHQPIVPSVMLMGIITSAISKHLpGPGSHVVNFSVNFIEPVFHYETLTFQ 107
Cdd:cd03455   11 PDPTLLFRYSAATRDFHRIHHDRDYARAVGYPDLYVNGPTLAGLVIRYVTDWA-GPDARVKSFAFRLGAPLYAGDTLRFG 89

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 488258055 108 FDVIKVDKmKDVVTISVEAENTNEDRVLDAVVMVQ 142
Cdd:cd03455   90 GRVTAKRD-DEVVTVELWARNSEGDHVMAGTATVA 123
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 59-141 5.10e-05

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: 40.15  E-value: 5.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258055  59 HQPIVPSVMLMGIITSAISKHLPGPGSH-----VVNFSVNFIEPVFHYETLTFQFDVIKVDkmKDVVTISVEAENTNEDR 133
Cdd:cd03440   14 GGGIVHGGLLLALADEAAGAAAARLGGRglgavTLSLDVRFLRPVRPGDTLTVEAEVVRVG--RSSVTVEVEVRNEDGKL 91


                 ....*...
gi 488258055 134 VLDAVVMV 141
Cdd:cd03440   92 VATATATF 99
HDE_HSD cd03448
HDE_HSD The R-hydratase-like hot dog fold of the 17-beta-hydroxysteriod dehydrogenase (HSD), ...
 23-123 9.91e-05

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: 39.90  E-value: 9.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258055  23 SLTESIEDNQLLLYlGLTNDANPLYIQHDFAQKTEYHQPIVPSVMLMGIITSAISKHL-PGPGSHVVNFSVNFIEPVFHY 101
Cdd:cd03448    8 VVEIPTSPDQALLY-RLSGDYNPLHIDPAFAKAAGFPRPILHGLCTYGFAARAVLEAFaDGDPARFKAIKVRFSSPVFPG 86

                         90       100       110
                 ....*....|....*....|....*....|...
gi 488258055 102 ETL-----------TFQFDVikvdKMKDVVTIS 123
Cdd:cd03448   87 ETLrtemwkegnrvIFQTKV----VERDVVVLS 115
PLN02864 PLN02864
enoyl-CoA hydratase
 26-104 2.64e-04

enoyl-CoA hydratase


Pssm-ID: 178455 [Multi-domain]  Cd Length: 310  Bit Score: 39.77  E-value: 2.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258055  26 ESIEDNQLLLYlGLTNDANPLYIQHDFAQKTEYHQPIVPSVMLMGIITSAISKHL-PGPGSHVVNFSVNFIEPVFHYETL 104
Cdd:PLN02864 194 DQTQPSQALLY-RLSGDYNPLHSDPMFAKVAGFTRPILHGLCTLGFAVRAVIKCFcNGDPTAVKTISGRFLLHVYPGETL 272
 
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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