(data stored in ACNUC10043 zone)

SWISSPROT: D1YUQ9_METPS

ID   D1YUQ9_METPS            Unreviewed;       444 AA.
AC   D1YUQ9;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   11-DEC-2019, entry version 64.
DE   RecName: Full=Dihydroorotase {ECO:0000256|HAMAP-Rule:MF_00220};
DE            Short=DHOase {ECO:0000256|HAMAP-Rule:MF_00220};
DE            EC=3.5.2.3 {ECO:0000256|HAMAP-Rule:MF_00220};
GN   Name=pyrC {ECO:0000256|HAMAP-Rule:MF_00220,
GN   ECO:0000313|EMBL:BAI60181.1};
GN   OrderedLocusNames=MCP_0109 {ECO:0000313|EMBL:BAI60181.1};
OS   Methanocella paludicola (strain DSM 17711 / JCM 13418 / NBRC 101707 /
OS   SANAE).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanocellales; Methanocellaceae; Methanocella.
OX   NCBI_TaxID=304371 {ECO:0000313|EMBL:BAI60181.1, ECO:0000313|Proteomes:UP000001882};
RN   [1] {ECO:0000313|Proteomes:UP000001882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17711 / JCM 13418 / NBRC 101707 / SANAE
RC   {ECO:0000313|Proteomes:UP000001882};
RX   PubMed=21829548; DOI=10.1371/journal.pone.0022898;
RA   Sakai S., Takaki Y., Shimamura S., Sekine M., Tajima T., Kosugi H.,
RA   Ichikawa N., Tasumi E., Hiraki A.T., Shimizu A., Kato Y., Nishiko R.,
RA   Mori K., Fujita N., Imachi H., Takai K.;
RT   "Genome sequence of a mesophilic hydrogenotrophic methanogen Methanocella
RT   paludicola, the first cultivated representative of the order
RT   Methanocellales.";
RL   PLoS ONE 6:E22898-E22898(2011).
CC   -!- FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate
CC       to dihydroorotate. {ECO:0000256|HAMAP-Rule:MF_00220}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate;
CC         Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00220};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00220};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00220};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       (S)-dihydroorotate from bicarbonate: step 3/3. {ECO:0000256|HAMAP-
CC       Rule:MF_00220}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       DHOase family. Class I DHOase subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_00220}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00220}.
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DR   EMBL; AP011532; BAI60181.1; -; Genomic_DNA.
DR   STRING; 304371.MCP_0109; -.
DR   EnsemblBacteria; BAI60181; BAI60181; MCP_0109.
DR   KEGG; mpd:MCP_0109; -.
DR   PATRIC; fig|304371.9.peg.115; -.
DR   eggNOG; arCOG00689; Archaea.
DR   eggNOG; COG0044; LUCA.
DR   HOGENOM; HOG000219143; -.
DR   KO; K01465; -.
DR   OMA; QHAQEPR; -.
DR   UniPathway; UPA00070; UER00117.
DR   Proteomes; UP000001882; Chromosome.
DR   GO; GO:0004151; F:dihydroorotase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.30.40.10; -; 1.
DR   HAMAP; MF_00220_A; PyrC_classI_A; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR004722; DHOase.
DR   InterPro; IPR002195; Dihydroorotase_CS.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51338; SSF51338; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   PROSITE; PS00483; DIHYDROOROTASE_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; D1YUQ9.
DR   SWISS-2DPAGE; D1YUQ9.
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00220};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00220};
KW   Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00220};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001882};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00220}.
FT   DOMAIN          48..380
FT                   /note="Amidohydro-rel"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
FT   REGION          59..61
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
FT   ACT_SITE        299
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
FT   METAL           57
FT                   /note="Zinc 1; via tele nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
FT   METAL           59
FT                   /note="Zinc 1; via tele nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
FT   METAL           143
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
FT   METAL           143
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
FT   METAL           177
FT                   /note="Zinc 2; via pros nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
FT   METAL           231
FT                   /note="Zinc 2; via tele nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
FT   METAL           299
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
FT   BINDING         91
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
FT   BINDING         303
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
SQ   SEQUENCE   444 AA;  48920 MW;  E0F61AA19449A02D CRC64;
     MHELVVENAR VPFGEDIVTC SIGIDEGRIA RIAKILKGEQ AYDARNMLVL PGVIDSHVHF
     RDMGQEEKED WLSGSRAAIY GGVTAVVDMP NTDPPTFDEE SFKIKLTVAQ NRSMIDFAIN
     GGVSGNLKAL PVLWRRGALA FGEIFMAKST GGFSVDEQAL KAALLEIKRL GATASIHAED
     EALNAEKARE LARDDSPDVY SQMRPPGSEL NAVKAAVRLE HETGAAMHIT HISTAKAVEA
     LRGEPITCDV TPHHLLLNMR HWEKLKSYGK MNPPLRPLRD VEALWKAARD GSIDVLASDH
     APHTREEKAA DIRSAPSGVP GVETMAPLIL KEVADGRLPL QRFIDMTTAN PARIFGINNK
     GRIEEGYDAD LIFVDMGARR VIRPYELHSK AGWTPYEGME AIFPHAVMQR GTLLLDGKEF
     LGRRGRGKFI RGRGYERKLP GRTS
//

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