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Conserved domains on  [gi|489496389|ref|WP_003401305|]
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MULTISPECIES: 3-hydroxyacyl-thioester dehydratase HtdX [Mycobacterium]

Protein Classification

MaoC family dehydratase( domain architecture ID 11973529)

MaoC family dehydratase similar to Arabidopsis thaliana peroxisomal enoyl-CoA hydratase 2, which catalyzes a hydration step in peroxisomal beta-oxidation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MaoC_dehydratas pfam01575
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ...
 176-276 5.19e-26

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: 98.95  E-value: 5.19e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489496389  176 ITPAKIRRYAAVGGDHNPIHTNPIAAKLFGFPTVIAHGMFTAAAVLANIEARFPD-----AVRYSVRFAKPVLLPATAGL 250
Cdd:pfam01575  18 VTEADIALFALVSGDHNPIHVDPEFAKKAGFGGPIAHGMLTLAIVAGLVEEWGGDnviarFGEIKVRFTKPVFPGDTLRT 97

                          90       100
                  ....*....|....*....|....*.
gi 489496389  251 YVAEGDGGWDLTLRNMAKGYPHLTAT 276
Cdd:pfam01575  98 EAEVVGKRDGRQTKVVEVTVEVTEVA 123
PLN02864 super family cl28571
enoyl-CoA hydratase
 65-238 4.63e-04

enoyl-CoA hydratase


The actual alignment was detected with superfamily member PLN02864:

Pssm-ID: 178455 [Multi-domain]  Cd Length: 310  Bit Score: 40.92  E-value: 4.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489496389  65 FALTFPSVMSLVTGFDFP---FAAMGAIHTENHITQYRPIAVTDAVGVRVRAENLREHRRGLLVDLVT---NVSVGNDVA 138
Cdd:PLN02864  68 FASLFNLGSLDGFGLDLPglnYDPSLLLHGQQYIEIYKPIPSSASVRNKVSIAGLHDKGKAAILELETlsyEKDSGELLC 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489496389 139 WHQVTTFLH--------QQRTSLSGEPKPPPQKKPKLPPPAAVL---RITPAKIRRYAaVGGDHNPIHTNPIAAKLFGFP 207
Cdd:PLN02864 148 MNRSTIFLRgaggfsnsSQPFSYSNYPTNQVSAVKIPKSQPDAVfedQTQPSQALLYR-LSGDYNPLHSDPMFAKVAGFT 226

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 489496389 208 TVIAHGM----FTAAAVLANIEARFPDAVR-YSVRF 238
Cdd:PLN02864 227 RPILHGLctlgFAVRAVIKCFCNGDPTAVKtISGRF 262
 
Name Accession Description Interval E-value
MaoC_dehydratas pfam01575
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ...
 176-276 5.19e-26

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: 98.95  E-value: 5.19e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489496389  176 ITPAKIRRYAAVGGDHNPIHTNPIAAKLFGFPTVIAHGMFTAAAVLANIEARFPD-----AVRYSVRFAKPVLLPATAGL 250
Cdd:pfam01575  18 VTEADIALFALVSGDHNPIHVDPEFAKKAGFGGPIAHGMLTLAIVAGLVEEWGGDnviarFGEIKVRFTKPVFPGDTLRT 97

                          90       100
                  ....*....|....*....|....*.
gi 489496389  251 YVAEGDGGWDLTLRNMAKGYPHLTAT 276
Cdd:pfam01575  98 EAEVVGKRDGRQTKVVEVTVEVTEVA 123
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
176-280 1.35e-18

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 79.93  E-value: 1.35e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489496389 176 ITPAKIRRYAAVGGDHNPIHTNPIAAKLFGFPTVIAHGMFTAAAVLANIEARFPDAV-----RYSVRFAKPVLLPAT--- 247
Cdd:COG2030   18 VTEEDIVLFAGATGDPNPIHLDEEAAAATGFGGRIAHGMLTLSLASGLLVDDLPGTAvanlgLQEVRFLRPVRVGDTlra 97

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 489496389 248 ----AGLYVAEGDGG--WDLTLRNmAKGYPHLTATVRGL 280
Cdd:COG2030   98 rvevLEKRESKSRGIvtLRTTVTN-QDGEVVLTGEATVL 135
SAV4209_like cd03453
SAV4209_like. Similar in sequence to the Streptomyces avermitilis SAV4209 protein, with a hot ...
 176-257 2.06e-18

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: 78.90  E-value: 2.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489496389 176 ITPAKIRRYAAVGGDHNPIHTNPIAAKLFGFPTVIAHGMFTAAAV--LANIEARFPDAVR-YSVRFAKPVLLPATAGLYV 252
Cdd:cd03453   12 VSRADLVRYAGASGDFNPIHYDEDFAKKVGLPGVIAHGMLTMGLLgrLVTDWVGDPGRVVsFGVRFTKPVPVPDTLTCTG 91


                 ....*
gi 489496389 253 AEGDG 257
Cdd:cd03453   92 IVVEK 96
fused_HadA_HadB NF040620
fused (3R)-hydroxyacyl-ACP dehydratase subunits HadA/HadB;
184-249 5.02e-13

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


Pssm-ID: 468592 [Multi-domain]  Cd Length: 329  Bit Score: 67.94  E-value: 5.02e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489496389 184 YAAVGGDHNPIHTNPIAAKLFGFPTVIAHGMFT---AAAVLANIeARFPDAV-RYSVRFAKPVLLPATAG 249
Cdd:NF040620 220 YAGVSGDPNPIHWSDEVARLAGLPTVVAHGMLTmglGAGYLTSW-LGDPGAVtKYSVRFTSPVYVPADAP 288
PRK13693 PRK13693
(3R)-hydroxyacyl-ACP dehydratase subunit HadB; Provisional
 173-246 1.84e-09

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


Pssm-ID: 184249 [Multi-domain]  Cd Length: 142  Bit Score: 54.84  E-value: 1.84e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489496389 173 VLRITPAKIRRYAAVGGDHNPIHTNPIAAKLFGFPTVIAHGMFTAAAVLANIEARF--PDAVR-YSVRFAKPVLLPA 246
Cdd:PRK13693  19 TYPLTRQDLVNYAGVSGDLNPIHWDDEIAKVVGLDTAIAHGMLTMGLGGGYVTSWVgdPGAVTeYNVRFTAVVPVPN 95
PLN02864 PLN02864
enoyl-CoA hydratase
 65-238 4.63e-04

enoyl-CoA hydratase


Pssm-ID: 178455 [Multi-domain]  Cd Length: 310  Bit Score: 40.92  E-value: 4.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489496389  65 FALTFPSVMSLVTGFDFP---FAAMGAIHTENHITQYRPIAVTDAVGVRVRAENLREHRRGLLVDLVT---NVSVGNDVA 138
Cdd:PLN02864  68 FASLFNLGSLDGFGLDLPglnYDPSLLLHGQQYIEIYKPIPSSASVRNKVSIAGLHDKGKAAILELETlsyEKDSGELLC 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489496389 139 WHQVTTFLH--------QQRTSLSGEPKPPPQKKPKLPPPAAVL---RITPAKIRRYAaVGGDHNPIHTNPIAAKLFGFP 207
Cdd:PLN02864 148 MNRSTIFLRgaggfsnsSQPFSYSNYPTNQVSAVKIPKSQPDAVfedQTQPSQALLYR-LSGDYNPLHSDPMFAKVAGFT 226

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 489496389 208 TVIAHGM----FTAAAVLANIEARFPDAVR-YSVRF 238
Cdd:PLN02864 227 RPILHGLctlgFAVRAVIKCFCNGDPTAVKtISGRF 262
 
Name Accession Description Interval E-value
MaoC_dehydratas pfam01575
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ...
 176-276 5.19e-26

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: 98.95  E-value: 5.19e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489496389  176 ITPAKIRRYAAVGGDHNPIHTNPIAAKLFGFPTVIAHGMFTAAAVLANIEARFPD-----AVRYSVRFAKPVLLPATAGL 250
Cdd:pfam01575  18 VTEADIALFALVSGDHNPIHVDPEFAKKAGFGGPIAHGMLTLAIVAGLVEEWGGDnviarFGEIKVRFTKPVFPGDTLRT 97

                          90       100
                  ....*....|....*....|....*.
gi 489496389  251 YVAEGDGGWDLTLRNMAKGYPHLTAT 276
Cdd:pfam01575  98 EAEVVGKRDGRQTKVVEVTVEVTEVA 123
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
176-280 1.35e-18

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 79.93  E-value: 1.35e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489496389 176 ITPAKIRRYAAVGGDHNPIHTNPIAAKLFGFPTVIAHGMFTAAAVLANIEARFPDAV-----RYSVRFAKPVLLPAT--- 247
Cdd:COG2030   18 VTEEDIVLFAGATGDPNPIHLDEEAAAATGFGGRIAHGMLTLSLASGLLVDDLPGTAvanlgLQEVRFLRPVRVGDTlra 97

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 489496389 248 ----AGLYVAEGDGG--WDLTLRNmAKGYPHLTATVRGL 280
Cdd:COG2030   98 rvevLEKRESKSRGIvtLRTTVTN-QDGEVVLTGEATVL 135
SAV4209_like cd03453
SAV4209_like. Similar in sequence to the Streptomyces avermitilis SAV4209 protein, with a hot ...
 176-257 2.06e-18

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: 78.90  E-value: 2.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489496389 176 ITPAKIRRYAAVGGDHNPIHTNPIAAKLFGFPTVIAHGMFTAAAV--LANIEARFPDAVR-YSVRFAKPVLLPATAGLYV 252
Cdd:cd03453   12 VSRADLVRYAGASGDFNPIHYDEDFAKKVGLPGVIAHGMLTMGLLgrLVTDWVGDPGRVVsFGVRFTKPVPVPDTLTCTG 91


                 ....*
gi 489496389 253 AEGDG 257
Cdd:cd03453   92 IVVEK 96
R_hydratase_like cd03441
(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl ...
 176-247 1.49e-15

(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: 71.53  E-value: 1.49e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489496389 176 ITPAKIRRYAAVGGDHNPIHTNPIAAKLFGFPTVIAHGMFTAAAVLANIEARFPDAVR-----YSVRFAKPVLLPAT 247
Cdd:cd03441   10 VTEADIALFARLSGDPNPIHVDPEYAKAAGFGGRIAHGMLTLSLASGLLVQWLPGTDGanlgsQSVRFLAPVFPGDT 86
FAS_MaoC cd03447
FAS_MaoC, the MaoC-like hot dog fold of the fatty acid synthase, beta subunit. Other enzymes ...
 177-244 1.99e-14

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: 68.46  E-value: 1.99e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489496389 177 TPAKIRRYAAVGGDHNPIHTNPIAAKLFGFPTVIAHGMFTAAAVLANIEARFPDAVRYSVR-----FAKPVLL 244
Cdd:cd03447   11 APASNEPYARVSGDFNPIHVSRVFASYAGLPGTITHGMYTSAAVRALVETWAADNDRSRVRsftasFVGMVLP 83
R_hydratase cd03449
(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA ...
 175-242 3.94e-13

(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: 64.87  E-value: 3.94e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489496389 175 RITPAKIRRYAAVGGDHNPIHTNPIAAKLFGFPTVIAHGMFTAA---AVLANieaRFPD----AVRYSVRFAKPV 242
Cdd:cd03449   12 TITEEDVELFAELSGDFNPIHLDEEYAKKTRFGGRIAHGMLTASlisAVLGT---LLPGpgtiYLSQSLRFLRPV 83
fused_HadA_HadB NF040620
fused (3R)-hydroxyacyl-ACP dehydratase subunits HadA/HadB;
184-249 5.02e-13

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


Pssm-ID: 468592 [Multi-domain]  Cd Length: 329  Bit Score: 67.94  E-value: 5.02e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489496389 184 YAAVGGDHNPIHTNPIAAKLFGFPTVIAHGMFT---AAAVLANIeARFPDAV-RYSVRFAKPVLLPATAG 249
Cdd:NF040620 220 YAGVSGDPNPIHWSDEVARLAGLPTVVAHGMLTmglGAGYLTSW-LGDPGAVtKYSVRFTSPVYVPADAP 288
PRK13693 PRK13693
(3R)-hydroxyacyl-ACP dehydratase subunit HadB; Provisional
 173-246 1.84e-09

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


Pssm-ID: 184249 [Multi-domain]  Cd Length: 142  Bit Score: 54.84  E-value: 1.84e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489496389 173 VLRITPAKIRRYAAVGGDHNPIHTNPIAAKLFGFPTVIAHGMFTAAAVLANIEARF--PDAVR-YSVRFAKPVLLPA 246
Cdd:PRK13693  19 TYPLTRQDLVNYAGVSGDLNPIHWDDEIAKVVGLDTAIAHGMLTMGLGGGYVTSWVgdPGAVTeYNVRFTAVVPVPN 95
HDE_HSD cd03448
HDE_HSD The R-hydratase-like hot dog fold of the 17-beta-hydroxysteriod dehydrogenase (HSD), ...
 189-242 1.52e-08

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: 51.84  E-value: 1.52e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489496389 189 GDHNPIHTNPIAAKLFGFPTVIAHGM----FTAAAVLANIEARFPDAVR-YSVRFAKPV 242
Cdd:cd03448   25 GDYNPLHIDPAFAKAAGFPRPILHGLctygFAARAVLEAFADGDPARFKaIKVRFSSPV 83
PRK08190 PRK08190
bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated
 171-244 5.25e-07

bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated


Pssm-ID: 236180 [Multi-domain]  Cd Length: 466  Bit Score: 50.26  E-value: 5.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489496389 171 AAVLRI-TPAKIRRYAAVGGDHNPIHTNPIAAKLFGFPTVIAHGMFTAA---AVLANieaRFPD-AVRY---SVRFAKPV 242
Cdd:PRK08190  20 ASLVRTlTPDDIELFAAMSGDVNPAHLDAAYAASDGFHHVVAHGMWGGAlisAVLGT---RLPGpGTIYlgqSLRFRRPV 96


                 ..
gi 489496389 243 LL 244
Cdd:PRK08190  97 RI 98
MaoC_like cd03446
MoaC_like Similar to the MaoC (monoamine oxidase C) dehydratase regulatory protein but ...
 176-244 3.72e-05

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: 42.68  E-value: 3.72e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489496389 176 ITPAKIRRYAAVGGDHNPIHTNPIAAKLFGFPTVIAHGMFTAAAVLANIEaRFPDAVRYSV--------RFAKPVLL 244
Cdd:cd03446   18 VTEADVVMFAGLSGDWNPIHTDAEYAKKTRFGERIAHGLLTLSIATGLLQ-RLGVFERTVVafygidnlRFLNPVFI 93
NodN cd03450
NodN (nodulation factor N) contains a single hot dog fold similar to those of the peroxisomal ...
 176-242 1.16e-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: 41.40  E-value: 1.16e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489496389 176 ITPAKIRRYAAVGGDHNPIHTNPIAAKLFGFPTVIAHGMFT--AAAVLANIEARFPD---AVRY---SVRFAKPV 242
Cdd:cd03450   24 VDQERIDQFADATGDHQWIHVDPERAAAEPFGGTIAHGFLTlsLLPALTPQLFRVEGvkmGVNYgldKVRFPAPV 98
PLN02864 PLN02864
enoyl-CoA hydratase
 65-238 4.63e-04

enoyl-CoA hydratase


Pssm-ID: 178455 [Multi-domain]  Cd Length: 310  Bit Score: 40.92  E-value: 4.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489496389  65 FALTFPSVMSLVTGFDFP---FAAMGAIHTENHITQYRPIAVTDAVGVRVRAENLREHRRGLLVDLVT---NVSVGNDVA 138
Cdd:PLN02864  68 FASLFNLGSLDGFGLDLPglnYDPSLLLHGQQYIEIYKPIPSSASVRNKVSIAGLHDKGKAAILELETlsyEKDSGELLC 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489496389 139 WHQVTTFLH--------QQRTSLSGEPKPPPQKKPKLPPPAAVL---RITPAKIRRYAaVGGDHNPIHTNPIAAKLFGFP 207
Cdd:PLN02864 148 MNRSTIFLRgaggfsnsSQPFSYSNYPTNQVSAVKIPKSQPDAVfedQTQPSQALLYR-LSGDYNPLHSDPMFAKVAGFT 226

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 489496389 208 TVIAHGM----FTAAAVLANIEARFPDAVR-YSVRF 238
Cdd:PLN02864 227 RPILHGLctlgFAVRAVIKCFCNGDPTAVKtISGRF 262
MaoC_C cd03452
MaoC_C The C-terminal hot dog fold of the MaoC (monoamine oxidase C) dehydratase regulatory ...
 175-242 1.32e-03

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: 38.15  E-value: 1.32e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489496389 175 RITPAKIRRYAAVGGDHNPIHTNPIAAKLFGFPTVIAHGMF--TAAAVLANIEARFPDAVRY---SVRFAKPV 242
Cdd:cd03452   17 TVTEADIVNFACLTGDHFYAHMDEIAAKASFFGKRVAHGYFvlSAAAGLFVDPAPGPVLANYgleNLRFLEPV 89
SAV4209 cd03455
SAV4209 is a Streptomyces avermitilis protein with a hot dog fold that is similar to those of ...
 173-221 4.92e-03

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: 36.14  E-value: 4.92e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 489496389 173 VLRITPAKIRRYAAVGGDHNPIHTNPIAAKLFGFPTVIAHGMFTAAAVL 221
Cdd:cd03455    8 SIPPDPTLLFRYSAATRDFHRIHHDRDYARAVGYPDLYVNGPTLAGLVI 56
 
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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