NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1215506077|gb|ASK88874|]
View 

mesaconyl-CoA hydratase [Sphingorhabdus sp. SMR4y]

Protein Classification

MaoC family dehydratase( domain architecture ID 10130985)

MaoC family dehydratase similar to Rhodobacter sphaeroides mesaconyl-CoA hydratase, also called 2-methylfumaryl-CoA hydratase, which catalyzes the reversible hydration of mesaconyl-CoA to form beta-methylmalyl-CoA in the ethylmalonyl-CoA pathway for acetate assimilation

CATH:  3.10.129.10
Gene Ontology:  GO:0016829
PubMed:  15307895

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
FkbR2 cd03451
FkbR2 is a Streptomyces hygroscopicus protein with a hot dog fold that belongs to a conserved ...
 18-163 8.79e-85

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: 245.58  E-value: 8.79e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215506077  18 GRYFEDFEVGHIYEHRPGRTITDTDNVHFTLLTMNTHPAHFDYEFAKNTEFKKPLVCSPLTVALMVGMSVSDTSQKAVAN 97
Cdd:cd03451     1 GLYFEDFTVGQVFEHAPGRTVTEADNVLFTLLTMNTAPLHFDAAYAAKTEFGRRLVNSLFTLSLALGLSVNDTSLTAVAN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1215506077  98 LGWDKIRLSHPLFPGDTLYAESEVLDKRESSSRPEQGIVTVKTIGKNQDGKIVCTFERTMLIWKRG 163
Cdd:cd03451    81 LGYDEVRFPAPVFHGDTLYAESEVLSKRESKSRPDAGIVTVRTVGYNQDGEPVLSFERTALVPKRG 146
 
Name Accession Description Interval E-value
FkbR2 cd03451
FkbR2 is a Streptomyces hygroscopicus protein with a hot dog fold that belongs to a conserved ...
 18-163 8.79e-85

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: 245.58  E-value: 8.79e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215506077  18 GRYFEDFEVGHIYEHRPGRTITDTDNVHFTLLTMNTHPAHFDYEFAKNTEFKKPLVCSPLTVALMVGMSVSDTSQKAVAN 97
Cdd:cd03451     1 GLYFEDFTVGQVFEHAPGRTVTEADNVLFTLLTMNTAPLHFDAAYAAKTEFGRRLVNSLFTLSLALGLSVNDTSLTAVAN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1215506077  98 LGWDKIRLSHPLFPGDTLYAESEVLDKRESSSRPEQGIVTVKTIGKNQDGKIVCTFERTMLIWKRG 163
Cdd:cd03451    81 LGYDEVRFPAPVFHGDTLYAESEVLSKRESKSRPDAGIVTVRTVGYNQDGEPVLSFERTALVPKRG 146
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
20-163 3.05e-52

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 163.13  E-value: 3.05e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215506077  20 YFEDFEVGHIYEHRPgRTITDTDNVHFTLLTMNTHPAHFDYEFAKNTEFKKPLVCSPLTVALMVGMSVSDTSQKAVANLG 99
Cdd:COG2030     1 YFEDLEVGDVLPHGG-RTVTEEDIVLFAGATGDPNPIHLDEEAAAATGFGGRIAHGMLTLSLASGLLVDDLPGTAVANLG 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1215506077 100 WDKIRLSHPLFPGDTLYAESEVLDKRESSSRpeqGIVTVKTIGKNQDGKIVCTFERTMLIWKRG 163
Cdd:COG2030    80 LQEVRFLRPVRVGDTLRARVEVLEKRESKSR---GIVTLRTTVTNQDGEVVLTGEATVLVPRRP 140
MaoC_dehydratas pfam01575
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ...
 30-144 5.98e-20

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: 80.08  E-value: 5.98e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215506077  30 YEHRPGRTITDTDNVHFTLLTMNTHPAHFDYEFAKNTEFKKPLVCSPLTVALMVGMSVSDTSQKAVANLGWDKIRLSHPL 109
Cdd:pfam01575  10 PDTEKPRTVTEADIALFALVSGDHNPIHVDPEFAKKAGFGGPIAHGMLTLAIVAGLVEEWGGDNVIARFGEIKVRFTKPV 89

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1215506077 110 FPGDTLYAESEVLDKRESSSRPEqGIVTVKTIGKN 144
Cdd:pfam01575  90 FPGDTLRTEAEVVGKRDGRQTKV-VEVTVEVTEVA 123
PRK08190 PRK08190
bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated
 19-152 1.14e-06

bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated


Pssm-ID: 236180 [Multi-domain]  Cd Length: 466  Bit Score: 47.18  E-value: 1.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215506077  19 RYFEDFEVGHIYEHRpgRTITDTDNVHFTLLTMNTHPAHFDYEFAKNTEFKKPLVCSPLTVALmvgmsVSdtsqkAVAN- 97
Cdd:PRK08190    9 RTFDEIAIGDSASLV--RTLTPDDIELFAAMSGDVNPAHLDAAYAASDGFHHVVAHGMWGGAL-----IS-----AVLGt 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1215506077  98 ---------LGWDkIRLSHPLFPGDTLYAESEVLDKResssrPEQGIVTVKTIGKNQDGKIVCT 152
Cdd:PRK08190   77 rlpgpgtiyLGQS-LRFRRPVRIGDTLTVTVTVREKD-----PEKRIVVLDCRCTNQDGEVVIT 134
 
Name Accession Description Interval E-value
FkbR2 cd03451
FkbR2 is a Streptomyces hygroscopicus protein with a hot dog fold that belongs to a conserved ...
 18-163 8.79e-85

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: 245.58  E-value: 8.79e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215506077  18 GRYFEDFEVGHIYEHRPGRTITDTDNVHFTLLTMNTHPAHFDYEFAKNTEFKKPLVCSPLTVALMVGMSVSDTSQKAVAN 97
Cdd:cd03451     1 GLYFEDFTVGQVFEHAPGRTVTEADNVLFTLLTMNTAPLHFDAAYAAKTEFGRRLVNSLFTLSLALGLSVNDTSLTAVAN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1215506077  98 LGWDKIRLSHPLFPGDTLYAESEVLDKRESSSRPEQGIVTVKTIGKNQDGKIVCTFERTMLIWKRG 163
Cdd:cd03451    81 LGYDEVRFPAPVFHGDTLYAESEVLSKRESKSRPDAGIVTVRTVGYNQDGEPVLSFERTALVPKRG 146
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
20-163 3.05e-52

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 163.13  E-value: 3.05e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215506077  20 YFEDFEVGHIYEHRPgRTITDTDNVHFTLLTMNTHPAHFDYEFAKNTEFKKPLVCSPLTVALMVGMSVSDTSQKAVANLG 99
Cdd:COG2030     1 YFEDLEVGDVLPHGG-RTVTEEDIVLFAGATGDPNPIHLDEEAAAATGFGGRIAHGMLTLSLASGLLVDDLPGTAVANLG 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1215506077 100 WDKIRLSHPLFPGDTLYAESEVLDKRESSSRpeqGIVTVKTIGKNQDGKIVCTFERTMLIWKRG 163
Cdd:COG2030    80 LQEVRFLRPVRVGDTLRARVEVLEKRESKSR---GIVTLRTTVTNQDGEVVLTGEATVLVPRRP 140
R_hydratase_like cd03441
(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl ...
 32-158 9.77e-41

(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: 133.54  E-value: 9.77e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215506077  32 HRPGRTITDTDNVHFTLLTMNTHPAHFDYEFAKNTEFKKPLVCSPLTVALMVGMSVSDTSQKAVANLGWDKIRLSHPLFP 111
Cdd:cd03441     4 DSSGRTVTEADIALFARLSGDPNPIHVDPEYAKAAGFGGRIAHGMLTLSLASGLLVQWLPGTDGANLGSQSVRFLAPVFP 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1215506077 112 GDTLYAESEVLDKRESSSRpeqGIVTVKTIGKNQDGKIVCTFERTML 158
Cdd:cd03441    84 GDTLRVEVEVLGKRPSKGR---GVVTVRTEARNQGGEVVLSGEATVL 127
MaoC_like cd03446
MoaC_like Similar to the MaoC (monoamine oxidase C) dehydratase regulatory protein but ...
 20-159 3.64e-32

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: 112.01  E-value: 3.64e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215506077  20 YFEDFEVGHIYEHRpGRTITDTDNVHFTLLTMNTHPAHFDYEFAKNTEFKKPLVCSPLTVALMVG--MSVSDTSQKAVAN 97
Cdd:cd03446     1 YFEDFEIGQVFESV-GRTVTEADVVMFAGLSGDWNPIHTDAEYAKKTRFGERIAHGLLTLSIATGllQRLGVFERTVVAF 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1215506077  98 LGWDKIRLSHPLFPGDTLYAESEVLDKREsSSRPEQGIVTVKTIGKNQDGKIVCTFERTMLI 159
Cdd:cd03446    80 YGIDNLRFLNPVFIGDTIRAEAEVVEKEE-KDGEDAGVVTRRIEVVNQRGEVVQSGEMSLLV 140
YdeM cd03454
YdeM is a Bacillus subtilis protein that belongs to a family of prokaryotic proteins of unkown ...
 21-159 3.19e-25

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: 94.17  E-value: 3.19e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215506077  21 FEDFEVGHIYEHRPgRTITDTDNVHFTlltmnTH----PAHFDYEFAKNTEFKKpLVCSPL-TVALMVGMSVsDTSQKAV 95
Cdd:cd03454     1 FEDLVIGQRFTSGS-YTVTEEEIIAFA-----REfdpqPFHLDEEAAKESLFGG-LAASGWhTAAITMRLLV-DAGLSGS 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1215506077  96 ANL---GWDKIRLSHPLFPGDTLYAESEVLDKRESSSRPEQGIVTVKTIGKNQDGKIVCTFERTMLI 159
Cdd:cd03454    73 ASGgspGIDELRWPRPVRPGDTLSVEVEVLDKRPSRSRPDRGIVTLRSETLNQRGEVVLTFEATVLV 139
MaoC_dehydratas pfam01575
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ...
 30-144 5.98e-20

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: 80.08  E-value: 5.98e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215506077  30 YEHRPGRTITDTDNVHFTLLTMNTHPAHFDYEFAKNTEFKKPLVCSPLTVALMVGMSVSDTSQKAVANLGWDKIRLSHPL 109
Cdd:pfam01575  10 PDTEKPRTVTEADIALFALVSGDHNPIHVDPEFAKKAGFGGPIAHGMLTLAIVAGLVEEWGGDNVIARFGEIKVRFTKPV 89

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1215506077 110 FPGDTLYAESEVLDKRESSSRPEqGIVTVKTIGKN 144
Cdd:pfam01575  90 FPGDTLRTEAEVVGKRDGRQTKV-VEVTVEVTEVA 123
MaoC_C cd03452
MaoC_C The C-terminal hot dog fold of the MaoC (monoamine oxidase C) dehydratase regulatory ...
 20-163 9.59e-15

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: 67.04  E-value: 9.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215506077  20 YFEDFEVG-HIYEHRpgRTITDTDNVHFTLLTMNTHPAHFDYEFAKNTEFKKPLVCSPLTVALMVGMSVSDTSQKAVANL 98
Cdd:cd03452     1 NLEQLRPGdSLLTHR--RTVTEADIVNFACLTGDHFYAHMDEIAAKASFFGKRVAHGYFVLSAAAGLFVDPAPGPVLANY 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1215506077  99 GWDKIRLSHPLFPGDTLYAESEVldKRES-SSRPEQGIVTVKTIGKNQDGKIVCTFERTMLIWKRG 163
Cdd:cd03452    79 GLENLRFLEPVYPGDTIQVRLTC--KRKIpRDGQDYGVVRWDAEVTNQNGELVASYDILTLVAKKG 142
R_hydratase cd03449
(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA ...
 36-159 2.19e-14

(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: 66.03  E-value: 2.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215506077  36 RTITDTDNVHFTLLTMNTHPAHFDYEFAKNTEFKKPLVCSPLTVALmvgmsVSdtsqKAVANL----GWdkIRLS----- 106
Cdd:cd03449    11 RTITEEDVELFAELSGDFNPIHLDEEYAKKTRFGGRIAHGMLTASL-----IS----AVLGTLlpgpGT--IYLSqslrf 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1215506077 107 -HPLFPGDTLYAESEVLDKresssRPEQGIVTVKTIGKNQDGKIVCTFERTMLI 159
Cdd:cd03449    80 lRPVFIGDTVTATVTVTEK-----REDKKRVTLETVCTNQNGEVVIEGEAVVLA 128
SAV4209 cd03455
SAV4209 is a Streptomyces avermitilis protein with a hot dog fold that is similar to those of ...
 31-154 1.64e-10

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: 55.40  E-value: 1.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215506077  31 EHRPGRTI--TDTDNVHFTLLTMNTHPAHFDYEFAKNTEFKKPLVCSPLTVALMVGMSVS----DTSQKAVAnlgwdkIR 104
Cdd:cd03455     2 DELPRLSIppDPTLLFRYSAATRDFHRIHHDRDYARAVGYPDLYVNGPTLAGLVIRYVTDwagpDARVKSFA------FR 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1215506077 105 LSHPLFPGDTLYAESEVLDKRESSsrpeqgIVTVKTIGKNQDGKIVCTFE 154
Cdd:cd03455    76 LGAPLYAGDTLRFGGRVTAKRDDE------VVTVELWARNSEGDHVMAGT 119
PRK08190 PRK08190
bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated
 19-152 1.14e-06

bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated


Pssm-ID: 236180 [Multi-domain]  Cd Length: 466  Bit Score: 47.18  E-value: 1.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215506077  19 RYFEDFEVGHIYEHRpgRTITDTDNVHFTLLTMNTHPAHFDYEFAKNTEFKKPLVCSPLTVALmvgmsVSdtsqkAVAN- 97
Cdd:PRK08190    9 RTFDEIAIGDSASLV--RTLTPDDIELFAAMSGDVNPAHLDAAYAASDGFHHVVAHGMWGGAL-----IS-----AVLGt 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1215506077  98 ---------LGWDkIRLSHPLFPGDTLYAESEVLDKResssrPEQGIVTVKTIGKNQDGKIVCT 152
Cdd:PRK08190   77 rlpgpgtiyLGQS-LRFRRPVRIGDTLTVTVTVREKD-----PEKRIVVLDCRCTNQDGEVVIT 134
MaoC_dehydrat_N pfam13452
N-terminal half of MaoC dehydratase; It is clear from the structures of bacterial members of ...
 52-153 4.08e-06

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: 43.84  E-value: 4.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215506077  52 NTHPAHFDYEFAKNTEFKKPLVcsPLTVALMVGMSVSDtsqkAVANLGWDKIRLSH---------PLFPGDTLYAESEVL 122
Cdd:pfam13452  28 ETNPAYWDEAAARAAGYGDLPA--PPTFLFVLGWDAPG----FMEQLGIDLSRLLHgeqrftyhrPLRAGDELTCRSQIA 101

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1215506077 123 DKRESSSRPEQGIVTVKTIGKNQDGKIVCTF 153
Cdd:pfam13452 102 DVYDKKGNGALCFVVVETEVTNQRGEPVATR 132
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 92-158 8.25e-06

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: 42.46  E-value: 8.25e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1215506077  92 QKAVANLGWDKIRLSHPLFPGDTLYAESEVLDKRESSsrpeqgiVTVKTIGKNQDGKIVCTFERTML 158
Cdd:cd03440    41 RGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSS-------VTVEVEVRNEDGKLVATATATFV 100
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH