GenomeNet

Database: UniProt
Entry: Q3K7J8
LinkDB: Q3K7J8
Original site: Q3K7J8 
ID   PYRC_PSEPF              Reviewed;         348 AA.
AC   Q3K7J8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   05-JUL-2017, entry version 79.
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=Pfl01_4519;
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1;
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(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; CP000094; ABA76256.1; -; Genomic_DNA.
DR   RefSeq; WP_011335738.1; NC_007492.2.
DR   ProteinModelPortal; Q3K7J8; -.
DR   SMR; Q3K7J8; -.
DR   STRING; 205922.Pfl01_4519; -.
DR   PRIDE; Q3K7J8; -.
DR   EnsemblBacteria; ABA76256; ABA76256; Pfl01_4519.
DR   KEGG; pfo:Pfl01_4519; -.
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; UP000002704; 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;
KW   Complete proteome; Hydrolase; Metal-binding; Pyrimidine biosynthesis;
KW   Zinc.
FT   CHAIN         1    348       Dihydroorotase.
FT                                /FTId=PRO_1000024038.
FT   REGION       16     18       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00219}.
FT   ACT_SITE    248    248       {ECO:0000255|HAMAP-Rule:MF_00219}.
FT   METAL        14     14       Zinc 1; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00219}.
FT   METAL        16     16       Zinc 1; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00219}.
FT   METAL       100    100       Zinc 1; via carbamate group.
FT                                {ECO:0000255|HAMAP-Rule:MF_00219}.
FT   METAL       100    100       Zinc 2; via carbamate group.
FT                                {ECO:0000255|HAMAP-Rule:MF_00219}.
FT   METAL       137    137       Zinc 2; via pros nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00219}.
FT   METAL       175    175       Zinc 2; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00219}.
FT   METAL       248    248       Zinc 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_00219}.
FT   BINDING      42     42       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00219}.
FT   BINDING     137    137       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00219}.
FT   BINDING     220    220       Substrate; via amide nitrogen and
FT                                carbonyl oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00219}.
FT   BINDING     252    252       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00219}.
FT   BINDING     264    264       Substrate; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00219}.
FT   MOD_RES     100    100       N6-carboxylysine. {ECO:0000255|HAMAP-
FT                                Rule:MF_00219}.
SQ   SEQUENCE   348 AA;  38480 MW;  AB078C90E2570A7E CRC64;
     MSDRLTLLRP DDWHIHLRDG AVLTNTVADV ARTFGRAIIM PNLVPPVRNA AEADGYRQRI
     LAARPAGSRF EPLMVLYLTD RTQPEEIREA KASGFVHAAK LYPAGATTNS DSGVTSIDKI
     FPVLEAMAEA GMPLLIHGEV TRGDVDVFDR EKIFIDEHMR RVVERFPTLK VVFEHITTGD
     AVQFVNEASA NVGATITAHH LLYNRNHMLV GGIRPHFYCL PILKRNTHQE ALLDAATSGS
     AKFFLGTDSA PHAQHAKEAA CGCAGCYTAY AAIELYAEAF EQRNALDKLE AFASLNGPRF
     YGLPANTDRI TLVRDEWTAP TSLPFGELTV IPLRAGEKLR WRLLEEHA
//
DBGET integrated database retrieval system