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Conserved domains on  [gi|445956505|ref|WP_000034360|]
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MULTISPECIES: MaoC family dehydratase [Leptospira]

Protein Classification

MaoC family dehydratase( domain architecture ID 10130992)

MaoC family dehydratase containing a hotdog fold

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SAV4209_like cd03453
SAV4209_like. Similar in sequence to the Streptomyces avermitilis SAV4209 protein, with a hot ...
 11-137 2.57e-62

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: 186.76  E-value: 2.57e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445956505  11 VGQELPPLkTEVITHANLVRYAGASGDFNPIHNDPDFARKTGLDGTIAHGMYVMAQLGRLCTSWA-DQKQIKEFGVTFKN 89
Cdd:cd03453    1 VGDELPPL-TPPVSRADLVRYAGASGDFNPIHYDEDFAKKVGLPGVIAHGMLTMGLLGRLVTDWVgDPGRVVSFGVRFTK 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 445956505  90 MTKPGQKLTCTGKVKRKKEENGEKLITVAVEATDDSGEVKCSGEMVVV 137
Cdd:cd03453   80 PVPVPDTLTCTGIVVEKTVADGEDALTVTVDATDQAGGKKVLGRAIVA 127
 
Name Accession Description Interval E-value
SAV4209_like cd03453
SAV4209_like. Similar in sequence to the Streptomyces avermitilis SAV4209 protein, with a hot ...
 11-137 2.57e-62

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: 186.76  E-value: 2.57e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445956505  11 VGQELPPLkTEVITHANLVRYAGASGDFNPIHNDPDFARKTGLDGTIAHGMYVMAQLGRLCTSWA-DQKQIKEFGVTFKN 89
Cdd:cd03453    1 VGDELPPL-TPPVSRADLVRYAGASGDFNPIHYDEDFAKKVGLPGVIAHGMLTMGLLGRLVTDWVgDPGRVVSFGVRFTK 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 445956505  90 MTKPGQKLTCTGKVKRKKEENGEKLITVAVEATDDSGEVKCSGEMVVV 137
Cdd:cd03453   80 PVPVPDTLTCTGIVVEKTVADGEDALTVTVDATDQAGGKKVLGRAIVA 127
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
6-138 1.47e-40

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 132.32  E-value: 1.47e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445956505   6 YDKMEVGQELPPLkTEVITHANLVRYAGASGDFNPIHNDPDFARKTGLDGTIAHGMYVMAQLGRLCTSWADQKQ---IKE 82
Cdd:COG2030    2 FEDLEVGDVLPHG-GRTVTEEDIVLFAGATGDPNPIHLDEEAAAATGFGGRIAHGMLTLSLASGLLVDDLPGTAvanLGL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 445956505  83 FGVTFKNMTKPGQKLTCTGKVKRKKEENGEKLITVAVEATDDSGEVKCSGEMVVVA 138
Cdd:COG2030   81 QEVRFLRPVRVGDTLRARVEVLEKRESKSRGIVTLRTTVTNQDGEVVLTGEATVLV 136
PRK13693 PRK13693
(3R)-hydroxyacyl-ACP dehydratase subunit HadB; Provisional
 1-138 6.44e-25

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


Pssm-ID: 184249 [Multi-domain]  Cd Length: 142  Bit Score: 92.59  E-value: 6.44e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445956505   1 MSKIEYDKMEVGQELPPlKTEVITHANLVRYAGASGDFNPIHNDPDFARKTGLDGTIAHGMYVMAQLGRLCTSW-ADQKQ 79
Cdd:PRK13693   1 MALREFSSVKVGDQLPE-KTYPLTRQDLVNYAGVSGDLNPIHWDDEIAKVVGLDTAIAHGMLTMGLGGGYVTSWvGDPGA 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445956505  80 IKEFGVTFKNMT-----KPGQKLTCTGKVKRKKEEngEKLITVAVEATddSGEVKCSGEMVVVA 138
Cdd:PRK13693  80 VTEYNVRFTAVVpvpndGKGAELVFNGRVKSVDPE--SKSVTIALTAT--TGGKKIFGRAIASA 139
MaoC_dehydratas pfam01575
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ...
 10-121 4.92e-23

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: 87.01  E-value: 4.92e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445956505   10 EVGQELPPLKTEVITHANLVRYAGASGDFNPIHNDPDFARKTGLDGTIAHGMYVMAQLGRLCTSWA---DQKQIKEFGVT 86
Cdd:pfam01575   5 APGEPPDTEKPRTVTEADIALFALVSGDHNPIHVDPEFAKKAGFGGPIAHGMLTLAIVAGLVEEWGgdnVIARFGEIKVR 84

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 445956505   87 FKNMTKPGQKL----TCTGKVKRKKEENGEKLITVAVEA 121
Cdd:pfam01575  85 FTKPVFPGDTLrteaEVVGKRDGRQTKVVEVTVEVTEVA 123
fused_HadA_HadB NF040620
fused (3R)-hydroxyacyl-ACP dehydratase subunits HadA/HadB;
4-104 7.86e-22

fused (3R)-hydroxyacyl-ACP dehydratase subunits HadA/HadB;


Pssm-ID: 468592 [Multi-domain]  Cd Length: 329  Bit Score: 88.35  E-value: 7.86e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445956505   4 IEYDKMEVGQELPPLKTEViTHANLVRYAGASGDFNPIHNDPDFARKTGLDGTIAHGMYVMAQLGRLCTSWA-DQKQIKE 82
Cdd:NF040620 194 IDFDDLAVGDELPPRTVRL-TRGDLVNYAGVSGDPNPIHWSDEVARLAGLPTVVAHGMLTMGLGAGYLTSWLgDPGAVTK 272

                         90       100
                 ....*....|....*....|....*..
gi 445956505  83 FGVTFKNM-----TKPGQkLTCTGKVK 104
Cdd:NF040620 273 YSVRFTSPvyvpaDAPAE-IEFTGKVK 298
 
Name Accession Description Interval E-value
SAV4209_like cd03453
SAV4209_like. Similar in sequence to the Streptomyces avermitilis SAV4209 protein, with a hot ...
 11-137 2.57e-62

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: 186.76  E-value: 2.57e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445956505  11 VGQELPPLkTEVITHANLVRYAGASGDFNPIHNDPDFARKTGLDGTIAHGMYVMAQLGRLCTSWA-DQKQIKEFGVTFKN 89
Cdd:cd03453    1 VGDELPPL-TPPVSRADLVRYAGASGDFNPIHYDEDFAKKVGLPGVIAHGMLTMGLLGRLVTDWVgDPGRVVSFGVRFTK 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 445956505  90 MTKPGQKLTCTGKVKRKKEENGEKLITVAVEATDDSGEVKCSGEMVVV 137
Cdd:cd03453   80 PVPVPDTLTCTGIVVEKTVADGEDALTVTVDATDQAGGKKVLGRAIVA 127
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
6-138 1.47e-40

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 132.32  E-value: 1.47e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445956505   6 YDKMEVGQELPPLkTEVITHANLVRYAGASGDFNPIHNDPDFARKTGLDGTIAHGMYVMAQLGRLCTSWADQKQ---IKE 82
Cdd:COG2030    2 FEDLEVGDVLPHG-GRTVTEEDIVLFAGATGDPNPIHLDEEAAAATGFGGRIAHGMLTLSLASGLLVDDLPGTAvanLGL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 445956505  83 FGVTFKNMTKPGQKLTCTGKVKRKKEENGEKLITVAVEATDDSGEVKCSGEMVVVA 138
Cdd:COG2030   81 QEVRFLRPVRVGDTLRARVEVLEKRESKSRGIVTLRTTVTNQDGEVVLTGEATVLV 136
R_hydratase_like cd03441
(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl ...
 16-137 6.10e-36

(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: 120.06  E-value: 6.10e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445956505  16 PPLKTEVITHANLVRYAGASGDFNPIHNDPDFARKTGLDGTIAHGMYVMAQLGRLCTSWADQK---QIKEFGVTFKNMTK 92
Cdd:cd03441    3 LDSSGRTVTEADIALFARLSGDPNPIHVDPEYAKAAGFGGRIAHGMLTLSLASGLLVQWLPGTdgaNLGSQSVRFLAPVF 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 445956505  93 PGQKLTCTGKVKRKKEENGEKLITVAVEATDDSGEVKCSGEMVVV 137
Cdd:cd03441   83 PGDTLRVEVEVLGKRPSKGRGVVTVRTEARNQGGEVVLSGEATVL 127
PRK13693 PRK13693
(3R)-hydroxyacyl-ACP dehydratase subunit HadB; Provisional
 1-138 6.44e-25

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


Pssm-ID: 184249 [Multi-domain]  Cd Length: 142  Bit Score: 92.59  E-value: 6.44e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445956505   1 MSKIEYDKMEVGQELPPlKTEVITHANLVRYAGASGDFNPIHNDPDFARKTGLDGTIAHGMYVMAQLGRLCTSW-ADQKQ 79
Cdd:PRK13693   1 MALREFSSVKVGDQLPE-KTYPLTRQDLVNYAGVSGDLNPIHWDDEIAKVVGLDTAIAHGMLTMGLGGGYVTSWvGDPGA 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445956505  80 IKEFGVTFKNMT-----KPGQKLTCTGKVKRKKEEngEKLITVAVEATddSGEVKCSGEMVVVA 138
Cdd:PRK13693  80 VTEYNVRFTAVVpvpndGKGAELVFNGRVKSVDPE--SKSVTIALTAT--TGGKKIFGRAIASA 139
MaoC_dehydratas pfam01575
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ...
 10-121 4.92e-23

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: 87.01  E-value: 4.92e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445956505   10 EVGQELPPLKTEVITHANLVRYAGASGDFNPIHNDPDFARKTGLDGTIAHGMYVMAQLGRLCTSWA---DQKQIKEFGVT 86
Cdd:pfam01575   5 APGEPPDTEKPRTVTEADIALFALVSGDHNPIHVDPEFAKKAGFGGPIAHGMLTLAIVAGLVEEWGgdnVIARFGEIKVR 84

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 445956505   87 FKNMTKPGQKL----TCTGKVKRKKEENGEKLITVAVEA 121
Cdd:pfam01575  85 FTKPVFPGDTLrteaEVVGKRDGRQTKVVEVTVEVTEVA 123
fused_HadA_HadB NF040620
fused (3R)-hydroxyacyl-ACP dehydratase subunits HadA/HadB;
4-104 7.86e-22

fused (3R)-hydroxyacyl-ACP dehydratase subunits HadA/HadB;


Pssm-ID: 468592 [Multi-domain]  Cd Length: 329  Bit Score: 88.35  E-value: 7.86e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445956505   4 IEYDKMEVGQELPPLKTEViTHANLVRYAGASGDFNPIHNDPDFARKTGLDGTIAHGMYVMAQLGRLCTSWA-DQKQIKE 82
Cdd:NF040620 194 IDFDDLAVGDELPPRTVRL-TRGDLVNYAGVSGDPNPIHWSDEVARLAGLPTVVAHGMLTMGLGAGYLTSWLgDPGAVTK 272

                         90       100
                 ....*....|....*....|....*..
gi 445956505  83 FGVTFKNM-----TKPGQkLTCTGKVK 104
Cdd:NF040620 273 YSVRFTSPvyvpaDAPAE-IEFTGKVK 298
FAS_MaoC cd03447
FAS_MaoC, the MaoC-like hot dog fold of the fatty acid synthase, beta subunit. Other enzymes ...
 31-136 4.00e-21

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: 82.33  E-value: 4.00e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445956505  31 YAGASGDFNPIHNDPDFARKTGLDGTIAHGMYVMAQLGRLCTSWA---DQKQIKEFGVTFKNMTKPGQKLTCtgKVKRKK 107
Cdd:cd03447   18 YARVSGDFNPIHVSRVFASYAGLPGTITHGMYTSAAVRALVETWAadnDRSRVRSFTASFVGMVLPNDELEV--RLEHVG 95

                         90       100
                 ....*....|....*....|....*....
gi 445956505 108 EENGEKLITVAVEAtDDSGEVKCSGEMVV 136
Cdd:cd03447   96 MVDGRKVIKVEARN-EETGELVLRGEAEV 123
R_hydratase cd03449
(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA ...
 10-138 1.17e-19

(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: 78.36  E-value: 1.17e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445956505  10 EVGQELPPLKTevITHANLVRYAGASGDFNPIHNDPDFARKTGLDGTIAHGM----YVMAQLGRLC----TSWADQkqik 81
Cdd:cd03449    2 KVGDSASLTRT--ITEEDVELFAELSGDFNPIHLDEEYAKKTRFGGRIAHGMltasLISAVLGTLLpgpgTIYLSQ---- 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 445956505  82 efGVTFKNMTKPGQKLTCTGKVKRKKEENgeKLITVAVEATDDSGEVKCSGEMVVVA 138
Cdd:cd03449   76 --SLRFLRPVFIGDTVTATVTVTEKREDK--KRVTLETVCTNQNGEVVIEGEAVVLA 128
SAV4209 cd03455
SAV4209 is a Streptomyces avermitilis protein with a hot dog fold that is similar to those of ...
 12-137 1.36e-18

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: 75.82  E-value: 1.36e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445956505  12 GQELPPLKTEvITHANLVRYAGASGDFNPIHNDPDFARKTGLDGTIAHGMYVMAQLGRLCTSWA-DQKQIKEFGVTFKNM 90
Cdd:cd03455    1 GDELPRLSIP-PDPTLLFRYSAATRDFHRIHHDRDYARAVGYPDLYVNGPTLAGLVIRYVTDWAgPDARVKSFAFRLGAP 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 445956505  91 TKPGQKLTCTGKVKRKkeeNGEKLITVAVEATDDSGEVKCSGEMVVV 137
Cdd:cd03455   80 LYAGDTLRFGGRVTAK---RDDEVVTVELWARNSEGDHVMAGTATVA 123
MaoC_like cd03446
MoaC_like Similar to the MaoC (monoamine oxidase C) dehydratase regulatory protein but ...
 5-136 2.50e-15

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: 67.71  E-value: 2.50e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445956505   5 EYDKMEVGQELPPL-KTevITHANLVRYAGASGDFNPIHNDPDFARKTGLDGTIAHGMYVMAQLgrlcTSWADQKQIKE- 82
Cdd:cd03446    1 YFEDFEIGQVFESVgRT--VTEADVVMFAGLSGDWNPIHTDAEYAKKTRFGERIAHGLLTLSIA----TGLLQRLGVFEr 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445956505  83 -----FGV---TFKNMTKPGQKLTCTGKVKRKKEENGEK--LITVAVEATDDSGEVKCSGEMVV 136
Cdd:cd03446   75 tvvafYGIdnlRFLNPVFIGDTIRAEAEVVEKEEKDGEDagVVTRRIEVVNQRGEVVQSGEMSL 138
PRK08190 PRK08190
bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated
 6-138 1.24e-13

bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated


Pssm-ID: 236180 [Multi-domain]  Cd Length: 466  Bit Score: 66.44  E-value: 1.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445956505   6 YDKMEVGQ--ELpplkTEVITHANLVRYAGASGDFNPIHNDPDFARKTGLDGTIAHGMYVMAQ----LG-RL---CTSWA 75
Cdd:PRK08190  11 FDEIAIGDsaSL----VRTLTPDDIELFAAMSGDVNPAHLDAAYAASDGFHHVVAHGMWGGALisavLGtRLpgpGTIYL 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 445956505  76 DQkqikefGVTFKNMTKPGQKLTCTGKVKRKKEENgeKLITVAVEATDDSGEVKCSGEMVVVA 138
Cdd:PRK08190  87 GQ------SLRFRRPVRIGDTLTVTVTVREKDPEK--RIVVLDCRCTNQDGEVVITGTAEVIA 141
HDE_HSD cd03448
HDE_HSD The R-hydratase-like hot dog fold of the 17-beta-hydroxysteriod dehydrogenase (HSD), ...
 35-98 3.09e-13

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: 61.85  E-value: 3.09e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 445956505  35 SGDFNPIHNDPDFARKTGLDGTIAHGMYVMAqlgrlCTSWA--------DQKQIKEFGVTFKNMTKPGQKLT 98
Cdd:cd03448   24 SGDYNPLHIDPAFAKAAGFPRPILHGLCTYG-----FAARAvleafadgDPARFKAIKVRFSSPVFPGETLR 90
MaoC_dehydrat_N pfam13452
N-terminal half of MaoC dehydratase; It is clear from the structures of bacterial members of ...
 11-128 3.66e-09

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: 51.54  E-value: 3.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445956505   11 VGQELPPLKTEvITHANLVRYAGASGDFNPIHNDPDFARKTGLDGTIAHGMYVMaqlgrlCTSWADQKQIKEFGV----- 85
Cdd:pfam13452   3 IGVEFGPVKYE-VERGAIREFARAIGETNPAYWDEAAARAAGYGDLPAPPTFLF------VLGWDAPGFMEQLGIdlsrl 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 445956505   86 -------TFKNMTKPGQKLTCTGKVK--RKKEENGE-KLITVAVEATDDSGEV 128
Cdd:pfam13452  76 lhgeqrfTYHRPLRAGDELTCRSQIAdvYDKKGNGAlCFVVVETEVTNQRGEP 128
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 55-137 7.35e-09

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: 49.78  E-value: 7.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445956505  55 GTIAHGMYVMAQLGRLCTSWADQKQIK-------EFGVTFKNMTKPGQKLTCTGKVKRKkeenGEKLITVAVEATDDSGE 127
Cdd:cd03440   15 GGIVHGGLLLALADEAAGAAAARLGGRglgavtlSLDVRFLRPVRPGDTLTVEAEVVRV----GRSSVTVEVEVRNEDGK 90

                         90
                 ....*....|
gi 445956505 128 VKCSGEMVVV 137
Cdd:cd03440   91 LVATATATFV 100
NodN cd03450
NodN (nodulation factor N) contains a single hot dog fold similar to those of the peroxisomal ...
 11-137 7.37e-06

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: 42.94  E-value: 7.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445956505  11 VGQELPPLKTEVITHANLVRYAGASGDFNPIHNDPDFARKTGLDGTIAHGMYVMAQLGRLctsWADQKQIKEFG------ 84
Cdd:cd03450   12 VGQELGVSDWVTVDQERIDQFADATGDHQWIHVDPERAAAEPFGGTIAHGFLTLSLLPAL---TPQLFRVEGVKmgvnyg 88

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 445956505  85 ---VTFKNMTKPGQKLTCTGKVKRKKEENGEKL-----ITVAVEatdDSGEVKCSGEMVVV 137
Cdd:cd03450   89 ldkVRFPAPVPVGSRVRGRFTLLSVEELKGGGVqvtleVTVEIE---GEDKPACVAEWISR 146
PLN02864 PLN02864
enoyl-CoA hydratase
 35-61 3.40e-05

enoyl-CoA hydratase


Pssm-ID: 178455 [Multi-domain]  Cd Length: 310  Bit Score: 42.08  E-value: 3.40e-05
                         10        20
                 ....*....|....*....|....*..
gi 445956505  35 SGDFNPIHNDPDFARKTGLDGTIAHGM 61
Cdd:PLN02864 207 SGDYNPLHSDPMFAKVAGFTRPILHGL 233
YdeM cd03454
YdeM is a Bacillus subtilis protein that belongs to a family of prokaryotic proteins of unkown ...
 6-137 7.10e-05

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: 39.86  E-value: 7.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445956505   6 YDKMEVGQELPpLKTEVITHANLVRYAGASgDFNPIHNDPDFARKTGLDGTIAHGMYVMAQLGRL-CTSWADQK------ 78
Cdd:cd03454    1 FEDLVIGQRFT-SGSYTVTEEEIIAFAREF-DPQPFHLDEEAAKESLFGGLAASGWHTAAITMRLlVDAGLSGSasggsp 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445956505  79 QIKEfgVTFKNMTKPGQKLTCTGKVK-----RKKEENGekLITVAVEATDDSGEVKCSGEMVVV 137
Cdd:cd03454   79 GIDE--LRWPRPVRPGDTLSVEVEVLdkrpsRSRPDRG--IVTLRSETLNQRGEVVLTFEATVL 138
MaoC_C cd03452
MaoC_C The C-terminal hot dog fold of the MaoC (monoamine oxidase C) dehydratase regulatory ...
 6-127 1.96e-04

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: 38.92  E-value: 1.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445956505   6 YDKMEVGQEL-PPLKTevITHANLVRYAGASGDFNPIHNDPDFARKTGLDGTIAHGMYVMAQLGRLCTSWADQKQIKEFG 84
Cdd:cd03452    2 LEQLRPGDSLlTHRRT--VTEADIVNFACLTGDHFYAHMDEIAAKASFFGKRVAHGYFVLSAAAGLFVDPAPGPVLANYG 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 445956505  85 VT---FKNMTKPGQ----KLTCTGKVKRKKEENGEklITVAVEATDDSGE 127
Cdd:cd03452   80 LEnlrFLEPVYPGDtiqvRLTCKRKIPRDGQDYGV--VRWDAEVTNQNGE 127
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 57-137 2.99e-04

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 38.39  E-value: 2.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445956505  57 IAHGMYVMAQL----GRLCTSWADQKQI---KEFGVTFKNMTKPGQKLTCTGKVKRKkeenGEKLITVAVEATDDSGEV- 128
Cdd:COG2050   49 TVHGGALAALAdsaaGLAANSALPPGRRavtIELNINFLRPARLGDRLTAEARVVRR----GRRLAVVEVEVTDEDGKLv 124

                         90
                 ....*....|
gi 445956505 129 -KCSGEMVVV 137
Cdd:COG2050  125 aTATGTFAVL 134
FkbR2 cd03451
FkbR2 is a Streptomyces hygroscopicus protein with a hot dog fold that belongs to a conserved ...
 6-136 5.52e-03

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: 34.87  E-value: 5.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445956505   6 YDKMEVGQEL--PPLKTevITHANLVRYAGASGDFNPIHNDPDFARKTGLDGTIAHGMYVMAQLGRLCTSWADQKQIKEF 83
Cdd:cd03451    4 FEDFTVGQVFehAPGRT--VTEADNVLFTLLTMNTAPLHFDAAYAAKTEFGRRLVNSLFTLSLALGLSVNDTSLTAVANL 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 445956505  84 G---VTFKNMTKPGQKLTCTGKVKRKKEENGEK---LITVAVEATDDSGEVKCSGEMVV 136
Cdd:cd03451   82 GydeVRFPAPVFHGDTLYAESEVLSKRESKSRPdagIVTVRTVGYNQDGEPVLSFERTA 140
 
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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