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Conserved domains on  [gi|1063742355|ref|NP_001318847|]
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hydroxyacyl-thioester dehydratase type-like protein [Arabidopsis thaliana]

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 ...
 26-154 1.17e-52

(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: 163.48  E-value: 1.17e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063742355  26 LKVGDVLRETRVFSSEDIKAYAEVSHDWNPLHFDPESARKAGFENRLVHGMLVSSMFPRIISAHFP--GAVYVSQSLHFR 103
Cdd:cd03449     1 LKVGDSASLTRTITEEDVELFAELSGDFNPIHLDEEYAKKTRFGGRIAHGMLTASLISAVLGTLLPgpGTIYLSQSLRFL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1063742355 104 SPVYIGDEILGLVQAIALRETKNkyIVKFSTKCFkNHNELVVIDGEATAIL 154
Cdd:cd03449    81 RPVFIGDTVTATVTVTEKREDKK--RVTLETVCT-NQNGEVVIEGEAVVLA 128
 
Name Accession Description Interval E-value
R_hydratase cd03449
(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA ...
 26-154 1.17e-52

(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: 163.48  E-value: 1.17e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063742355  26 LKVGDVLRETRVFSSEDIKAYAEVSHDWNPLHFDPESARKAGFENRLVHGMLVSSMFPRIISAHFP--GAVYVSQSLHFR 103
Cdd:cd03449     1 LKVGDSASLTRTITEEDVELFAELSGDFNPIHLDEEYAKKTRFGGRIAHGMLTASLISAVLGTLLPgpGTIYLSQSLRFL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1063742355 104 SPVYIGDEILGLVQAIALRETKNkyIVKFSTKCFkNHNELVVIDGEATAIL 154
Cdd:cd03449    81 RPVFIGDTVTATVTVTEKREDKK--RVTLETVCT-NQNGEVVIEGEAVVLA 128
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
26-155 1.34e-40

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 133.47  E-value: 1.34e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063742355  26 LKVGDVLR-ETRVFSSEDIKAYAEVSHDWNPLHFDPESARKAGFENRLVHGMLVSSMFPRIISAHFPGAV---YVSQSLH 101
Cdd:COG2030     5 LEVGDVLPhGGRTVTEEDIVLFAGATGDPNPIHLDEEAAAATGFGGRIAHGMLTLSLASGLLVDDLPGTAvanLGLQEVR 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1063742355 102 FRSPVYIGDEILGLVQAIALRETKNKYIVKFSTKCFKNHNElVVIDGEATAILP 155
Cdd:COG2030    85 FLRPVRVGDTLRARVEVLEKRESKSRGIVTLRTTVTNQDGE-VVLTGEATVLVP 137
PRK08190 PRK08190
bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated
 26-155 5.65e-26

bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated


Pssm-ID: 236180 [Multi-domain]  Cd Length: 466  Bit Score: 102.27  E-value: 5.65e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063742355  26 LKVGDVLRETRVFSSEDIKAYAEVSHDWNPLHFDPESARKAGFENRLVHGMLVSSMfpriISAHF------PGAVYVSQS 99
Cdd:PRK08190   14 IAIGDSASLVRTLTPDDIELFAAMSGDVNPAHLDAAYAASDGFHHVVAHGMWGGAL----ISAVLgtrlpgPGTIYLGQS 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1063742355 100 LHFRSPVYIGDEILGLVQAIALRETKNkyIVKFSTKCfKNHNELVVIDGEATAILP 155
Cdd:PRK08190   90 LRFRRPVRIGDTLTVTVTVREKDPEKR--IVVLDCRC-TNQDGEVVITGTAEVIAP 142
MaoC_dehydratas pfam01575
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ...
 39-112 3.92e-19

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: 78.15  E-value: 3.92e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063742355  39 SSEDIKAYAEVSHDWNPLHFDPESARKAGFENRLVHGMLVSSMFPRIISAHFPG---AVYVSQSLHFRSPVYIGDEI 112
Cdd:pfam01575  19 TEADIALFALVSGDHNPIHVDPEFAKKAGFGGPIAHGMLTLAIVAGLVEEWGGDnviARFGEIKVRFTKPVFPGDTL 95
 
Name Accession Description Interval E-value
R_hydratase cd03449
(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA ...
 26-154 1.17e-52

(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: 163.48  E-value: 1.17e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063742355  26 LKVGDVLRETRVFSSEDIKAYAEVSHDWNPLHFDPESARKAGFENRLVHGMLVSSMFPRIISAHFP--GAVYVSQSLHFR 103
Cdd:cd03449     1 LKVGDSASLTRTITEEDVELFAELSGDFNPIHLDEEYAKKTRFGGRIAHGMLTASLISAVLGTLLPgpGTIYLSQSLRFL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1063742355 104 SPVYIGDEILGLVQAIALRETKNkyIVKFSTKCFkNHNELVVIDGEATAIL 154
Cdd:cd03449    81 RPVFIGDTVTATVTVTEKREDKK--RVTLETVCT-NQNGEVVIEGEAVVLA 128
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
26-155 1.34e-40

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 133.47  E-value: 1.34e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063742355  26 LKVGDVLR-ETRVFSSEDIKAYAEVSHDWNPLHFDPESARKAGFENRLVHGMLVSSMFPRIISAHFPGAV---YVSQSLH 101
Cdd:COG2030     5 LEVGDVLPhGGRTVTEEDIVLFAGATGDPNPIHLDEEAAAATGFGGRIAHGMLTLSLASGLLVDDLPGTAvanLGLQEVR 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1063742355 102 FRSPVYIGDEILGLVQAIALRETKNKYIVKFSTKCFKNHNElVVIDGEATAILP 155
Cdd:COG2030    85 FLRPVRVGDTLRARVEVLEKRESKSRGIVTLRTTVTNQDGE-VVLTGEATVLVP 137
R_hydratase_like cd03441
(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl ...
 29-153 7.14e-37

(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: 123.53  E-value: 7.14e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063742355  29 GDVLRETRVFSSEDIKAYAEVSHDWNPLHFDPESARKAGFENRLVHGMLVSSMFPRIISAHFP---GAVYVSQSLHFRSP 105
Cdd:cd03441     1 GELDSSGRTVTEADIALFARLSGDPNPIHVDPEYAKAAGFGGRIAHGMLTLSLASGLLVQWLPgtdGANLGSQSVRFLAP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1063742355 106 VYIGDEILGLVQAIALRETKNKYIVKFSTKCFkNHNELVVIDGEATAI 153
Cdd:cd03441    81 VFPGDTLRVEVEVLGKRPSKGRGVVTVRTEAR-NQGGEVVLSGEATVL 127
PRK08190 PRK08190
bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated
 26-155 5.65e-26

bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated


Pssm-ID: 236180 [Multi-domain]  Cd Length: 466  Bit Score: 102.27  E-value: 5.65e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063742355  26 LKVGDVLRETRVFSSEDIKAYAEVSHDWNPLHFDPESARKAGFENRLVHGMLVSSMfpriISAHF------PGAVYVSQS 99
Cdd:PRK08190   14 IAIGDSASLVRTLTPDDIELFAAMSGDVNPAHLDAAYAASDGFHHVVAHGMWGGAL----ISAVLgtrlpgPGTIYLGQS 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1063742355 100 LHFRSPVYIGDEILGLVQAIALRETKNkyIVKFSTKCfKNHNELVVIDGEATAILP 155
Cdd:PRK08190   90 LRFRRPVRIGDTLTVTVTVREKDPEKR--IVVLDCRC-TNQDGEVVITGTAEVIAP 142
MaoC_dehydratas pfam01575
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ...
 39-112 3.92e-19

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: 78.15  E-value: 3.92e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063742355  39 SSEDIKAYAEVSHDWNPLHFDPESARKAGFENRLVHGMLVSSMFPRIISAHFPG---AVYVSQSLHFRSPVYIGDEI 112
Cdd:pfam01575  19 TEADIALFALVSGDHNPIHVDPEFAKKAGFGGPIAHGMLTLAIVAGLVEEWGGDnviARFGEIKVRFTKPVFPGDTL 95
SAV4209_like cd03453
SAV4209_like. Similar in sequence to the Streptomyces avermitilis SAV4209 protein, with a hot ...
 28-150 2.85e-16

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: 70.81  E-value: 2.85e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063742355  28 VGDVLRE-TRVFSSEDIKAYAEVSHDWNPLHFDPESARKAGFENRLVHGMLVSSMFPRIIS--AHFPGAVyVSQSLHFRS 104
Cdd:cd03453     1 VGDELPPlTPPVSRADLVRYAGASGDFNPIHYDEDFAKKVGLPGVIAHGMLTMGLLGRLVTdwVGDPGRV-VSFGVRFTK 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1063742355 105 PVYIGDEILGLVQAIALRETKNKYIVKFSTKCFKNHNELVVIdGEA 150
Cdd:cd03453    80 PVPVPDTLTCTGIVVEKTVADGEDALTVTVDATDQAGGKKVL-GRA 124
MaoC_like cd03446
MoaC_like Similar to the MaoC (monoamine oxidase C) dehydratase regulatory protein but ...
 28-154 2.28e-14

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: 66.17  E-value: 2.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063742355  28 VGDVLRET-RVFSSEDIKAYAEVSHDWNPLHFDPESARKAGFENRLVHGMLVSS------MFPRIISAHFPgAVYVSQSL 100
Cdd:cd03446     7 IGQVFESVgRTVTEADVVMFAGLSGDWNPIHTDAEYAKKTRFGERIAHGLLTLSiatgllQRLGVFERTVV-AFYGIDNL 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1063742355 101 HFRSPVYIGDEILGLVQAIALRE-TKNKY-IVKFSTKcFKNHNELVVIDGEATAIL 154
Cdd:cd03446    86 RFLNPVFIGDTIRAEAEVVEKEEkDGEDAgVVTRRIE-VVNQRGEVVQSGEMSLLV 140
PRK13693 PRK13693
(3R)-hydroxyacyl-ACP dehydratase subunit HadB; Provisional
 12-108 9.53e-13

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


Pssm-ID: 184249 [Multi-domain]  Cd Length: 142  Bit Score: 61.77  E-value: 9.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063742355  12 LVLRSFSSVasktllKVGDVLRETRV-FSSEDIKAYAEVSHDWNPLHFDPESARKAGFENRLVHGMLVSSMFPRIISAHF 90
Cdd:PRK13693    1 MALREFSSV------KVGDQLPEKTYpLTRQDLVNYAGVSGDLNPIHWDDEIAKVVGLDTAIAHGMLTMGLGGGYVTSWV 74

                          90       100
                  ....*....|....*....|
gi 1063742355  91 --PGAVyVSQSLHFRSPVYI 108
Cdd:PRK13693   75 gdPGAV-TEYNVRFTAVVPV 93
MaoC_C cd03452
MaoC_C The C-terminal hot dog fold of the MaoC (monoamine oxidase C) dehydratase regulatory ...
 26-146 2.92e-11

MaoC_C The C-terminal hot dog fold of the MaoC (monoamine oxidase C) dehydratase regulatory protein. Orthologs of MaoC include PaaZ [Escherichia coli] and PaaN [Pseudomonas putida], which are putative ring-opening enzymes involved in phenylacetic acid degradation. The C-terminal domain of MaoC has sequence similarity to (R)-specific enoyl-CoA hydratase,Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit. MaoC also has an N-terminal PutA domain like that found in the E. coli PutA proline dehydrogenase and other members of the aldehyde dehydrogenase family.


Pssm-ID: 239536 [Multi-domain]  Cd Length: 142  Bit Score: 57.79  E-value: 2.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063742355  26 LKVGD-VLRETRVFSSEDIKAYAEVSHDWNPLHFDPESARKAGFENRLVHGMLVSSMFPRIISAHFPGAV---YVSQSLH 101
Cdd:cd03452     5 LRPGDsLLTHRRTVTEADIVNFACLTGDHFYAHMDEIAAKASFFGKRVAHGYFVLSAAAGLFVDPAPGPVlanYGLENLR 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1063742355 102 FRSPVYIGDEILG--LVQAIALRETKNKYIVKFSTKCFKNHNELVVI 146
Cdd:cd03452    85 FLEPVYPGDTIQVrlTCKRKIPRDGQDYGVVRWDAEVTNQNGELVAS 131
FAS_MaoC cd03447
FAS_MaoC, the MaoC-like hot dog fold of the fatty acid synthase, beta subunit. Other enzymes ...
 32-150 3.69e-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: 51.90  E-value: 3.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063742355  32 LRETRVFSSEDIKAYAEVSHDWNPLHFDPESARKAGFENRLVHGMLVSSMFPRIISAHFPGAV---YVSQSLHFRSPVYI 108
Cdd:cd03447     4 GASLTITAPASNEPYARVSGDFNPIHVSRVFASYAGLPGTITHGMYTSAAVRALVETWAADNDrsrVRSFTASFVGMVLP 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1063742355 109 GDEILGLVQAIALREtkNKYIVKFstKCFKNHNELVVIDGEA 150
Cdd:cd03447    84 NDELEVRLEHVGMVD--GRKVIKV--EARNEETGELVLRGEA 121
HDE_HSD cd03448
HDE_HSD The R-hydratase-like hot dog fold of the 17-beta-hydroxysteriod dehydrogenase (HSD), ...
 50-112 7.83e-09

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: 51.07  E-value: 7.83e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063742355  50 SHDWNPLHFDPESARKAGFENRLVHGMLVSSMFPRIISAHFPG---AVYVSQSLHFRSPVYIGDEI 112
Cdd:cd03448    24 SGDYNPLHIDPAFAKAAGFPRPILHGLCTYGFAARAVLEAFADgdpARFKAIKVRFSSPVFPGETL 89
FkbR2 cd03451
FkbR2 is a Streptomyces hygroscopicus protein with a hot dog fold that belongs to a conserved ...
 54-155 1.31e-08

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: 51.05  E-value: 1.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063742355  54 NPLHFDPESARKAGFENRLVHGMLVSSMfprIISAHFPGavyVSQ---------SLHFRSPVYIGDEILGLVQAIALRET 124
Cdd:cd03451    37 APLHFDAAYAAKTEFGRRLVNSLFTLSL---ALGLSVND---TSLtavanlgydEVRFPAPVFHGDTLYAESEVLSKRES 110

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1063742355 125 KNKY---IVKFSTKCFKNHNElVVIDGEATAILP 155
Cdd:cd03451   111 KSRPdagIVTVRTVGYNQDGE-PVLSFERTALVP 143
SAV4209 cd03455
SAV4209 is a Streptomyces avermitilis protein with a hot dog fold that is similar to those of ...
 34-110 1.64e-08

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: 50.01  E-value: 1.64e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063742355  34 ETRVFSsedikaYAEVSHDWNPLHFDPESARKAGFENRLVHGMLVSSMFPRIISAHF-PGAVYVSQSLHFRSPVYIGD 110
Cdd:cd03455    13 PTLLFR------YSAATRDFHRIHHDRDYARAVGYPDLYVNGPTLAGLVIRYVTDWAgPDARVKSFAFRLGAPLYAGD 84
MaoC_dehydrat_N pfam13452
N-terminal half of MaoC dehydratase; It is clear from the structures of bacterial members of ...
 34-154 5.60e-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: 46.15  E-value: 5.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063742355  34 ETRVFSSEDIKAYAEVSHDWNPLHFDPESARKAGFenrlvHGMLVSSMFPRIIS---AHF--------PGAVYVSQSLHF 102
Cdd:pfam13452  10 VKYEVERGAIREFARAIGETNPAYWDEAAARAAGY-----GDLPAPPTFLFVLGwdaPGFmeqlgidlSRLLHGEQRFTY 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1063742355 103 RSPVYIGDEILGLVQAIALRETKNKYIVKFSTKCfknhNELVVIDGEATAIL 154
Cdd:pfam13452  85 HRPLRAGDELTCRSQIADVYDKKGNGALCFVVVE----TEVTNQRGEPVATR 132
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 68-145 3.69e-05

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


Pssm-ID: 239524 [Multi-domain]  Cd Length: 100  Bit Score: 40.54  E-value: 3.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063742355  68 FENRLVHGMLVSSMFPRIISAHFP-------GAVYVSQSLHFRSPVYIGDEILGLVQAIALRETknkyIVKFSTKCFKNH 140
Cdd:cd03440    13 DGGGIVHGGLLLALADEAAGAAAArlggrglGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRS----SVTVEVEVRNED 88


                  ....*
gi 1063742355 141 NELVV 145
Cdd:cd03440    89 GKLVA 93
YdeM cd03454
YdeM is a Bacillus subtilis protein that belongs to a family of prokaryotic proteins of unkown ...
 26-155 7.08e-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: 40.63  E-value: 7.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063742355  26 LKVGDVLR-ETRVFSSEDIKAYAEVsHDWNPLHFDPESARKAGFeNRLV-HGMLVSSMFPRIISAHFPGAVYVSQS---- 99
Cdd:cd03454     4 LVIGQRFTsGSYTVTEEEIIAFARE-FDPQPFHLDEEAAKESLF-GGLAaSGWHTAAITMRLLVDAGLSGSASGGSpgid 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063742355 100 -LHFRSPVYIGDEILGLVQAIALRETKNK---YIVKFSTKCFkNHNELVVIDGEATAILP 155
Cdd:cd03454    82 eLRWPRPVRPGDTLSVEVEVLDKRPSRSRpdrGIVTLRSETL-NQRGEVVLTFEATVLVR 140
NodN cd03450
NodN (nodulation factor N) contains a single hot dog fold similar to those of the peroxisomal ...
 41-84 3.28e-04

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: 38.70  E-value: 3.28e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1063742355  41 EDIKAYAEVSHDWNPLHFDPESARKAGFENRLVHGMLVSSMFPR 84
Cdd:cd03450    27 ERIDQFADATGDHQWIHVDPERAAAEPFGGTIAHGFLTLSLLPA 70
PLN02864 PLN02864
enoyl-CoA hydratase
 49-76 8.71e-04

enoyl-CoA hydratase


Pssm-ID: 178455 [Multi-domain]  Cd Length: 310  Bit Score: 38.61  E-value: 8.71e-04
                          10        20
                  ....*....|....*....|....*...
gi 1063742355  49 VSHDWNPLHFDPESARKAGFENRLVHGM 76
Cdd:PLN02864  206 LSGDYNPLHSDPMFAKVAGFTRPILHGL 233
 
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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