(data stored in ACNUC7421 zone)

SWISSPROT: PYRC_SINFN

ID   PYRC_SINFN              Reviewed;         345 AA.
AC   C3MF80;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   05-JUL-2017, entry version 47.
DE   RecName: Full=Dihydroorotase {ECO:0000255|HAMAP-Rule:MF_00219};
DE            Short=DHOase {ECO:0000255|HAMAP-Rule:MF_00219};
DE            EC=3.5.2.3 {ECO:0000255|HAMAP-Rule:MF_00219};
GN   Name=pyrC {ECO:0000255|HAMAP-Rule:MF_00219};
GN   OrderedLocusNames=NGR_c01140;
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
CC   -!- FUNCTION: Catalyzes the reversible cyclization of carbamoyl
CC       aspartate to dihydroorotate. {ECO:0000255|HAMAP-Rule:MF_00219}.
CC   -!- CATALYTIC ACTIVITY: (S)-dihydroorotate + H(2)O = N-carbamoyl-L-
CC       aspartate. {ECO:0000255|HAMAP-Rule:MF_00219}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00219};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00219};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; (S)-dihydroorotate from bicarbonate: step 3/3.
CC       {ECO:0000255|HAMAP-Rule:MF_00219}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00219}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases
CC       superfamily. DHOase family. Class II DHOase subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00219}.
DR   EMBL; CP001389; ACP23917.1; -; Genomic_DNA.
DR   RefSeq; WP_012706702.1; NC_012587.1.
DR   RefSeq; YP_002824670.1; NC_012587.1.
DR   ProteinModelPortal; C3MF80; -.
DR   SMR; C3MF80; -.
DR   STRING; 394.NGR_c01140; -.
DR   EnsemblBacteria; ACP23917; ACP23917; NGR_c01140.
DR   GeneID; 7790693; -.
DR   KEGG; rhi:NGR_c01140; -.
DR   PATRIC; fig|394.7.peg.2912; -.
DR   eggNOG; ENOG4105EKE; Bacteria.
DR   eggNOG; COG0418; LUCA.
DR   HOGENOM; HOG000256259; -.
DR   KO; K01465; -.
DR   OMA; HLRDGAM; -.
DR   OrthoDB; POG091H06EN; -.
DR   UniPathway; UPA00070; UER00117.
DR   Proteomes; UP000001054; 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   GO; GO:0019856; P:pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR   CDD; cd01294; DHOase; 1.
DR   HAMAP; MF_00219; PyrC_classII; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR004721; DHOdimr.
DR   InterPro; IPR002195; Dihydroorotase_CS.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   PANTHER; PTHR43137:SF1; PTHR43137:SF1; 1.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   PIRSF; PIRSF001237; DHOdimr; 1.
DR   SFLD; SFLDF00074; dihydroorotase3; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   TIGRFAMs; TIGR00856; pyrC_dimer; 1.
DR   PROSITE; PS00482; DIHYDROOROTASE_1; 1.
DR   PROSITE; PS00483; DIHYDROOROTASE_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; C3MF80.
DR   SWISS-2DPAGE; C3MF80.
KW   Complete proteome; Hydrolase; Metal-binding; Pyrimidine biosynthesis;
KW   Reference proteome; Zinc.
FT   CHAIN         1    345       Dihydroorotase.
FT                                /FTId=PRO_1000193080.
FT   REGION       15     17       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00219}.
FT   ACT_SITE    247    247       {ECO:0000255|HAMAP-Rule:MF_00219}.
FT   METAL        13     13       Zinc 1; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00219}.
FT   METAL        15     15       Zinc 1; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00219}.
FT   METAL        99     99       Zinc 1; via carbamate group.
FT                                {ECO:0000255|HAMAP-Rule:MF_00219}.
FT   METAL        99     99       Zinc 2; via carbamate group.
FT                                {ECO:0000255|HAMAP-Rule:MF_00219}.
FT   METAL       136    136       Zinc 2; via pros nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00219}.
FT   METAL       174    174       Zinc 2; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00219}.
FT   METAL       247    247       Zinc 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_00219}.
FT   BINDING      41     41       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00219}.
FT   BINDING     136    136       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00219}.
FT   BINDING     219    219       Substrate; via amide nitrogen and
FT                                carbonyl oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00219}.
FT   BINDING     251    251       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00219}.
FT   BINDING     263    263       Substrate; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00219}.
FT   MOD_RES      99     99       N6-carboxylysine. {ECO:0000255|HAMAP-
FT                                Rule:MF_00219}.
SQ   SEQUENCE   345 AA;  37852 MW;  F0930CD1C0B57DCD CRC64;
     MQELVIRRPD DWHLHLRDGG VLRGVIGDTS RHFARAIVMP NLVPPVVTSA DAAAYRQRIL
     AAIPAGDRFE PLMTLYLTEG TDPDDVEAGY GSGLVKAVKL YPAGATTNSH SGVRDIAKAM
     PVLERMAEIG MPLCVHGEVT TPEVDIFDRE AVFIETVLDP LRRRLPDLRI TMEHVTTKDG
     VDYIKEHAGN LAGSITTHHL IINRNAILVG GIKPHYYCLP VAKRERHRQA LRAAAVSGDV
     RFFLGTDSAP HVDPLKECAC GCAGIYTSVN TMSCLAHVFE EEGALDRLEA FTSLNGPAWY
     GLPANEETIT LRKANEPVRY PAKIETEAGL ITVFDPLFPL YWAVA
//

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