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Conserved domains on  [gi|2026374909|emb|CAE6819275|]
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hypothetical protein R70006_06124 [Paraburkholderia domus]

Protein Classification

MaoC family dehydratase N-terminal domain-containing protein( domain architecture ID 10602981)

MaoC family dehydratase N-terminal domain-containing protein belonging to the hotdog fold superfamily of thioesterases and dehydratases

CATH:  3.10.129.10
Gene Ontology:  GO:0016836
PubMed:  15307895

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MaoC_dehydrat_N pfam13452
N-terminal half of MaoC dehydratase; It is clear from the structures of bacterial members of ...
 5-137 9.58e-62

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: 185.97  E-value: 9.58e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026374909   5 KHIGKVIPSFRTVAEAGRLRFFAKATGETNPVYFDESAARDAGHPGLPLPPTFLFSLELEQPDksWRDEIGIQVARILHG 84
Cdd:pfam13452   1 ALIGVEFGPVKYEVERGAIREFARAIGETNPAYWDEAAARAAGYGDLPAPPTFLFVLGWDAPG--FMEQLGIDLSRLLHG 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2026374909  85 EQSFTYHRMAYAGDVLLFECRIADIYDKKG-GALDFVVRETRVTNQNGEHVADM 137
Cdd:pfam13452  79 EQRFTYHRPLRAGDELTCRSQIADVYDKKGnGALCFVVVETEVTNQRGEPVATR 132
 
Name Accession Description Interval E-value
MaoC_dehydrat_N pfam13452
N-terminal half of MaoC dehydratase; It is clear from the structures of bacterial members of ...
 5-137 9.58e-62

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: 185.97  E-value: 9.58e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026374909   5 KHIGKVIPSFRTVAEAGRLRFFAKATGETNPVYFDESAARDAGHPGLPLPPTFLFSLELEQPDksWRDEIGIQVARILHG 84
Cdd:pfam13452   1 ALIGVEFGPVKYEVERGAIREFARAIGETNPAYWDEAAARAAGYGDLPAPPTFLFVLGWDAPG--FMEQLGIDLSRLLHG 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2026374909  85 EQSFTYHRMAYAGDVLLFECRIADIYDKKG-GALDFVVRETRVTNQNGEHVADM 137
Cdd:pfam13452  79 EQRFTYHRPLRAGDELTCRSQIADVYDKKGnGALCFVVVETEVTNQRGEPVATR 132
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
6-144 1.80e-24

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 91.49  E-value: 1.80e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026374909   6 HIGKVIPSFRTVAEAGRLRFFAKATGETNPVYFDESAARDAGHPGLPLPPTFLFSLeleQPDKSWRDEIGIQVARIlhGE 85
Cdd:COG2030     6 EVGDVLPHGGRTVTEEDIVLFAGATGDPNPIHLDEEAAAATGFGGRIAHGMLTLSL---ASGLLVDDLPGTAVANL--GL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026374909  86 QSFTYHRMAYAGDVLLFECRIADIYDKKGGALdfVVRETRVTNQNGEHVADMRS-VLVHR 144
Cdd:COG2030    81 QEVRFLRPVRVGDTLRARVEVLEKRESKSRGI--VTLRTTVTNQDGEVVLTGEAtVLVPR 138
R_hydratase_like cd03441
(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl ...
 8-142 3.13e-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. 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: 77.69  E-value: 3.13e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026374909   8 GKVIPSFRTVAEAgRLRFFAKATGETNPVYFDESAARDAGHPGLPLPPTFLFSLELEQpdksWRDEIGiQVARILHGEQS 87
Cdd:cd03441     1 GELDSSGRTVTEA-DIALFARLSGDPNPIHVDPEYAKAAGFGGRIAHGMLTLSLASGL----LVQWLP-GTDGANLGSQS 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2026374909  88 FTYHRMAYAGDVLLFECRIADIYDKKGgaLDFVVRETRVTNQNGEHVADMRSVLV 142
Cdd:cd03441    75 VRFLAPVFPGDTLRVEVEVLGKRPSKG--RGVVTVRTEARNQGGEVVLSGEATVL 127
PRK13691 PRK13691
(3R)-hydroxyacyl-ACP dehydratase subunit HadC; Provisional
 22-146 8.83e-14

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


Pssm-ID: 139768 [Multi-domain]  Cd Length: 166  Bit Score: 64.46  E-value: 8.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026374909  22 RLRFFAKATGETNPVYFDESAARDAGHPGLPLPPTFLFSL-ELEQPDKSWRDEIGIQVARILHGEQSFTYHRMAYAGDVL 100
Cdd:PRK13691   24 QIRQFARAVKCDHPAFFSEDAAAELGYDALVAPLTFVTIFaKYVQLDFFRHVDVGMETMQIVQVDQRFVFHKPVLAGDKL 103

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2026374909 101 LFECRIADIyDKKGGAlDFVVRETRVTNQNGEHVADMRSVLVHRNG 146
Cdd:PRK13691  104 WARMDIHSV-DERFGA-DIVVTRNVCTNDDGELVMEAYTTLMGQQG 147
 
Name Accession Description Interval E-value
MaoC_dehydrat_N pfam13452
N-terminal half of MaoC dehydratase; It is clear from the structures of bacterial members of ...
 5-137 9.58e-62

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: 185.97  E-value: 9.58e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026374909   5 KHIGKVIPSFRTVAEAGRLRFFAKATGETNPVYFDESAARDAGHPGLPLPPTFLFSLELEQPDksWRDEIGIQVARILHG 84
Cdd:pfam13452   1 ALIGVEFGPVKYEVERGAIREFARAIGETNPAYWDEAAARAAGYGDLPAPPTFLFVLGWDAPG--FMEQLGIDLSRLLHG 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2026374909  85 EQSFTYHRMAYAGDVLLFECRIADIYDKKG-GALDFVVRETRVTNQNGEHVADM 137
Cdd:pfam13452  79 EQRFTYHRPLRAGDELTCRSQIADVYDKKGnGALCFVVVETEVTNQRGEPVATR 132
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
6-144 1.80e-24

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 91.49  E-value: 1.80e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026374909   6 HIGKVIPSFRTVAEAGRLRFFAKATGETNPVYFDESAARDAGHPGLPLPPTFLFSLeleQPDKSWRDEIGIQVARIlhGE 85
Cdd:COG2030     6 EVGDVLPHGGRTVTEEDIVLFAGATGDPNPIHLDEEAAAATGFGGRIAHGMLTLSL---ASGLLVDDLPGTAVANL--GL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026374909  86 QSFTYHRMAYAGDVLLFECRIADIYDKKGGALdfVVRETRVTNQNGEHVADMRS-VLVHR 144
Cdd:COG2030    81 QEVRFLRPVRVGDTLRARVEVLEKRESKSRGI--VTLRTTVTNQDGEVVLTGEAtVLVPR 138
R_hydratase_like cd03441
(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl ...
 8-142 3.13e-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. 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: 77.69  E-value: 3.13e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026374909   8 GKVIPSFRTVAEAgRLRFFAKATGETNPVYFDESAARDAGHPGLPLPPTFLFSLELEQpdksWRDEIGiQVARILHGEQS 87
Cdd:cd03441     1 GELDSSGRTVTEA-DIALFARLSGDPNPIHVDPEYAKAAGFGGRIAHGMLTLSLASGL----LVQWLP-GTDGANLGSQS 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2026374909  88 FTYHRMAYAGDVLLFECRIADIYDKKGgaLDFVVRETRVTNQNGEHVADMRSVLV 142
Cdd:cd03441    75 VRFLAPVFPGDTLRVEVEVLGKRPSKG--RGVVTVRTEARNQGGEVVLSGEATVL 127
PRK13691 PRK13691
(3R)-hydroxyacyl-ACP dehydratase subunit HadC; Provisional
 22-146 8.83e-14

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


Pssm-ID: 139768 [Multi-domain]  Cd Length: 166  Bit Score: 64.46  E-value: 8.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026374909  22 RLRFFAKATGETNPVYFDESAARDAGHPGLPLPPTFLFSL-ELEQPDKSWRDEIGIQVARILHGEQSFTYHRMAYAGDVL 100
Cdd:PRK13691   24 QIRQFARAVKCDHPAFFSEDAAAELGYDALVAPLTFVTIFaKYVQLDFFRHVDVGMETMQIVQVDQRFVFHKPVLAGDKL 103

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2026374909 101 LFECRIADIyDKKGGAlDFVVRETRVTNQNGEHVADMRSVLVHRNG 146
Cdd:PRK13691  104 WARMDIHSV-DERFGA-DIVVTRNVCTNDDGELVMEAYTTLMGQQG 147
PRK13692 PRK13692
(3R)-hydroxyacyl-ACP dehydratase subunit HadA; Provisional
 17-146 9.79e-11

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


Pssm-ID: 237473  Cd Length: 159  Bit Score: 56.34  E-value: 9.79e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026374909  17 VAEAGRLRFFAKATGETNPVYFDESAARDAGHPGLPLPPTFLFSLELEQPDKSWRD-EIGIQVARILHGEQSFTYHRMAY 95
Cdd:PRK13692   19 EVEREKIREYAVAVQNDDAAYFEEDAAAELGYKGLLAPLTFICVFGYKAQSAFFKHaNIAVADAQIVQVDQVLKFEKPIV 98

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2026374909  96 AGDVLLFECRIADIydKKGGALDFVVRETRVTNQNGEHVADMRSVLVHRNG 146
Cdd:PRK13692   99 AGDKLYCDVYVDSV--REAHGTQIIVTKNIVTNEEGDVVQETYTTLAGRAG 147
R_hydratase cd03449
(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA ...
 15-136 5.44e-06

(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: 42.92  E-value: 5.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026374909  15 RTVAEAgRLRFFAKATGETNPVYFDESAARDAGHPGLPLPPTFLFSLeleqpdkswrdeIGIQVARILHG------EQSF 88
Cdd:cd03449    11 RTITEE-DVELFAELSGDFNPIHLDEEYAKKTRFGGRIAHGMLTASL------------ISAVLGTLLPGpgtiylSQSL 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2026374909  89 TYHRMAYAGDVLLFECRIADIYDKKGgaldFVVRETRVTNQNGEHVAD 136
Cdd:cd03449    78 RFLRPVFIGDTVTATVTVTEKREDKK----RVTLETVCTNQNGEVVIE 121
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 73-142 6.88e-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: 39.38  E-value: 6.88e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026374909  73 EIGIQVARILHGEQSFTYHRMAYAGDVLLFECRIADIYDKkggaldFVVRETRVTNQNGEHVADMRSVLV 142
Cdd:cd03440    37 RLGGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRS------SVTVEVEVRNEDGKLVATATATFV 100
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 85-145 4.13e-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: 37.59  E-value: 4.13e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2026374909  85 EQSFTYHRMAYAGDVLLFECRIADIYDKkggaldFVVRETRVTNQNGEHVADMRSVLVHRN 145
Cdd:cd00586    56 ELEIDYLRPLRLGDRLTVETRVLRLGRK------SFTFEQEIFREDGELLATAETVLVCVD 110
FkbR2 cd03451
FkbR2 is a Streptomyces hygroscopicus protein with a hot dog fold that belongs to a conserved ...
 15-146 4.41e-04

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: 37.95  E-value: 4.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026374909  15 RTVAEAGRLrFFAKATGETNPVYFDESAARDAGHPGLPLPPTFLFSLELEQpdkSWRDEIGIQVARILHGEQSFTYHrmA 94
Cdd:cd03451    19 RTVTEADNV-LFTLLTMNTAPLHFDAAYAAKTEFGRRLVNSLFTLSLALGL---SVNDTSLTAVANLGYDEVRFPAP--V 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2026374909  95 YAGDVLLFECRIADIYDKKG----GALDFvvrETRVTNQNGEHVADM-RSVLVHRNG 146
Cdd:cd03451    93 FHGDTLYAESEVLSKRESKSrpdaGIVTV---RTVGYNQDGEPVLSFeRTALVPKRG 146
 
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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