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Conserved domains on  [gi|983472071|ref|WP_060630045|]
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MULTISPECIES: MaoC family dehydratase [Bacillus cereus group]

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 ...
 18-144 3.06e-68

(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: 202.39  E-value: 3.06e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472071  18 IQVGDQASLTKQITDEDVINFAKLTGDVNPIHILDSFAKTTMFKERIAHGMLVSSFISTILGTKLPGKNTIYLSQNVSFR 97
Cdd:cd03449    1 LKVGDSASLTRTITEEDVELFAELSGDFNPIHLDEEYAKKTRFGGRIAHGMLTASLISAVLGTLLPGPGTIYLSQSLRFL 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 983472071  98 APVKIGDTLRVVAEVIKKRDDKKIITLQTNIYNQSDDIVVEGTATIL 144
Cdd:cd03449   81 RPVFIGDTVTATVTVTEKREDKKRVTLETVCTNQNGEVVIEGEAVVL 127
 
Name Accession Description Interval E-value
R_hydratase cd03449
(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA ...
 18-144 3.06e-68

(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: 202.39  E-value: 3.06e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472071  18 IQVGDQASLTKQITDEDVINFAKLTGDVNPIHILDSFAKTTMFKERIAHGMLVSSFISTILGTKLPGKNTIYLSQNVSFR 97
Cdd:cd03449    1 LKVGDSASLTRTITEEDVELFAELSGDFNPIHLDEEYAKKTRFGGRIAHGMLTASLISAVLGTLLPGPGTIYLSQSLRFL 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 983472071  98 APVKIGDTLRVVAEVIKKRDDKKIITLQTNIYNQSDDIVVEGTATIL 144
Cdd:cd03449   81 RPVFIGDTVTATVTVTEKREDKKRVTLETVCTNQNGEVVIEGEAVVL 127
PRK08190 PRK08190
bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated
 15-144 3.87e-52

bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated


Pssm-ID: 236180 [Multi-domain]  Cd Length: 466  Bit Score: 171.22  E-value: 3.87e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472071  15 YDEIQVGDQASLTKQITDEDVINFAKLTGDVNPIHILDSFAKTTMFKERIAHGMLVSSFISTILGTKLPGKNTIYLSQNV 94
Cdd:PRK08190  11 FDEIAIGDSASLVRTLTPDDIELFAAMSGDVNPAHLDAAYAASDGFHHVVAHGMWGGALISAVLGTRLPGPGTIYLGQSL 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 983472071  95 SFRAPVKIGDTLRVVAEVIKKRDDKKIITLQTNIYNQSDDIVVEGTATIL 144
Cdd:PRK08190  91 RFRRPVRIGDTLTVTVTVREKDPEKRIVVLDCRCTNQDGEVVITGTAEVI 140
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
15-144 2.82e-46

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 146.95  E-value: 2.82e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472071  15 YDEIQVGDQASL-TKQITDEDVINFAKLTGDVNPIHILDSFAKTTMFKERIAHGMLVSSFISTILGTKLPGKNTI-YLSQ 92
Cdd:COG2030    2 FEDLEVGDVLPHgGRTVTEEDIVLFAGATGDPNPIHLDEEAAAATGFGGRIAHGMLTLSLASGLLVDDLPGTAVAnLGLQ 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 983472071  93 NVSFRAPVKIGDTLRVVAEVIKKRDDKK--IITLQTNIYNQSDDIVVEGTATIL 144
Cdd:COG2030   82 EVRFLRPVRVGDTLRARVEVLEKRESKSrgIVTLRTTVTNQDGEVVLTGEATVL 135
MaoC_dehydratas pfam01575
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ...
 24-122 5.53e-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: 89.71  E-value: 5.53e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472071   24 ASLTKQITDEDVINFAKLTGDVNPIHILDSFAKTTMFKERIAHGMLVSSFISTILGTKLPGKNTI-YLSQNVSFRAPVKI 102
Cdd:pfam01575  12 TEKPRTVTEADIALFALVSGDHNPIHVDPEFAKKAGFGGPIAHGMLTLAIVAGLVEEWGGDNVIArFGEIKVRFTKPVFP 91

                          90       100
                  ....*....|....*....|
gi 983472071  103 GDTLRVVAEVIKKRDDKKII 122
Cdd:pfam01575  92 GDTLRTEAEVVGKRDGRQTK 111
 
Name Accession Description Interval E-value
R_hydratase cd03449
(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA ...
 18-144 3.06e-68

(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: 202.39  E-value: 3.06e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472071  18 IQVGDQASLTKQITDEDVINFAKLTGDVNPIHILDSFAKTTMFKERIAHGMLVSSFISTILGTKLPGKNTIYLSQNVSFR 97
Cdd:cd03449    1 LKVGDSASLTRTITEEDVELFAELSGDFNPIHLDEEYAKKTRFGGRIAHGMLTASLISAVLGTLLPGPGTIYLSQSLRFL 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 983472071  98 APVKIGDTLRVVAEVIKKRDDKKIITLQTNIYNQSDDIVVEGTATIL 144
Cdd:cd03449   81 RPVFIGDTVTATVTVTEKREDKKRVTLETVCTNQNGEVVIEGEAVVL 127
PRK08190 PRK08190
bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated
 15-144 3.87e-52

bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated


Pssm-ID: 236180 [Multi-domain]  Cd Length: 466  Bit Score: 171.22  E-value: 3.87e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472071  15 YDEIQVGDQASLTKQITDEDVINFAKLTGDVNPIHILDSFAKTTMFKERIAHGMLVSSFISTILGTKLPGKNTIYLSQNV 94
Cdd:PRK08190  11 FDEIAIGDSASLVRTLTPDDIELFAAMSGDVNPAHLDAAYAASDGFHHVVAHGMWGGALISAVLGTRLPGPGTIYLGQSL 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 983472071  95 SFRAPVKIGDTLRVVAEVIKKRDDKKIITLQTNIYNQSDDIVVEGTATIL 144
Cdd:PRK08190  91 RFRRPVRIGDTLTVTVTVREKDPEKRIVVLDCRCTNQDGEVVITGTAEVI 140
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
15-144 2.82e-46

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 146.95  E-value: 2.82e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472071  15 YDEIQVGDQASL-TKQITDEDVINFAKLTGDVNPIHILDSFAKTTMFKERIAHGMLVSSFISTILGTKLPGKNTI-YLSQ 92
Cdd:COG2030    2 FEDLEVGDVLPHgGRTVTEEDIVLFAGATGDPNPIHLDEEAAAATGFGGRIAHGMLTLSLASGLLVDDLPGTAVAnLGLQ 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 983472071  93 NVSFRAPVKIGDTLRVVAEVIKKRDDKK--IITLQTNIYNQSDDIVVEGTATIL 144
Cdd:COG2030   82 EVRFLRPVRVGDTLRARVEVLEKRESKSrgIVTLRTTVTNQDGEVVLTGEATVL 135
R_hydratase_like cd03441
(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl ...
 21-144 1.15e-43

(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: 140.09  E-value: 1.15e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472071  21 GDQASLTKQITDEDVINFAKLTGDVNPIHILDSFAKTTMFKERIAHGMLVSSFISTILGTKLPGKN-TIYLSQNVSFRAP 99
Cdd:cd03441    1 GELDSSGRTVTEADIALFARLSGDPNPIHVDPEYAKAAGFGGRIAHGMLTLSLASGLLVQWLPGTDgANLGSQSVRFLAP 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 983472071 100 VKIGDTLRVVAEVIKKRDDKK--IITLQTNIYNQSDDIVVEGTATIL 144
Cdd:cd03441   81 VFPGDTLRVEVEVLGKRPSKGrgVVTVRTEARNQGGEVVLSGEATVL 127
MaoC_like cd03446
MoaC_like Similar to the MaoC (monoamine oxidase C) dehydratase regulatory protein but ...
 15-144 2.01e-30

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: 106.62  E-value: 2.01e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472071  15 YDEIQVGDQ-ASLTKQITDEDVINFAKLTGDVNPIHILDSFAKTTMFKERIAHGMLVSSfISTILGTKLPGKNT----IY 89
Cdd:cd03446    2 FEDFEIGQVfESVGRTVTEADVVMFAGLSGDWNPIHTDAEYAKKTRFGERIAHGLLTLS-IATGLLQRLGVFERtvvaFY 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 983472071  90 LSQNVSFRAPVKIGDTLRVVAEVIKKRD----DKKIITLQTNIYNQSDDIVVEGTATIL 144
Cdd:cd03446   81 GIDNLRFLNPVFIGDTIRAEAEVVEKEEkdgeDAGVVTRRIEVVNQRGEVVQSGEMSLL 139
MaoC_dehydratas pfam01575
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ...
 24-122 5.53e-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: 89.71  E-value: 5.53e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472071   24 ASLTKQITDEDVINFAKLTGDVNPIHILDSFAKTTMFKERIAHGMLVSSFISTILGTKLPGKNTI-YLSQNVSFRAPVKI 102
Cdd:pfam01575  12 TEKPRTVTEADIALFALVSGDHNPIHVDPEFAKKAGFGGPIAHGMLTLAIVAGLVEEWGGDNVIArFGEIKVRFTKPVFP 91

                          90       100
                  ....*....|....*....|
gi 983472071  103 GDTLRVVAEVIKKRDDKKII 122
Cdd:pfam01575  92 GDTLRTEAEVVGKRDGRQTK 111
FkbR2 cd03451
FkbR2 is a Streptomyces hygroscopicus protein with a hot dog fold that belongs to a conserved ...
 13-144 7.22e-21

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: 82.25  E-value: 7.22e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472071  13 LRYDEIQVGD--QASLTKQITDEDVINFAKLTGDVNPIHILDSFAKTTMFKERIAHGMLVssfISTILGTKLPGkntiyL 90
Cdd:cd03451    2 LYFEDFTVGQvfEHAPGRTVTEADNVLFTLLTMNTAPLHFDAAYAAKTEFGRRLVNSLFT---LSLALGLSVND-----T 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 983472071  91 SQN---------VSFRAPVKIGDTLRVVAEVIKKRDDKK-----IITLQTNIYNQSDDIVVEGTATIL 144
Cdd:cd03451   74 SLTavanlgydeVRFPAPVFHGDTLYAESEVLSKRESKSrpdagIVTVRTVGYNQDGEPVLSFERTAL 141
MaoC_C cd03452
MaoC_C The C-terminal hot dog fold of the MaoC (monoamine oxidase C) dehydratase regulatory ...
 15-144 3.81e-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: 75.51  E-value: 3.81e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472071  15 YDEIQVGDQ-ASLTKQITDEDVINFAKLTGDVNPIHILDSFAKTTMFKERIAHGMLVSSFISTILGTKLPG---KNtiYL 90
Cdd:cd03452    2 LEQLRPGDSlLTHRRTVTEADIVNFACLTGDHFYAHMDEIAAKASFFGKRVAHGYFVLSAAAGLFVDPAPGpvlAN--YG 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 983472071  91 SQNVSFRAPVKIGDTLRV---VAEVI-KKRDDKKIITLQTNIYNQSDDIVveGTATIL 144
Cdd:cd03452   80 LENLRFLEPVYPGDTIQVrltCKRKIpRDGQDYGVVRWDAEVTNQNGELV--ASYDIL 135
SAV4209_like cd03453
SAV4209_like. Similar in sequence to the Streptomyces avermitilis SAV4209 protein, with a hot ...
 20-143 9.79e-17

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: 71.20  E-value: 9.79e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472071  20 VGDQ-ASLTKQITDEDVINFAKLTGDVNPIHILDSFAKTTMFKERIAHGMLVSSFISTILGTKLPGKNTIyLSQNVSFRA 98
Cdd:cd03453    1 VGDElPPLTPPVSRADLVRYAGASGDFNPIHYDEDFAKKVGLPGVIAHGMLTMGLLGRLVTDWVGDPGRV-VSFGVRFTK 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 983472071  99 PVKIGDTLRVVAEV--IKKRDDKKIITLQTNIYNQSDDIVVEGTATI 143
Cdd:cd03453   80 PVPVPDTLTCTGIVveKTVADGEDALTVTVDATDQAGGKKVLGRAIV 126
YdeM cd03454
YdeM is a Bacillus subtilis protein that belongs to a family of prokaryotic proteins of unkown ...
 15-144 1.46e-14

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: 66.05  E-value: 1.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472071  15 YDEIQVGDQASL-TKQITDEDVINFAKlTGDVNPIHILDSFAKTTMFKERIAHG---------MLVSSFI--STILGTkl 82
Cdd:cd03454    1 FEDLVIGQRFTSgSYTVTEEEIIAFAR-EFDPQPFHLDEEAAKESLFGGLAASGwhtaaitmrLLVDAGLsgSASGGS-- 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 983472071  83 PGKNtiylsqNVSFRAPVKIGDTLRVVAEVIKK-----RDDKKIITLQTNIYNQSDDIVVEGTATIL 144
Cdd:cd03454   78 PGID------ELRWPRPVRPGDTLSVEVEVLDKrpsrsRPDRGIVTLRSETLNQRGEVVLTFEATVL 138
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 63-144 2.85e-13

The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase) structure and subsequently in 4HBT (4-hydroxybenzoyl-CoA thioesterase) from Pseudomonas. A number of other seemingly unrelated proteins also share the hotdog fold. These proteins have related, but distinct, catalytic activities that include metabolic roles such as thioester hydrolysis in fatty acid metabolism, and degradation of phenylacetic acid and the environmental pollutant 4-chlorobenzoate. This superfamily also includes the PaaI-like protein FapR, a non-catalytic bacterial homolog involved in transcriptional regulation of fatty acid biosynthesis.


Pssm-ID: 239524 [Multi-domain]  Cd Length: 100  Bit Score: 61.72  E-value: 2.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472071  63 RIAHGMLVSSFISTILGT-----KLPGKNTIYLSQNVSFRAPVKIGDTLRVVAEVIKKRddKKIITLQTNIYNQSDDIVV 137
Cdd:cd03440   16 GIVHGGLLLALADEAAGAaaarlGGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVG--RSSVTVEVEVRNEDGKLVA 93


                 ....*..
gi 983472071 138 EGTATIL 144
Cdd:cd03440   94 TATATFV 100
PRK13693 PRK13693
(3R)-hydroxyacyl-ACP dehydratase subunit HadB; Provisional
 14-102 2.13e-11

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


Pssm-ID: 184249 [Multi-domain]  Cd Length: 142  Bit Score: 57.92  E-value: 2.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472071  14 RYDEIQVGDQ-ASLTKQITDEDVINFAKLTGDVNPIHILDSFAKTTMFKERIAHGMLV----SSFISTILGTklPGKNTI 88
Cdd:PRK13693   5 EFSSVKVGDQlPEKTYPLTRQDLVNYAGVSGDLNPIHWDDEIAKVVGLDTAIAHGMLTmglgGGYVTSWVGD--PGAVTE 82

                         90
                 ....*....|....
gi 983472071  89 YlsqNVSFRAPVKI 102
Cdd:PRK13693  83 Y---NVRFTAVVPV 93
SAV4209 cd03455
SAV4209 is a Streptomyces avermitilis protein with a hot dog fold that is similar to those of ...
 25-143 1.49e-10

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: 55.02  E-value: 1.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472071  25 SLTKQITDEDVINFAKLTGDVNPIHILDSFAKTTMFKERIAHGMLVSSFISTILGTKLPGKNTIylsQNVSFR--APVKI 102
Cdd:cd03455    6 RLSIPPDPTLLFRYSAATRDFHRIHHDRDYARAVGYPDLYVNGPTLAGLVIRYVTDWAGPDARV---KSFAFRlgAPLYA 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 983472071 103 GDTLRVVAEVIKKRDDkKIITLQTNIYNQSDDIVVEGTATI 143
Cdd:cd03455   83 GDTLRFGGRVTAKRDD-EVVTVELWARNSEGDHVMAGTATV 122
FAS_MaoC cd03447
FAS_MaoC, the MaoC-like hot dog fold of the fatty acid synthase, beta subunit. Other enzymes ...
 38-143 1.18e-09

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: 52.67  E-value: 1.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472071  38 FAKLTGDVNPIHILDSFAKTTMFKERIAHGMLVSSFISTILGTkLPGKNTIY--LSQNVSFRAPVKIGDTLRVVAEVIKK 115
Cdd:cd03447   18 YARVSGDFNPIHVSRVFASYAGLPGTITHGMYTSAAVRALVET-WAADNDRSrvRSFTASFVGMVLPNDELEVRLEHVGM 96

                         90       100
                 ....*....|....*....|....*...
gi 983472071 116 RDDKKIITLQTNIyNQSDDIVVEGTATI 143
Cdd:cd03447   97 VDGRKVIKVEARN-EETGELVLRGEAEV 123
NodN cd03450
NodN (nodulation factor N) contains a single hot dog fold similar to those of the peroxisomal ...
 32-114 1.87e-07

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: 47.56  E-value: 1.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472071  32 DEDVIN-FAKLTGDVNPIHILDSFAKTTMFKERIAHGMLVSSFISTiLGTKLPGKNTIYLSQN-----VSFRAPVKIGDT 105
Cdd:cd03450   25 DQERIDqFADATGDHQWIHVDPERAAAEPFGGTIAHGFLTLSLLPA-LTPQLFRVEGVKMGVNygldkVRFPAPVPVGSR 103


                 ....*....
gi 983472071 106 LRVVAEVIK 114
Cdd:cd03450  104 VRGRFTLLS 112
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 93-142 2.41e-07

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 46.86  E-value: 2.41e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 983472071  93 NVSFRAPVKIGDTLRVVAEVIKKRddKKIITLQTNIYNQSDDIVVEGTAT 142
Cdd:COG2050   83 NINFLRPARLGDRLTAEARVVRRG--RRLAVVEVEVTDEDGKLVATATGT 130
MaoC_dehydrat_N pfam13452
N-terminal half of MaoC dehydratase; It is clear from the structures of bacterial members of ...
 30-138 5.72e-07

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: 45.76  E-value: 5.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472071   30 ITDEDVINFAKLTGDVNPIHILDSFAKTTMFKERIAHGMLVSSFISTILGT----KLPGKNTIYLSQNVSFRAPVKIGDT 105
Cdd:pfam13452  14 VERGAIREFARAIGETNPAYWDEAAARAAGYGDLPAPPTFLFVLGWDAPGFmeqlGIDLSRLLHGEQRFTYHRPLRAGDE 93

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 983472071  106 LRVVAEVIKKRDDK-----KIITLQTNIYNQSDDIVVE 138
Cdd:pfam13452  94 LTCRSQIADVYDKKgngalCFVVVETEVTNQRGEPVAT 131
HDE_HSD cd03448
HDE_HSD The R-hydratase-like hot dog fold of the 17-beta-hydroxysteriod dehydrogenase (HSD), ...
 41-145 6.05e-07

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


Pssm-ID: 239532 [Multi-domain]  Cd Length: 122  Bit Score: 45.67  E-value: 6.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472071  41 LTGDVNPIHILDSFAKTTMFKERIAHGMLVSSFIS-TILGTKLPGKNTIYLSQNVSFRAPVKIGDTLRVvaEVIKkrdDK 119
Cdd:cd03448   23 LSGDYNPLHIDPAFAKAAGFPRPILHGLCTYGFAArAVLEAFADGDPARFKAIKVRFSSPVFPGETLRT--EMWK---EG 97

                         90       100
                 ....*....|....*....|....*.
gi 983472071 120 KIITLQTnIYNQSDDIVVEGTATILK 145
Cdd:cd03448   98 NRVIFQT-KVVERDVVVLSNGAALLA 122
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 64-144 3.61e-05

PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several proteins responsible for phenylacetic acid (PA) degradation in bacteria. Although orthologs of PaaI exist in archaea and eukaryotes, their function has not been determined. Sequence similarity between PaaI, E. coli medium chain acyl-CoA thioesterase II, and human thioesterase III suggests they all belong to the same thioesterase superfamily. The conserved fold present in these thioesterases is referred to as an asymmetric hot dog fold, similar to those of 4-hydroxybenzoyl-CoA thioesterase (4HBT) and the beta-hydroxydecanoyl-ACP dehydratases (FabA/FabZ).


Pssm-ID: 239527 [Multi-domain]  Cd Length: 113  Bit Score: 40.62  E-value: 3.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983472071  64 IAHGMLVSSFISTILG----TKLPGKNTIY-LSQNVSFRAPVKIGDtLRVVAEVIKKRddKKIITLQTNIYNQSDDIVVE 138
Cdd:cd03443   30 IVHGGAIATLADTAGGlaalSALPPGALAVtVDLNVNYLRPARGGD-LTARARVVKLG--RRLAVVEVEVTDEDGKLVAT 106


                 ....*.
gi 983472071 139 GTATIL 144
Cdd:cd03443  107 ARGTFA 112
PRK04424 PRK04424
transcription factor FapR;
93-140 1.88e-04

transcription factor FapR;


Pssm-ID: 179847 [Multi-domain]  Cd Length: 185  Bit Score: 39.42  E-value: 1.88e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 983472071  93 NVSFRAPVKIGDTLRVVAEVIKKRDDKKIITLQTNIynqSDDIVVEGT 140
Cdd:PRK04424 132 NIRFKRPVKLGERVVAKAEVVRKKGNKYIVEVKSYV---GDELVFRGK 176
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 91-144 9.01e-04

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: 36.82  E-value: 9.01e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 983472071  91 SQNVSFRAPVKIGDTLRVVAEVIKKrdDKKIITLQTNIYNQSDDIVVEGTATIL 144
Cdd:cd00586   56 ELEIDYLRPLRLGDRLTVETRVLRL--GRKSFTFEQEIFREDGELLATAETVLV 107
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 90-137 1.74e-03

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: 35.31  E-value: 1.74e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 983472071   90 LSQNVSFRAPVKIGDTLRVVAEVIKKRddKKIITLQTNIYNQSDDIVV 137
Cdd:pfam03061  34 VELSIDFLRPARLGDRLTVEARVVRLG--RTSAVVEVEVRDEDGRLVA 79
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 91-143 5.27e-03

Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440586 [Multi-domain]  Cd Length: 139  Bit Score: 34.87  E-value: 5.27e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 983472071  91 SQNVSFRAPVKIGDTLRVVAEVIKKrdDKKIITLQTNIYNQSDD-IVVEGTATI 143
Cdd:COG0824   61 EAEIDYLRPARYGDELTVETRVVRL--GGSSLTFEYEIFRADDGeLLATGETVL 112
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
93-114 5.54e-03

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 35.16  E-value: 5.54e-03
                         10        20
                 ....*....|....*....|..
gi 983472071  93 NVSFRAPVKIGDTLRVVAEVIK 114
Cdd:COG1607   56 SVDFLRPVRVGDIVELYARVVR 77
 
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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