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 01-MAY-2013, entry version 40.
DE RecName: Full=Dihydroorotase;
DE Short=DHOase;
DE EC=3.5.2.3;
GN Name=pyrC; 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 -!- CATALYTIC ACTIVITY: (S)-dihydroorotate + H(2)O = N-carbamoyl-L-
CC aspartate.
CC -!- COFACTOR: Binds 2 zinc ions per subunit (By similarity).
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC pathway; (S)-dihydroorotate from bicarbonate: step 3/3.
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SIMILARITY: Belongs to the DHOase family. Type 2 subfamily.
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DR EMBL; CP000813; ABV62132.1; -; Genomic_DNA.
DR RefSeq; YP_001486692.1; NC_009848.1.
DR ProteinModelPortal; A8FD15; -.
DR STRING; 315750.BPUM_1449; -.
DR MEROPS; M38.972; -.
DR EnsemblBacteria; ABV62132; ABV62132; BPUM_1449.
DR GeneID; 5620716; -.
DR KEGG; bpu:BPUM_1449; -.
DR PATRIC; 18966735; VBIBacPum16546_1464.
DR eggNOG; COG0044; -.
DR HOGENOM; HOG000219142; -.
DR KO; K01465; -.
DR OMA; GKNSPFI; -.
DR ProtClustDB; CLSK887279; -.
DR BioCyc; BPUM315750:GH6N-1538-MONOMER; -.
DR UniPathway; UPA00070; UER00117.
DR GO; GO:0004151; F:dihydroorotase activity; IEA:HAMAP.
DR GO; GO:0008270; F:zinc ion binding; IEA:HAMAP.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR HAMAP; MF_00220_B; PyrC_type2_B; 1; -.
DR InterPro; IPR006680; Amidohydro_1.
DR InterPro; IPR004722; DHOase.
DR InterPro; IPR002195; Dihydroorotase_CS.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; Metalo_hydrolase; 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 Zinc.
FT CHAIN 1 428 Dihydroorotase.
FT /FTId=PRO_1000058653.
FT METAL 59 59 Zinc 1 (By similarity).
FT METAL 61 61 Zinc 1 (By similarity).
FT METAL 141 141 Zinc 1; via carbamate group (By
FT similarity).
FT METAL 141 141 Zinc 2; via carbamate group (By
FT similarity).
FT METAL 178 178 Zinc 2 (By similarity).
FT METAL 231 231 Zinc 2 (By similarity).
FT METAL 304 304 Zinc 1 (By similarity).
FT MOD_RES 141 141 N6-carboxylysine (By similarity).
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
//
