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Conserved domains on  [gi|593429522|gb|EXQ19198|]
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acyl dehydratase MaoC [Staphylococcus aureus H68996]

Protein Classification

MaoC family dehydratase( domain architecture ID 10130993)

MaoC family dehydratase similar to MaoC-like dehydratase from Rhodospirillum rubrum and Bacillus subtilis YdeM

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YdeM cd03454
YdeM is a Bacillus subtilis protein that belongs to a family of prokaryotic proteins of unkown ...
 3-139 1.07e-65

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: 195.86  E-value: 1.07e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429522   3 YDDFIVGETFKTKSLHITEEEIIQFATTFDPQYMHIDKEKAEQSRFKGIIASGMHTLSISFKLWVEEGKYGEEVVAGTQM 82
Cdd:cd03454    1 FEDLVIGQRFTSGSYTVTEEEIIAFAREFDPQPFHLDEEAAKESLFGGLAASGWHTAAITMRLLVDAGLSGSASGGSPGI 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 593429522  83 NNVKFIKPVYPGNTLYVIAEITNKK--SIKKENGLVTVSLSTYNENEEIVFKGEVTALI 139
Cdd:cd03454   81 DELRWPRPVRPGDTLSVEVEVLDKRpsRSRPDRGIVTLRSETLNQRGEVVLTFEATVLV 139
 
Name Accession Description Interval E-value
YdeM cd03454
YdeM is a Bacillus subtilis protein that belongs to a family of prokaryotic proteins of unkown ...
 3-139 1.07e-65

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: 195.86  E-value: 1.07e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429522   3 YDDFIVGETFKTKSLHITEEEIIQFATTFDPQYMHIDKEKAEQSRFKGIIASGMHTLSISFKLWVEEGKYGEEVVAGTQM 82
Cdd:cd03454    1 FEDLVIGQRFTSGSYTVTEEEIIAFAREFDPQPFHLDEEAAKESLFGGLAASGWHTAAITMRLLVDAGLSGSASGGSPGI 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 593429522  83 NNVKFIKPVYPGNTLYVIAEITNKK--SIKKENGLVTVSLSTYNENEEIVFKGEVTALI 139
Cdd:cd03454   81 DELRWPRPVRPGDTLSVEVEVLDKRpsRSRPDRGIVTLRSETLNQRGEVVLTFEATVLV 139
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
3-139 1.74e-42

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 137.32  E-value: 1.74e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429522   3 YDDFIVGETFKTKSLHITEEEIIQFAT-TFDPQYMHIDKEKAEQSRFKGIIASGMHTLSISFKLWVEEgkYGEEVVAGTQ 81
Cdd:COG2030    2 FEDLEVGDVLPHGGRTVTEEDIVLFAGaTGDPNPIHLDEEAAAATGFGGRIAHGMLTLSLASGLLVDD--LPGTAVANLG 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 593429522  82 MNNVKFIKPVYPGNTLYVIAEITNKKSiKKENGLVTVSLSTYNENEEIVFKGEVTALI 139
Cdd:COG2030   80 LQEVRFLRPVRVGDTLRARVEVLEKRE-SKSRGIVTLRTTVTNQDGEVVLTGEATVLV 136
MaoC_dehydratas pfam01575
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ...
 8-124 7.90e-37

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: 122.45  E-value: 7.90e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429522    8 VGETFKT-KSLHITEEEIIQFAT-TFDPQYMHIDKEKAEQSRFKGIIASGMHTLSISFKLWVEEGkyGEEVVAGTQMNNV 85
Cdd:pfam01575   6 PGEPPDTeKPRTVTEADIALFALvSGDHNPIHVDPEFAKKAGFGGPIAHGMLTLAIVAGLVEEWG--GDNVIARFGEIKV 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 593429522   86 KFIKPVYPGNTLYVIAEITNKKSIKKE-NGLVTVSLSTYN 124
Cdd:pfam01575  84 RFTKPVFPGDTLRTEAEVVGKRDGRQTkVVEVTVEVTEVA 123
PRK08190 PRK08190
bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated
 3-136 2.15e-06

bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated


Pssm-ID: 236180 [Multi-domain]  Cd Length: 466  Bit Score: 45.64  E-value: 2.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429522   3 YDDFIVGETFKTKSLhITEEEIIQFATTF-DPQYMHIDKEKAEQSRFKGIIASGMHTLS-ISfklwveegkygeeVVAGT 80
Cdd:PRK08190  11 FDEIAIGDSASLVRT-LTPDDIELFAAMSgDVNPAHLDAAYAASDGFHHVVAHGMWGGAlIS-------------AVLGT 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 593429522  81 QM---------NNVKFIKPVYPGNTLYVIAEITNKKSikkENGLVTVSLSTYNENEEIVFKGEVT 136
Cdd:PRK08190  77 RLpgpgtiylgQSLRFRRPVRIGDTLTVTVTVREKDP---EKRIVVLDCRCTNQDGEVVITGTAE 138
 
Name Accession Description Interval E-value
YdeM cd03454
YdeM is a Bacillus subtilis protein that belongs to a family of prokaryotic proteins of unkown ...
 3-139 1.07e-65

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: 195.86  E-value: 1.07e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429522   3 YDDFIVGETFKTKSLHITEEEIIQFATTFDPQYMHIDKEKAEQSRFKGIIASGMHTLSISFKLWVEEGKYGEEVVAGTQM 82
Cdd:cd03454    1 FEDLVIGQRFTSGSYTVTEEEIIAFAREFDPQPFHLDEEAAKESLFGGLAASGWHTAAITMRLLVDAGLSGSASGGSPGI 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 593429522  83 NNVKFIKPVYPGNTLYVIAEITNKK--SIKKENGLVTVSLSTYNENEEIVFKGEVTALI 139
Cdd:cd03454   81 DELRWPRPVRPGDTLSVEVEVLDKRpsRSRPDRGIVTLRSETLNQRGEVVLTFEATVLV 139
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
3-139 1.74e-42

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 137.32  E-value: 1.74e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429522   3 YDDFIVGETFKTKSLHITEEEIIQFAT-TFDPQYMHIDKEKAEQSRFKGIIASGMHTLSISFKLWVEEgkYGEEVVAGTQ 81
Cdd:COG2030    2 FEDLEVGDVLPHGGRTVTEEDIVLFAGaTGDPNPIHLDEEAAAATGFGGRIAHGMLTLSLASGLLVDD--LPGTAVANLG 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 593429522  82 MNNVKFIKPVYPGNTLYVIAEITNKKSiKKENGLVTVSLSTYNENEEIVFKGEVTALI 139
Cdd:COG2030   80 LQEVRFLRPVRVGDTLRARVEVLEKRE-SKSRGIVTLRTTVTNQDGEVVLTGEATVLV 136
MaoC_dehydratas pfam01575
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ...
 8-124 7.90e-37

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: 122.45  E-value: 7.90e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429522    8 VGETFKT-KSLHITEEEIIQFAT-TFDPQYMHIDKEKAEQSRFKGIIASGMHTLSISFKLWVEEGkyGEEVVAGTQMNNV 85
Cdd:pfam01575   6 PGEPPDTeKPRTVTEADIALFALvSGDHNPIHVDPEFAKKAGFGGPIAHGMLTLAIVAGLVEEWG--GDNVIARFGEIKV 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 593429522   86 KFIKPVYPGNTLYVIAEITNKKSIKKE-NGLVTVSLSTYN 124
Cdd:pfam01575  84 RFTKPVFPGDTLRTEAEVVGKRDGRQTkVVEVTVEVTEVA 123
R_hydratase_like cd03441
(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl ...
 10-138 3.01e-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: 118.52  E-value: 3.01e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429522  10 ETFKTKSLHITEEEIIQFAT-TFDPQYMHIDKEKAEQSRFKGIIASGMHTLSISFKLWVEEgkYGEEVVAGTQMNNVKFI 88
Cdd:cd03441    1 GELDSSGRTVTEADIALFARlSGDPNPIHVDPEYAKAAGFGGRIAHGMLTLSLASGLLVQW--LPGTDGANLGSQSVRFL 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 593429522  89 KPVYPGNTLYVIAEITNKKsIKKENGLVTVSLSTYNENEEIVFKGEVTAL 138
Cdd:cd03441   79 APVFPGDTLRVEVEVLGKR-PSKGRGVVTVRTEARNQGGEVVLSGEATVL 127
MaoC_like cd03446
MoaC_like Similar to the MaoC (monoamine oxidase C) dehydratase regulatory protein but ...
 3-139 1.04e-26

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: 96.99  E-value: 1.04e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429522   3 YDDFIVGETFKTKSLHITEEEIIQFAT-TFDPQYMHIDKEKAEQSRFKGIIASGMHTLSISFKLWVEEGKYGEEVVAGTQ 81
Cdd:cd03446    2 FEDFEIGQVFESVGRTVTEADVVMFAGlSGDWNPIHTDAEYAKKTRFGERIAHGLLTLSIATGLLQRLGVFERTVVAFYG 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 593429522  82 MNNVKFIKPVYPGNTLYVIAEITNKKSI-KKENGLVTVSLSTYNENEEIVFKGEVTALI 139
Cdd:cd03446   82 IDNLRFLNPVFIGDTIRAEAEVVEKEEKdGEDAGVVTRRIEVVNQRGEVVQSGEMSLLV 140
FkbR2 cd03451
FkbR2 is a Streptomyces hygroscopicus protein with a hot dog fold that belongs to a conserved ...
 3-139 4.08e-23

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: 88.03  E-value: 4.08e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429522   3 YDDFIVGETFKtkslH-----ITEEEIIQFAT-TFDPQYMHIDKEKAEQSRFKGIIASGMHTLSISFKLWVEEgkYGEEV 76
Cdd:cd03451    4 FEDFTVGQVFE----HapgrtVTEADNVLFTLlTMNTAPLHFDAAYAAKTEFGRRLVNSLFTLSLALGLSVND--TSLTA 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 593429522  77 VAGTQMNNVKFIKPVYPGNTLYVIAEITNKKSIKKEN--GLVTVSLSTYNENEEIVFKGEVTALI 139
Cdd:cd03451   78 VANLGYDEVRFPAPVFHGDTLYAESEVLSKRESKSRPdaGIVTVRTVGYNQDGEPVLSFERTALV 142
MaoC_C cd03452
MaoC_C The C-terminal hot dog fold of the MaoC (monoamine oxidase C) dehydratase regulatory ...
 3-130 1.21e-18

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: 76.28  E-value: 1.21e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429522   3 YDDFIVGETFKTKSLHITEEEIIQFAT-TFDPQYMHIDKEKAEQSRFKGIIASGMHTLSISFKLWVEEGKygEEVVAGTQ 81
Cdd:cd03452    2 LEQLRPGDSLLTHRRTVTEADIVNFAClTGDHFYAHMDEIAAKASFFGKRVAHGYFVLSAAAGLFVDPAP--GPVLANYG 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 593429522  82 MNNVKFIKPVYPGNTLYViaEITNKKSIKKEN---GLVTVSLSTYNENEEIV 130
Cdd:cd03452   80 LENLRFLEPVYPGDTIQV--RLTCKRKIPRDGqdyGVVRWDAEVTNQNGELV 129
R_hydratase cd03449
(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA ...
 8-139 3.23e-17

(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: 72.19  E-value: 3.23e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429522   8 VGETFkTKSLHITEEEIIQFAT-TFDPQYMHIDKEKAEQSRFKGIIASGMHTLS-ISFKLwveeGKY--GEEVVAGTQmn 83
Cdd:cd03449    3 VGDSA-SLTRTITEEDVELFAElSGDFNPIHLDEEYAKKTRFGGRIAHGMLTASlISAVL----GTLlpGPGTIYLSQ-- 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 593429522  84 NVKFIKPVYPGNTLYVIAEITNKksiKKENGLVTVSLSTYNENEEIVFKGEVTALI 139
Cdd:cd03449   76 SLRFLRPVFIGDTVTATVTVTEK---REDKKRVTLETVCTNQNGEVVIEGEAVVLA 128
NodN cd03450
NodN (nodulation factor N) contains a single hot dog fold similar to those of the peroxisomal ...
 8-107 1.41e-09

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: 52.95  E-value: 1.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429522   8 VG-ETFKTKSLHITEEEIIQFA-TTFDPQYMHIDKEKAEQSRFKGIIASGMHTLSISFKLWVEEGkygeeVVAGTQM--- 82
Cdd:cd03450   12 VGqELGVSDWVTVDQERIDQFAdATGDHQWIHVDPERAAAEPFGGTIAHGFLTLSLLPALTPQLF-----RVEGVKMgvn 86

                         90       100       110
                 ....*....|....*....|....*....|.
gi 593429522  83 ---NNVKFIKPVYPGNTLY---VIAEITNKK 107
Cdd:cd03450   87 yglDKVRFPAPVPVGSRVRgrfTLLSVEELK 117
SAV4209_like cd03453
SAV4209_like. Similar in sequence to the Streptomyces avermitilis SAV4209 protein, with a hot ...
 8-135 5.64e-07

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: 45.39  E-value: 5.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429522   8 VGETFKTKSLHITEEEIIQFATT---FDPqyMHIDKEKAEQSRFKGIIASGMHTLSISFKL---WVEEG----KYGeevv 77
Cdd:cd03453    1 VGDELPPLTPPVSRADLVRYAGAsgdFNP--IHYDEDFAKKVGLPGVIAHGMLTMGLLGRLvtdWVGDPgrvvSFG---- 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 593429522  78 agtqmnnVKFIKPVYPGNTLYVIAEITNKKSIKKENgLVTVSLSTYNENEEIVFKGEV 135
Cdd:cd03453   75 -------VRFTKPVPVPDTLTCTGIVVEKTVADGED-ALTVTVDATDQAGGKKVLGRA 124
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 52-138 1.82e-06

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: 43.62  E-value: 1.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429522  52 IASGMHTLSISFKLWVE--EGKYGEEVVAGTQMNNVKFIKPVYPGNTLYVIAEItnkksIKKENGLVTVSLSTYNENEEI 129
Cdd:cd03440   17 IVHGGLLLALADEAAGAaaARLGGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEV-----VRVGRSSVTVEVEVRNEDGKL 91


                 ....*....
gi 593429522 130 VFKGEVTAL 138
Cdd:cd03440   92 VATATATFV 100
PRK08190 PRK08190
bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated
 3-136 2.15e-06

bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated


Pssm-ID: 236180 [Multi-domain]  Cd Length: 466  Bit Score: 45.64  E-value: 2.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429522   3 YDDFIVGETFKTKSLhITEEEIIQFATTF-DPQYMHIDKEKAEQSRFKGIIASGMHTLS-ISfklwveegkygeeVVAGT 80
Cdd:PRK08190  11 FDEIAIGDSASLVRT-LTPDDIELFAAMSgDVNPAHLDAAYAASDGFHHVVAHGMWGGAlIS-------------AVLGT 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 593429522  81 QM---------NNVKFIKPVYPGNTLYVIAEITNKKSikkENGLVTVSLSTYNENEEIVFKGEVT 136
Cdd:PRK08190  77 RLpgpgtiylgQSLRFRRPVRIGDTLTVTVTVREKDP---EKRIVVLDCRCTNQDGEVVITGTAE 138
HDE_HSD cd03448
HDE_HSD The R-hydratase-like hot dog fold of the 17-beta-hydroxysteriod dehydrogenase (HSD), ...
 36-97 8.63e-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: 42.21  E-value: 8.63e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 593429522  36 MHIDKEKAEQSRFKGIIASGMHTLSISFKLWVEEgkYGEEVVAGTQMNNVKFIKPVYPGNTL 97
Cdd:cd03448   30 LHIDPAFAKAAGFPRPILHGLCTYGFAARAVLEA--FADGDPARFKAIKVRFSSPVFPGETL 89
FabA COG0764
3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and ...
 65-137 5.92e-04

3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and metabolism]; 3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440527  Cd Length: 141  Bit Score: 37.48  E-value: 5.92e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 593429522  65 LWVEEGKYGEEVVAGTQMNNVKFIKPVYPGNTLYVIAEITNKKS-IKKENGLVTVslstyneNEEIVFKGEVTA 137
Cdd:COG0764   70 LKSEGLEGKGRLVYFLGIDKVKFRGPVVPGDTLTLEVEIKRVRRgIGKADGKATV-------DGKLVAEAELTF 136
SAV4209 cd03455
SAV4209 is a Streptomyces avermitilis protein with a hot dog fold that is similar to those of ...
 9-136 6.98e-04

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: 37.30  E-value: 6.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429522   9 GETFKTKSLHITEEEIIQFAT-TFDPQYMHIDKEKAEQSRFKGIIASGMHTLSisfkLWVEegkygeevVAGTQMNNVKF 87
Cdd:cd03455    1 GDELPRLSIPPDPTLLFRYSAaTRDFHRIHHDRDYARAVGYPDLYVNGPTLAG----LVIR--------YVTDWAGPDAR 68

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 593429522  88 IK--------PVYPGNTLYVIAEITNkksiKKENGLVTVSLSTYNENEEIVFKGEVT 136
Cdd:cd03455   69 VKsfafrlgaPLYAGDTLRFGGRVTA----KRDDEVVTVELWARNSEGDHVMAGTAT 121
MaoC_dehydrat_N pfam13452
N-terminal half of MaoC dehydratase; It is clear from the structures of bacterial members of ...
 8-131 1.03e-03

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: 36.90  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429522    8 VGETFKTKSLHITEEEIIQFA-TTFDPQYMHIDKEKAEQSRFKGIIASGMHTLSISFK--LWVEEGKYG-EEVVAGTQmn 83
Cdd:pfam13452   3 IGVEFGPVKYEVERGAIREFArAIGETNPAYWDEAAARAAGYGDLPAPPTFLFVLGWDapGFMEQLGIDlSRLLHGEQ-- 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 593429522   84 NVKFIKPVYPGNTLYVIAEITNKKsIKKENG---LVTVSLSTYNENEEIVF 131
Cdd:pfam13452  81 RFTYHRPLRAGDELTCRSQIADVY-DKKGNGalcFVVVETEVTNQRGEPVA 130
PRK04424 PRK04424
transcription factor FapR;
77-134 1.30e-03

transcription factor FapR;


Pssm-ID: 179847 [Multi-domain]  Cd Length: 185  Bit Score: 37.11  E-value: 1.30e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 593429522  77 VAGTQMNNVKFIKPVYPGNTLYVIAEITNKKsikkeNGLVTVSLSTYnENEEIVFKGE 134
Cdd:PRK04424 125 LALTGVANIRFKRPVKLGERVVAKAEVVRKK-----GNKYIVEVKSY-VGDELVFRGK 176
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 73-139 8.05e-03

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 34.53  E-value: 8.05e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 593429522  73 GEEVVAGTQMNNVKFIKPVYPGNTLYVIAEItnkksIKKENGLVTVSLSTYNENEEIVFKGEVTALI 139
Cdd:COG2050   72 PPGRRAVTIELNINFLRPARLGDRLTAEARV-----VRRGRRLAVVEVEVTDEDGKLVATATGTFAV 133
 
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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