PYRC_RHOBA
ID PYRC_RHOBA Reviewed; 456 AA.
AC Q7UNR2;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 99.
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 {ECO:0000250|UniProtKB:Q81WF0}; OrderedLocusNames=RB7430;
OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=243090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA Reinhardt R.;
RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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 -!- 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}.
CC -!- CAUTION: This protein does not encode the conserved residues that
CC usually bind zinc. {ECO:0000305}.
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DR EMBL; BX294146; CAD75356.1; -; Genomic_DNA.
DR RefSeq; NP_867809.1; NC_005027.1.
DR AlphaFoldDB; Q7UNR2; -.
DR SMR; Q7UNR2; -.
DR STRING; 243090.RB7430; -.
DR PRIDE; Q7UNR2; -.
DR EnsemblBacteria; CAD75356; CAD75356; RB7430.
DR KEGG; rba:RB7430; -.
DR PATRIC; fig|243090.15.peg.3584; -.
DR eggNOG; COG0044; Bacteria.
DR HOGENOM; CLU_015572_1_0_0; -.
DR InParanoid; Q7UNR2; -.
DR OMA; QHAQEPR; -.
DR OrthoDB; 1319925at2; -.
DR UniPathway; UPA00070; UER00117.
DR Proteomes; UP000001025; Chromosome.
DR GO; GO:0004151; F:dihydroorotase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01317; DHOase_IIa; 1.
DR Gene3D; 2.30.40.10; -; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR004722; DHOase.
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.
PE 3: Inferred from homology;
KW Hydrolase; Pyrimidine biosynthesis; Reference proteome.
FT CHAIN 1..456
FT /note="Putative dihydroorotase"
FT /id="PRO_0000147245"
SQ SEQUENCE 456 AA; 48514 MW; 5F1FD702B75BB95D CRC64;
MVVGQRERKR RCIRGEPLMN DTTWVLDGGR LIDPANGIDR IARLVLHEGK VHSIDTPDGD
VPPDAGRLDV TGKIVAPGLV DLATELREPG SEEDETIQTG SNAALAGGYT TVLCCSSTKP
LMDSAASVQL VRQIAQRVDG VRVLPIACLS KGRQAEQMAE LGILAAAGAA GFSDTPRPMP
NDALLKRALD YCRMFDLPIF DRPEVPELAD GGVMHDGQIG LILGLKGLPT EAEDLAVARD
VRLAEATKGR LHVGPVSTMG SIDMIGRVKS RGIHISASVC PHNLFGSDEL LRSYDSRYKV
HPPMRSPSHV EALRNAVAEG VIDAIESGHM PRAQEKKAND LDLAPFGASA LETTLAAIAT
DLVETKILPW SRAIECLSTA PARIAGVKGG TLSVGANADV TVIDPLNAWS VEAKEFRSRC
HSSPMTGRTL TARVTHTLVG GRLKFELHPT VASAAS
