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Conserved domains on  [gi|489185852|ref|WP_003095272|]
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MULTISPECIES: MaoC/PaaZ C-terminal domain-containing protein [Pseudomonas]

Protein Classification

MaoC family dehydratase( domain architecture ID 10005211)

MaoC family dehydratase similar to Pseudomonas aeruginosa (R)-specific enoyl-CoA hydratase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
181-246 3.39e-14

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


:

Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 67.99  E-value: 3.39e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185852 181 ADIgRRYARAAGDYNPIHLSAPSAKLFGFPRAIAHGLWNKARSLAALGERLP----ASGYRVEVRFQKPV 246
Cdd:COG2030   21 EDI-VLFAGATGDPNPIHLDEEAAAATGFGGRIAHGMLTLSLASGLLVDDLPgtavANLGLQEVRFLRPV 89
 
Name Accession Description Interval E-value
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
181-246 3.39e-14

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 67.99  E-value: 3.39e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185852 181 ADIgRRYARAAGDYNPIHLSAPSAKLFGFPRAIAHGLWNKARSLAALGERLP----ASGYRVEVRFQKPV 246
Cdd:COG2030   21 EDI-VLFAGATGDPNPIHLDEEAAAATGFGGRIAHGMLTLSLASGLLVDDLPgtavANLGLQEVRFLRPV 89
R_hydratase cd03449
(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA ...
 181-246 2.06e-12

(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: 62.95  E-value: 2.06e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489185852 181 ADIgRRYARAAGDYNPIHLSAPSAKLFGFPRAIAHGLWnkARSL--AALGERLPASG--YR-VEVRFQKPV 246
Cdd:cd03449   16 EDV-ELFAELSGDFNPIHLDEEYAKKTRFGGRIAHGML--TASLisAVLGTLLPGPGtiYLsQSLRFLRPV 83
MaoC_dehydratas pfam01575
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ...
 154-249 2.31e-12

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: 62.74  E-value: 2.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185852  154 VKVPGEiPPKAEQePLPLEPVDNWkapadigrRYARAAGDYNPIHLSAPSAKLFGFPRAIAHGLWNKARSLAALGERLP- 232
Cdd:pfam01575   3 QNAPGE-PPDTEK-PRTVTEADIA--------LFALVSGDHNPIHVDPEFAKKAGFGGPIAHGMLTLAIVAGLVEEWGGd 72

                          90       100
                  ....*....|....*....|
gi 489185852  233 --ASGYRV-EVRFQKPVLLP 249
Cdd:pfam01575  73 nvIARFGEiKVRFTKPVFPG 92
PRK08190 PRK08190
bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated
 180-248 2.29e-07

bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated


Pssm-ID: 236180 [Multi-domain]  Cd Length: 466  Bit Score: 51.42  E-value: 2.29e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489185852 180 PADIgRRYARAAGDYNPIHLSAPSAKLFGFPRAIAHGLWNKARSLAALGERLPASG--YRVE-VRFQKPVLL 248
Cdd:PRK08190  28 PDDI-ELFAAMSGDVNPAHLDAAYAASDGFHHVVAHGMWGGALISAVLGTRLPGPGtiYLGQsLRFRRPVRI 98
fused_HadA_HadB NF040620
fused (3R)-hydroxyacyl-ACP dehydratase subunits HadA/HadB;
187-249 8.88e-06

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


Pssm-ID: 468592 [Multi-domain]  Cd Length: 329  Bit Score: 46.37  E-value: 8.88e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489185852 187 YARAAGDYNPIHLSAPSAKLFGFPRAIAHGLWNKArsLAA------LGErlPASGYRVEVRFQKPVLLP 249
Cdd:NF040620 220 YAGVSGDPNPIHWSDEVARLAGLPTVVAHGMLTMG--LGAgyltswLGD--PGAVTKYSVRFTSPVYVP 284
 
Name Accession Description Interval E-value
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
181-246 3.39e-14

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 67.99  E-value: 3.39e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185852 181 ADIgRRYARAAGDYNPIHLSAPSAKLFGFPRAIAHGLWNKARSLAALGERLP----ASGYRVEVRFQKPV 246
Cdd:COG2030   21 EDI-VLFAGATGDPNPIHLDEEAAAATGFGGRIAHGMLTLSLASGLLVDDLPgtavANLGLQEVRFLRPV 89
R_hydratase cd03449
(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA ...
 181-246 2.06e-12

(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: 62.95  E-value: 2.06e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489185852 181 ADIgRRYARAAGDYNPIHLSAPSAKLFGFPRAIAHGLWnkARSL--AALGERLPASG--YR-VEVRFQKPV 246
Cdd:cd03449   16 EDV-ELFAELSGDFNPIHLDEEYAKKTRFGGRIAHGML--TASLisAVLGTLLPGPGtiYLsQSLRFLRPV 83
MaoC_dehydratas pfam01575
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ...
 154-249 2.31e-12

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: 62.74  E-value: 2.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185852  154 VKVPGEiPPKAEQePLPLEPVDNWkapadigrRYARAAGDYNPIHLSAPSAKLFGFPRAIAHGLWNKARSLAALGERLP- 232
Cdd:pfam01575   3 QNAPGE-PPDTEK-PRTVTEADIA--------LFALVSGDHNPIHVDPEFAKKAGFGGPIAHGMLTLAIVAGLVEEWGGd 72

                          90       100
                  ....*....|....*....|
gi 489185852  233 --ASGYRV-EVRFQKPVLLP 249
Cdd:pfam01575  73 nvIARFGEiKVRFTKPVFPG 92
SAV4209_like cd03453
SAV4209_like. Similar in sequence to the Streptomyces avermitilis SAV4209 protein, with a hot ...
 186-249 1.05e-10

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: 58.10  E-value: 1.05e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185852 186 RYARAAGDYNPIHLSAPSAKLFGFPRAIAHGLWnkarSLAALGE------RLPASGYRVEVRFQKPVLLP 249
Cdd:cd03453   19 RYAGASGDFNPIHYDEDFAKKVGLPGVIAHGML----TMGLLGRlvtdwvGDPGRVVSFGVRFTKPVPVP 84
FAS_MaoC cd03447
FAS_MaoC, the MaoC-like hot dog fold of the fatty acid synthase, beta subunit. Other enzymes ...
 178-248 4.93e-10

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: 56.13  E-value: 4.93e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489185852 178 KAPADiGRRYARAAGDYNPIHLSAPSAKLFGFPRAIAHGLWNKARSLAALgERLPASGYRVEVR-----FQKPVLL 248
Cdd:cd03447   10 TAPAS-NEPYARVSGDFNPIHVSRVFASYAGLPGTITHGMYTSAAVRALV-ETWAADNDRSRVRsftasFVGMVLP 83
R_hydratase_like cd03441
(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl ...
 180-247 7.13e-10

(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: 55.73  E-value: 7.13e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489185852 180 PADIgRRYARAAGDYNPIHLSAPSAKLFGFPRAIAHGLWnkarsLAALGERL--------PASGYRV-EVRFQKPVL 247
Cdd:cd03441   12 EADI-ALFARLSGDPNPIHVDPEYAKAAGFGGRIAHGML-----TLSLASGLlvqwlpgtDGANLGSqSVRFLAPVF 82
PRK08190 PRK08190
bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated
 180-248 2.29e-07

bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated


Pssm-ID: 236180 [Multi-domain]  Cd Length: 466  Bit Score: 51.42  E-value: 2.29e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489185852 180 PADIgRRYARAAGDYNPIHLSAPSAKLFGFPRAIAHGLWNKARSLAALGERLPASG--YRVE-VRFQKPVLL 248
Cdd:PRK08190  28 PDDI-ELFAAMSGDVNPAHLDAAYAASDGFHHVVAHGMWGGALISAVLGTRLPGPGtiYLGQsLRFRRPVRI 98
fused_HadA_HadB NF040620
fused (3R)-hydroxyacyl-ACP dehydratase subunits HadA/HadB;
187-249 8.88e-06

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


Pssm-ID: 468592 [Multi-domain]  Cd Length: 329  Bit Score: 46.37  E-value: 8.88e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489185852 187 YARAAGDYNPIHLSAPSAKLFGFPRAIAHGLWNKArsLAA------LGErlPASGYRVEVRFQKPVLLP 249
Cdd:NF040620 220 YAGVSGDPNPIHWSDEVARLAGLPTVVAHGMLTMG--LGAgyltswLGD--PGAVTKYSVRFTSPVYVP 284
PRK13693 PRK13693
(3R)-hydroxyacyl-ACP dehydratase subunit HadB; Provisional
 187-249 1.23e-05

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


Pssm-ID: 184249 [Multi-domain]  Cd Length: 142  Bit Score: 44.05  E-value: 1.23e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489185852 187 YARAAGDYNPIHLSAPSAKLFGFPRAIAHGLWNKARSLAALGERL--PASGYRVEVRFQKPVLLP 249
Cdd:PRK13693  30 YAGVSGDLNPIHWDDEIAKVVGLDTAIAHGMLTMGLGGGYVTSWVgdPGAVTEYNVRFTAVVPVP 94
HDE_HSD cd03448
HDE_HSD The R-hydratase-like hot dog fold of the 17-beta-hydroxysteriod dehydrogenase (HSD), ...
 189-246 1.73e-05

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: 43.36  E-value: 1.73e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489185852 189 RAAGDYNPIHLSAPSAKLFGFPRAIAHGL--WNKA--RSLAALGERLPASGYRVEVRFQKPV 246
Cdd:cd03448   22 RLSGDYNPLHIDPAFAKAAGFPRPILHGLctYGFAarAVLEAFADGDPARFKAIKVRFSSPV 83
PLN02864 PLN02864
enoyl-CoA hydratase
 189-217 9.66e-04

enoyl-CoA hydratase


Pssm-ID: 178455 [Multi-domain]  Cd Length: 310  Bit Score: 40.15  E-value: 9.66e-04
                         10        20
                 ....*....|....*....|....*....
gi 489185852 189 RAAGDYNPIHLSAPSAKLFGFPRAIAHGL 217
Cdd:PLN02864 205 RLSGDYNPLHSDPMFAKVAGFTRPILHGL 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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