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Database: UniProt
Entry: A8FD15
LinkDB: A8FD15
Original site: A8FD15 
ID   PYRC_BACP2              Reviewed;         428 AA.
AC   A8FD15;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   30-AUG-2017, entry version 66.
DE   RecName: Full=Dihydroorotase {ECO:0000255|HAMAP-Rule:MF_00220};
DE            Short=DHOase {ECO:0000255|HAMAP-Rule:MF_00220};
DE            EC=3.5.2.3 {ECO:0000255|HAMAP-Rule:MF_00220};
GN   Name=pyrC {ECO:0000255|HAMAP-Rule:MF_00220};
GN   OrderedLocusNames=BPUM_1449;
OS   Bacillus pumilus (strain SAFR-032).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=315750;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAFR-032;
RX   PubMed=17895969; DOI=10.1371/journal.pone.0000928;
RA   Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D.,
RA   Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C.,
RA   Dinh H., Lee S., Nazareth L., Blyth P., Holder M., Buhay C.,
RA   Tirumalai M.R., Liu Y., Dasgupta I., Bokhetache L., Fujita M.,
RA   Karouia F., Eswara Moorthy P., Siefert J., Uzman A., Buzumbo P.,
RA   Verma A., Zwiya H., McWilliams B.D., Olowu A., Clinkenbeard K.D.,
RA   Newcombe D., Golebiewski L., Petrosino J.F., Nicholson W.L., Fox G.E.,
RA   Venkateswaran K., Highlander S.K., Weinstock G.M.;
RT   "Paradoxical DNA repair and peroxide resistance gene conservation in
RT   Bacillus pumilus SAFR-032.";
RL   PLoS ONE 2:E928-E928(2007).
CC   -!- FUNCTION: Catalyzes the reversible cyclization of carbamoyl
CC       aspartate to dihydroorotate. {ECO:0000255|HAMAP-Rule:MF_00220}.
CC   -!- CATALYTIC ACTIVITY: (S)-dihydroorotate + H(2)O = N-carbamoyl-L-
CC       aspartate. {ECO:0000255|HAMAP-Rule:MF_00220}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00220};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00220};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; (S)-dihydroorotate from bicarbonate: step 3/3.
CC       {ECO:0000255|HAMAP-Rule:MF_00220}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases
CC       superfamily. DHOase family. Class I DHOase subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00220}.
DR   EMBL; CP000813; ABV62132.1; -; Genomic_DNA.
DR   RefSeq; WP_012009895.1; NC_009848.4.
DR   ProteinModelPortal; A8FD15; -.
DR   SMR; A8FD15; -.
DR   STRING; 315750.BPUM_1449; -.
DR   PRIDE; A8FD15; -.
DR   EnsemblBacteria; ABV62132; ABV62132; BPUM_1449.
DR   KEGG; bpu:BPUM_1449; -.
DR   eggNOG; ENOG4105CD3; Bacteria.
DR   eggNOG; COG0044; LUCA.
DR   HOGENOM; HOG000219142; -.
DR   KO; K01465; -.
DR   OMA; EYVKAFD; -.
DR   OrthoDB; POG091H02CH; -.
DR   UniPathway; UPA00070; UER00117.
DR   Proteomes; UP000001355; 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   CDD; cd01317; DHOase_IIa; 1.
DR   Gene3D; 2.30.40.10; -; 1.
DR   HAMAP; MF_00220_B; PyrC_classI_B; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR004722; DHOase.
DR   InterPro; IPR002195; Dihydroorotase_CS.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51338; SSF51338; 2.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   TIGRFAMs; TIGR00857; pyrC_multi; 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    428       Dihydroorotase.
FT                                /FTId=PRO_1000058653.
FT   REGION       61     63       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00220}.
FT   REGION      322    323       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00220}.
FT   ACT_SITE    304    304       {ECO:0000255|HAMAP-Rule:MF_00220}.
FT   METAL        59     59       Zinc 1; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00220}.
FT   METAL        61     61       Zinc 1; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00220}.
FT   METAL       151    151       Zinc 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_00220}.
FT   METAL       151    151       Zinc 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00220}.
FT   METAL       178    178       Zinc 2; via pros nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00220}.
FT   METAL       231    231       Zinc 2; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00220}.
FT   METAL       304    304       Zinc 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_00220}.
FT   BINDING      93     93       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00220}.
FT   BINDING     277    277       Substrate; via amide nitrogen and
FT                                carbonyl oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00220}.
FT   BINDING     308    308       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00220}.
SQ   SEQUENCE   428 AA;  46993 MW;  B50A9168280389E2 CRC64;
     MSYLIKNGFI LTSTGEKVQQ DIRVEGEVIQ AIGHLEREDG EEVIDAKGLF VSPGLIDLHV
     HLREPGGEKK ETIETGSKAA ARGGYTTIAA MPNTRPVPDT KEQMEWLMNR IEETSSVRVL
     PYASITTRQI GEEMTDFAAL KEAGAFAFTD DGVGIQTAGM MYEAMKKAAS LDQAIVAHCE
     DNSLIYGGCV HEGEFSKANG LNGIPSICES VHIARDVLLA EAANCHYHVC HISTKESVRV
     VRDAKKAGIR VTAEVSPHHL LLCDADIPGL DTNYKMNPPL RGKEDREALI EGLLDGTIDF
     IATDHAPHTE EEKNETMQRA PFGIVGLETA FPLLYTRFVK TGEWTLKELV DYMTIKPAEA
     FSLPYGKLEK GQIADITLID LNKEMAIDKK SFLSKGQNTP FDKLTVSGWP VMTLASGKVV
     YEEGRLVK
//
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