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Conserved domains on  [gi|76556761|emb|CAI48335|]
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MaoC domain protein [Natronomonas pharaonis DSM 2160]

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 ...
 32-154 1.19e-47

(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: 150.39  E-value: 1.19e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76556761  32 SVGDTLRFSKPVSEADVERFALASGDTNPLHLDEASAAGTRFGGRIVHGGLIAGIISAALA-RLPG-TVVYLEQDLTFRS 109
Cdd:cd03449   2 KVGDSASLTRTITEEDVELFAELSGDFNPIHLDEEYAKKTRFGGRIAHGMLTASLISAVLGtLLPGpGTIYLSQSLRFLR 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 76556761 110 PVRIGETVTAELEVVDDLSEAK-YRLRTVART-DGDAAVEGTATVLI 154
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 ...
 32-154 1.19e-47

(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: 150.39  E-value: 1.19e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76556761  32 SVGDTLRFSKPVSEADVERFALASGDTNPLHLDEASAAGTRFGGRIVHGGLIAGIISAALA-RLPG-TVVYLEQDLTFRS 109
Cdd:cd03449   2 KVGDSASLTRTITEEDVELFAELSGDFNPIHLDEEYAKKTRFGGRIAHGMLTASLISAVLGtLLPGpGTIYLSQSLRFLR 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 76556761 110 PVRIGETVTAELEVVDDLSEAK-YRLRTVART-DGDAAVEGTATVLI 154
Cdd:cd03449  82 PVFIGDTVTATVTVTEKREDKKrVTLETVCTNqNGEVVIEGEAVVLA 128
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
32-155 4.37e-35

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 118.83  E-value: 4.37e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76556761  32 SVGDTLRF-SKPVSEADVERFALASGDTNPLHLDEASAAGTRFGGRIVHGGLIAGIISAALA-RLPGTVV--YLEQDLTF 107
Cdd:COG2030   6 EVGDVLPHgGRTVTEEDIVLFAGATGDPNPIHLDEEAAAATGFGGRIAHGMLTLSLASGLLVdDLPGTAVanLGLQEVRF 85

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 76556761 108 RSPVRIGETVTAELEVVD---DLSEAKYRLRTVART-DGDAAVEGTATVLIE 155
Cdd:COG2030  86 LRPVRVGDTLRARVEVLEkreSKSRGIVTLRTTVTNqDGEVVLTGEATVLVP 137
PRK08190 PRK08190
bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated
 30-153 3.08e-27

bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated


Pssm-ID: 236180 [Multi-domain]  Cd Length: 466  Bit Score: 105.35  E-value: 3.08e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76556761   30 EPSVGDTLRFSKPVSEADVERFALASGDTNPLHLDEASAAGTRFGGRIVHGGLIAGIISAALA-RLPGT-VVYLEQDLTF 107
Cdd:PRK08190  13 EIAIGDSASLVRTLTPDDIELFAAMSGDVNPAHLDAAYAASDGFHHVVAHGMWGGALISAVLGtRLPGPgTIYLGQSLRF 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 76556761  108 RSPVRIGETVTAELEVVDDLSEAKY-RLRTVART-DGDAAVEGTATVL 153
Cdd:PRK08190  93 RRPVRIGDTLTVTVTVREKDPEKRIvVLDCRCTNqDGEVVITGTAEVI 140
MaoC_dehydratas pfam01575
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ...
 30-142 1.73e-24

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: 91.25  E-value: 1.73e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76556761    30 EPSVGDTLRFSK--PVSEADVERFALASGDTNPLHLDEASAAGTRFGGRIVHGGLIAGIISAALARLPGTVV---YLEQD 104
Cdd:pfam01575   3 QNAPGEPPDTEKprTVTEADIALFALVSGDHNPIHVDPEFAKKAGFGGPIAHGMLTLAIVAGLVEEWGGDNViarFGEIK 82

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 76556761   105 LTFRSPVRIGETVTAELEVVDDlsEAKYRLRTVARTDG 142
Cdd:pfam01575  83 VRFTKPVFPGDTLRTEAEVVGK--RDGRQTKVVEVTVE 118
 
Name Accession Description Interval E-value
R_hydratase cd03449
(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA ...
 32-154 1.19e-47

(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: 150.39  E-value: 1.19e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76556761  32 SVGDTLRFSKPVSEADVERFALASGDTNPLHLDEASAAGTRFGGRIVHGGLIAGIISAALA-RLPG-TVVYLEQDLTFRS 109
Cdd:cd03449   2 KVGDSASLTRTITEEDVELFAELSGDFNPIHLDEEYAKKTRFGGRIAHGMLTASLISAVLGtLLPGpGTIYLSQSLRFLR 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 76556761 110 PVRIGETVTAELEVVDDLSEAK-YRLRTVART-DGDAAVEGTATVLI 154
Cdd:cd03449  82 PVFIGDTVTATVTVTEKREDKKrVTLETVCTNqNGEVVIEGEAVVLA 128
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
32-155 4.37e-35

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 118.83  E-value: 4.37e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76556761  32 SVGDTLRF-SKPVSEADVERFALASGDTNPLHLDEASAAGTRFGGRIVHGGLIAGIISAALA-RLPGTVV--YLEQDLTF 107
Cdd:COG2030   6 EVGDVLPHgGRTVTEEDIVLFAGATGDPNPIHLDEEAAAATGFGGRIAHGMLTLSLASGLLVdDLPGTAVanLGLQEVRF 85

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 76556761 108 RSPVRIGETVTAELEVVD---DLSEAKYRLRTVART-DGDAAVEGTATVLIE 155
Cdd:COG2030  86 LRPVRVGDTLRARVEVLEkreSKSRGIVTLRTTVTNqDGEVVLTGEATVLVP 137
R_hydratase_like cd03441
(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl ...
 34-153 3.17e-30

(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: 106.19  E-value: 3.17e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76556761  34 GDTLRFSKPVSEADVERFALASGDTNPLHLDEASAAGTRFGGRIVHGGLIAGIISAALARLPGT---VVYLEQDLTFRSP 110
Cdd:cd03441   1 GELDSSGRTVTEADIALFARLSGDPNPIHVDPEYAKAAGFGGRIAHGMLTLSLASGLLVQWLPGtdgANLGSQSVRFLAP 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 76556761 111 VRIGETVTAELEVVDDLSEAKY---RLRTVAR-TDGDAAVEGTATVL 153
Cdd:cd03441  81 VFPGDTLRVEVEVLGKRPSKGRgvvTVRTEARnQGGEVVLSGEATVL 127
PRK08190 PRK08190
bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated
 30-153 3.08e-27

bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated


Pssm-ID: 236180 [Multi-domain]  Cd Length: 466  Bit Score: 105.35  E-value: 3.08e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76556761   30 EPSVGDTLRFSKPVSEADVERFALASGDTNPLHLDEASAAGTRFGGRIVHGGLIAGIISAALA-RLPGT-VVYLEQDLTF 107
Cdd:PRK08190  13 EIAIGDSASLVRTLTPDDIELFAAMSGDVNPAHLDAAYAASDGFHHVVAHGMWGGALISAVLGtRLPGPgTIYLGQSLRF 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 76556761  108 RSPVRIGETVTAELEVVDDLSEAKY-RLRTVART-DGDAAVEGTATVL 153
Cdd:PRK08190  93 RRPVRIGDTLTVTVTVREKDPEKRIvVLDCRCTNqDGEVVITGTAEVI 140
MaoC_dehydratas pfam01575
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ...
 30-142 1.73e-24

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: 91.25  E-value: 1.73e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76556761    30 EPSVGDTLRFSK--PVSEADVERFALASGDTNPLHLDEASAAGTRFGGRIVHGGLIAGIISAALARLPGTVV---YLEQD 104
Cdd:pfam01575   3 QNAPGEPPDTEKprTVTEADIALFALVSGDHNPIHVDPEFAKKAGFGGPIAHGMLTLAIVAGLVEEWGGDNViarFGEIK 82

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 76556761   105 LTFRSPVRIGETVTAELEVVDDlsEAKYRLRTVARTDG 142
Cdd:pfam01575  83 VRFTKPVFPGDTLRTEAEVVGK--RDGRQTKVVEVTVE 118
MaoC_like cd03446
MoaC_like Similar to the MaoC (monoamine oxidase C) dehydratase regulatory protein but ...
 43-154 8.14e-20

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: 80.04  E-value: 8.14e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76556761  43 VSEADVERFALASGDTNPLHLDEASAAGTRFGGRIVHGGLIAGIISAALARLPG---TVV--YLEQDLTFRSPVRIGETV 117
Cdd:cd03446  18 VTEADVVMFAGLSGDWNPIHTDAEYAKKTRFGERIAHGLLTLSIATGLLQRLGVferTVVafYGIDNLRFLNPVFIGDTI 97

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 76556761 118 TAELEVV-------DDLSEAKYRLRTVARtDGDAAVEGTATVLI 154
Cdd:cd03446  98 RAEAEVVekeekdgEDAGVVTRRIEVVNQ-RGEVVQSGEMSLLV 140
FkbR2 cd03451
FkbR2 is a Streptomyces hygroscopicus protein with a hot dog fold that belongs to a conserved ...
 32-154 2.03e-13

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: 63.38  E-value: 2.03e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76556761  32 SVGDTLR--FSKPVSEADVERFALASGDTNPLHLDEASAAGTRFGGRIVHGGLIAGIISAALAR-LPGTVV----YleQD 104
Cdd:cd03451   8 TVGQVFEhaPGRTVTEADNVLFTLLTMNTAPLHFDAAYAAKTEFGRRLVNSLFTLSLALGLSVNdTSLTAVanlgY--DE 85

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 76556761 105 LTFRSPVRIGETVTAELEVVdDLSEAKYR-------LRTVARTDGDAAV-EGTATVLI 154
Cdd:cd03451  86 VRFPAPVFHGDTLYAESEVL-SKRESKSRpdagivtVRTVGYNQDGEPVlSFERTALV 142
SAV4209_like cd03453
SAV4209_like. Similar in sequence to the Streptomyces avermitilis SAV4209 protein, with a hot ...
 33-152 2.60e-12

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: 60.03  E-value: 2.60e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76556761  33 VGDTL-RFSKPVSEADVERFALASGDTNPLHLDEASAAGTRFGGRIVHGGLIAGIISAAL---ARLPGTVVylEQDLTFR 108
Cdd:cd03453   1 VGDELpPLTPPVSRADLVRYAGASGDFNPIHYDEDFAKKVGLPGVIAHGMLTMGLLGRLVtdwVGDPGRVV--SFGVRFT 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 76556761 109 SPVRIGETVTAELEVVDDLSEAKYRLRTVA----RTDGDAAVEGTATV 152
Cdd:cd03453  79 KPVPVPDTLTCTGIVVEKTVADGEDALTVTvdatDQAGGKKVLGRAIV 126
MaoC_C cd03452
MaoC_C The C-terminal hot dog fold of the MaoC (monoamine oxidase C) dehydratase regulatory ...
 33-121 1.40e-11

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: 58.57  E-value: 1.40e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76556761  33 VGDTL-RFSKPVSEADVERFALASGDTNPLHLDEASAAGTRFGGRIVHGGLiagIISAALARL----PGTVV--YLEQDL 105
Cdd:cd03452   7 PGDSLlTHRRTVTEADIVNFACLTGDHFYAHMDEIAAKASFFGKRVAHGYF---VLSAAAGLFvdpaPGPVLanYGLENL 83

                        90
                ....*....|....*.
gi 76556761 106 TFRSPVRIGETVTAEL 121
Cdd:cd03452  84 RFLEPVYPGDTIQVRL 99
HDE_HSD cd03448
HDE_HSD The R-hydratase-like hot dog fold of the 17-beta-hydroxysteriod dehydrogenase (HSD), ...
 55-153 5.27e-08

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: 48.75  E-value: 5.27e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76556761  55 SGDTNPLHLDEASAAGTRFGGRIVHG----GLIA-GIISAALARLPGTVVYLeqDLTFRSPVRIGETVTAELEVVDDlse 129
Cdd:cd03448  24 SGDYNPLHIDPAFAKAAGFPRPILHGlctyGFAArAVLEAFADGDPARFKAI--KVRFSSPVFPGETLRTEMWKEGN--- 98

                        90       100
                ....*....|....*....|....
gi 76556761 130 aKYRLRTVARTDGDAAVEGTATVL 153
Cdd:cd03448  99 -RVIFQTKVVERDVVVLSNGAALL 121
YdeM cd03454
YdeM is a Bacillus subtilis protein that belongs to a family of prokaryotic proteins of unkown ...
 32-154 6.31e-08

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: 48.72  E-value: 6.31e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76556761  32 SVGDTLRF-SKPVSEADVERFAlASGDTNPLHLDEASAAGTRFggrivhGGLIA-GIISAAL-------ARLPGTVVYLE 102
Cdd:cd03454   5 VIGQRFTSgSYTVTEEEIIAFA-REFDPQPFHLDEEAAKESLF------GGLAAsGWHTAAItmrllvdAGLSGSASGGS 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 76556761 103 ---QDLTFRSPVRIGETVTAELEVVD--------DLSEAKYRLRTVaRTDGDAAVEGTATVLI 154
Cdd:cd03454  78 pgiDELRWPRPVRPGDTLSVEVEVLDkrpsrsrpDRGIVTLRSETL-NQRGEVVLTFEATVLV 139
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 73-153 3.44e-07

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: 45.93  E-value: 3.44e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76556761  73 FGGRIVHGGLIAGIISAALARL-------PGTVVYLEQDLTFRSPVRIGETVTAELEVVdDLSEAKYRLRTVART-DGDA 144
Cdd:cd03440  13 DGGGIVHGGLLLALADEAAGAAaarlggrGLGAVTLSLDVRFLRPVRPGDTLTVEAEVV-RVGRSSVTVEVEVRNeDGKL 91


                ....*....
gi 76556761 145 AVEGTATVL 153
Cdd:cd03440  92 VATATATFV 100
MaoC_dehydrat_N pfam13452
N-terminal half of MaoC dehydratase; It is clear from the structures of bacterial members of ...
 42-125 2.96e-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: 2.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76556761    42 PVSEADVERFALASGDTNPLHLDEASAAGTRfggrivHGGLIA--------GIISAALARLPG----TVVYLEQDLTFRS 109
Cdd:pfam13452  13 EVERGAIREFARAIGETNPAYWDEAAARAAG------YGDLPApptflfvlGWDAPGFMEQLGidlsRLLHGEQRFTYHR 86

                          90
                  ....*....|....*.
gi 76556761   110 PVRIGETVTAELEVVD 125
Cdd:pfam13452  87 PLRAGDELTCRSQIAD 102
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 77-124 3.16e-04

Thioesterase superfamily; This family contains a wide variety of enzymes, principally thioesterases. This family includes 4HBT (EC 3.1.2.23) which catalyzes the final step in the biosynthesis of 4-hydroxybenzoate from 4-chlorobenzoate in the soil dwelling microbe Pseudomonas CBS-3. This family includes various cytosolic long-chain acyl-CoA thioester hydrolases. Long-chain acyl-CoA hydrolases hydrolyse palmitoyl-CoA to CoA and palmitate, they also catalyze the hydrolysis of other long chain fatty acyl-CoA thioesters.


Pssm-ID: 427116 [Multi-domain]  Cd Length: 79  Bit Score: 37.62  E-value: 3.16e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 76556761    77 IVHGGLI-------AGIISAALARLPGTVVYLEQDLTFRSPVRIGETVTAELEVV 124
Cdd:pfam03061   3 VVHGGVYlaladeaAGAAARRLGGSQQVVVVVELSIDFLRPARLGDRLTVEARVV 57
NodN cd03450
NodN (nodulation factor N) contains a single hot dog fold similar to those of the peroxisomal ...
 43-125 1.13e-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: 37.16  E-value: 1.13e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76556761  43 VSEADVERFALASGDTNPLHLDEASAAGTRFGGRIVHGGLIAGIISA---ALARLPG---TVVY-LEQdLTFRSPVRIGE 115
Cdd:cd03450  24 VDQERIDQFADATGDHQWIHVDPERAAAEPFGGTIAHGFLTLSLLPAltpQLFRVEGvkmGVNYgLDK-VRFPAPVPVGS 102

                        90
                ....*....|
gi 76556761 116 TVTAELEVVD 125
Cdd:cd03450 103 RVRGRFTLLS 112
FAS_MaoC cd03447
FAS_MaoC, the MaoC-like hot dog fold of the fatty acid synthase, beta subunit. Other enzymes ...
 46-122 1.52e-03

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: 36.49  E-value: 1.52e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76556761  46 ADVERFALASGDTNPLHLDEASAAGTRFGGRIVHGGLIAGIISA-----ALARLPGTVVYLEqdLTFRSPVRIGETVTAE 120
Cdd:cd03447  13 ASNEPYARVSGDFNPIHVSRVFASYAGLPGTITHGMYTSAAVRAlvetwAADNDRSRVRSFT--ASFVGMVLPNDELEVR 90


                ..
gi 76556761 121 LE 122
Cdd:cd03447  91 LE 92
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 84-153 7.96e-03

4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate degradation pathway in which 4-chlorobenzoate is converted to 4-hydroxybenzoate in certain soil-dwelling bacteria. 4HBT forms a homotetramer with four active sites. There is no evidence to suggest that 4HBT is related to the type I thioesterases functioning in primary or secondary metabolic pathways. Each subunit of the 4HBT tetramer adopts a so-called hot-dog fold similar to those of beta-hydroxydecanoyl-ACP dehydratase, (R)-specific enoyl-CoA hydratase, and type II, thioesterase (TEII).


Pssm-ID: 238329 [Multi-domain]  Cd Length: 110  Bit Score: 34.12  E-value: 7.96e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 76556761  84 AGIISAALARLPGTVVYLEQDLTFRSPVRIGETVTAELEVVdDLSEAKYRLR-TVARTDGDAAVEGTATVL 153
Cdd:cd00586  38 LGLGYDELEEQGLGLVVVELEIDYLRPLRLGDRLTVETRVL-RLGRKSFTFEqEIFREDGELLATAETVLV 107
 
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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