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Database: UniProt
Entry: Q5P6Y5
LinkDB: Q5P6Y5
Original site: Q5P6Y5 
ID   PYRC_AROAE              Reviewed;         344 AA.
AC   Q5P6Y5;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   25-OCT-2017, entry version 80.
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=AZOSEA08010; ORFNames=ebA1456;
OS   Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Aromatoleum.
OX   NCBI_TaxID=76114;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EbN1;
RX   PubMed=15551059; DOI=10.1007/s00203-004-0742-9;
RA   Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F.,
RA   Reinhardt R.;
RT   "The genome sequence of an anaerobic aromatic-degrading denitrifying
RT   bacterium, strain EbN1.";
RL   Arch. Microbiol. 183:27-36(2005).
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; CR555306; CAI06926.1; -; Genomic_DNA.
DR   RefSeq; WP_011236652.1; NC_006513.1.
DR   ProteinModelPortal; Q5P6Y5; -.
DR   SMR; Q5P6Y5; -.
DR   STRING; 76114.ebA1456; -.
DR   MEROPS; M38.A02; -.
DR   EnsemblBacteria; CAI06926; CAI06926; ebA1456.
DR   KEGG; eba:ebA1456; -.
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; UP000006552; 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; PTHR43137; 1.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   PIRSF; PIRSF001237; DHOdimr; 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   Reference proteome; Zinc.
FT   CHAIN         1    344       Dihydroorotase.
FT                                /FTId=PRO_0000325570.
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   344 AA;  37310 MW;  75E74BD36B3B7FC3 CRC64;
     MQTISLIRPD DWHLHVRDGA ALATVVPHTA RRFGRALIMP NLRPPVTTAA QALEYRARIL
     AAVPPGQHFE PLMSLYLTDN TSPDEIDRAK ASGAVVAVKL YPAGATTNSD AGVTAIEKVH
     AVLERMEKLG MVLCVHGEVT HGDVDVFDRE QVFIEQVLAP LVARFPALRV VFEHITTAEA
     ARFVQDAGPN VAATVTAHHL LLNRNAIFAG GIRPHHYCLP VLKRETHRRA LVEAATSGNA
     KFFLGTDSAP HSRAAKETAC GCAGCYTAHA AIELYAEAFE QAGALDRLEA FASLNGPAFY
     GLAPNAERIT LAKDAWEVPG EYEYLHDDPL VPLRAGETVA WRVL
//
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