PYRC_THEMA
ID PYRC_THEMA Reviewed; 376 AA.
AC Q9WYH0;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Putative dihydroorotase {ECO:0000250|UniProtKB:Q81WF0};
DE Short=DHOase {ECO:0000250|UniProtKB:Q81WF0};
DE EC=3.5.2.3 {ECO:0000250|UniProtKB:Q81WF0};
GN Name=pyrC; OrderedLocusNames=TM_0335;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
CC -!- FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate
CC to dihydroorotate. {ECO:0000250|UniProtKB:Q81WF0}.
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:0000250|UniProtKB:Q81WF0};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q81WF0};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q81WF0};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 3/3.
CC {ECO:0000250|UniProtKB:Q81WF0}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC DHOase family. Class I DHOase subfamily. {ECO:0000305}.
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DR EMBL; AE000512; AAD35422.1; -; Genomic_DNA.
DR PIR; A72391; A72391.
DR RefSeq; NP_228146.1; NC_000853.1.
DR RefSeq; WP_004083103.1; NC_000853.1.
DR AlphaFoldDB; Q9WYH0; -.
DR SMR; Q9WYH0; -.
DR STRING; 243274.THEMA_03045; -.
DR PRIDE; Q9WYH0; -.
DR EnsemblBacteria; AAD35422; AAD35422; TM_0335.
DR KEGG; tma:TM0335; -.
DR KEGG; tmw:THMA_0343; -.
DR PATRIC; fig|243274.18.peg.594; -.
DR eggNOG; COG0044; Bacteria.
DR InParanoid; Q9WYH0; -.
DR OMA; QHAQEPR; -.
DR OrthoDB; 1319925at2; -.
DR UniPathway; UPA00070; UER00117.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0004151; F:dihydroorotase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR002195; Dihydroorotase_CS.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR SUPFAM; SSF51338; SSF51338; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR PROSITE; PS00482; DIHYDROOROTASE_1; 1.
PE 3: Inferred from homology;
KW Hydrolase; Metal-binding; Pyrimidine biosynthesis; Reference proteome;
KW Zinc.
FT CHAIN 1..376
FT /note="Putative dihydroorotase"
FT /id="PRO_0000147264"
FT ACT_SITE 257
FT /evidence="ECO:0000250|UniProtKB:Q81WF0"
FT BINDING 35
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q81WF0"
FT BINDING 37..39
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q81WF0"
FT BINDING 37
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q81WF0"
FT BINDING 66
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q81WF0"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q81WF0"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q81WF0"
FT BINDING 138
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q81WF0"
FT BINDING 187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q81WF0"
FT BINDING 230
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q81WF0"
FT BINDING 257
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q81WF0"
FT BINDING 261
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q81WF0"
FT BINDING 273..274
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q81WF0"
SQ SEQUENCE 376 AA; 42633 MW; C65EDF6EE0A95A81 CRC64;
MRIYDPFRKK WIEEEIETPF PSKGLVATFP FVDLHVHVRL NGGEDYSSLE EASLVGGFFK
VVVQPNTKPL IDSKEVLERH LDLSKNRAVE FLFAVSPFGS IEAEGERVVG FSTDGIEYDY
PTLVETMKKK KKALWFDHSQ MYEVDGIFYE GAPLPFQKRP RSNEAIAIAR TVLTGLEYGF
ERFHIQHVTT KYSVEVISFL KNLAKVSCEV TPHHLFFCYE DIKNTNFKIN PPLGSPEDRR
ALIEAVKKDV IDVLATDHAP HHEKPDDFLT APYGSTSIEI AFPAYYTALG DLELVVKKLT
KKPLEVLGVE ARLTEDTLVF IDPEAEFIVD AKKFKSKGKN SMFDGVRLKG KVVALKLKGR
WVMIDGEVIA DQKEND
