GenomeNet

Database: UniProt
Entry: A0L0B8
LinkDB: A0L0B8
Original site: A0L0B8 
ID   PYRC_SHESA              Reviewed;         343 AA.
AC   A0L0B8;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 2.
DT   25-OCT-2017, entry version 65.
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=Shewana3_3263;
OS   Shewanella sp. (strain ANA-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=94122;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANA-3;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Newman D., Salticov C., Konstantinidis K., Klappenback J.,
RA   Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Shewanella sp. ANA-3.";
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABK49487.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; CP000469; ABK49487.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_023269013.1; NC_008577.1.
DR   ProteinModelPortal; A0L0B8; -.
DR   SMR; A0L0B8; -.
DR   STRING; 94122.Shewana3_3263; -.
DR   EnsemblBacteria; ABK49487; ABK49487; Shewana3_3263.
DR   KEGG; shn:Shewana3_3263; -.
DR   eggNOG; ENOG4105EKE; Bacteria.
DR   eggNOG; COG0418; LUCA.
DR   HOGENOM; HOG000256259; -.
DR   KO; K01465; -.
DR   OrthoDB; POG091H06EN; -.
DR   UniPathway; UPA00070; UER00117.
DR   Proteomes; UP000002589; 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   Zinc.
FT   CHAIN         1    343       Dihydroorotase.
FT                                /FTId=PRO_0000325576.
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   343 AA;  37816 MW;  970480BEDB230585 CRC64;
     MTTLTITRPD DWHIHLRDGA QLKDTVRDIS RYMGRAIVMP NLVPPAIDTE TALAYYDRIK
     AQVPAGSQFE PLMVLYLTDK TSPEEIRKAK ASGKIVAAKL YPAGATTNSD SGVTDLKNIY
     PALEAMQEVG MLFLVHGEVT DSSIDIFDRE RVFIENILSK IVADFPKLKI VLEHITTKDA
     VDFVTQASDN VAATITAHHL LYNRNHMLAG GIRPHFYCLP ILKRNTHQQA LLGAAASGNK
     KFFLGTDSAP HAKDRKEAAC GCAGSYTAHA AIELYAEAFE SVNALDKLEA FASFNGPDFY
     NLPRNSDTIT LVKKSWDVPV SYPLGDNNVV PIRAGEQIDW QVE
//
DBGET integrated database retrieval system