ID PYRC_STAAN Reviewed; 424 AA.
AC P65906; Q99UR7;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 01-MAY-2013, entry version 67.
DE RecName: Full=Dihydroorotase;
DE Short=DHOase;
DE EC=3.5.2.3;
GN Name=pyrC; OrderedLocusNames=SA1044;
OS Staphylococcus aureus (strain N315).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus.
OX NCBI_TaxID=158879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N315;
RX PubMed=11418146; DOI=10.1016/S0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I.,
RA Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K.,
RA Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M.,
RA Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M.,
RA Ogasawara N., Hayashi H., Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus
RT aureus.";
RL Lancet 357:1225-1240(2001).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RA Stenz L.;
RT "Shotgun proteomic analysis of total protein extract of S. aureus S30
RT versus N315.";
RL Submitted (NOV-2005) to UniProtKB.
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=N315;
RA Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.;
RT "Shotgun proteomic analysis of total and membrane protein extracts of
RT S. aureus strain N315.";
RL Submitted (OCT-2007) to UniProtKB.
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; BA000018; BAB42296.1; -; Genomic_DNA.
DR PIR; D89892; D89892.
DR RefSeq; NP_374317.1; NC_002745.2.
DR ProteinModelPortal; P65906; -.
DR SMR; P65906; 1-423.
DR STRING; 158879.SA1044; -.
DR PRIDE; P65906; -.
DR EnsemblBacteria; BAB42296; BAB42296; BAB42296.
DR GeneID; 1123875; -.
DR KEGG; sau:SA1044; -.
DR PATRIC; 19574306; VBIStaAur116463_1122.
DR eggNOG; COG0044; -.
DR HOGENOM; HOG000219142; -.
DR KO; K01465; -.
DR OMA; GINTPFT; -.
DR ProtClustDB; PRK09357; -.
DR BioCyc; SAUR158879:GJCB-1104-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 1: Evidence at protein level;
KW Complete proteome; Hydrolase; Metal-binding; Pyrimidine biosynthesis;
KW Zinc.
FT CHAIN 1 424 Dihydroorotase.
FT /FTId=PRO_0000147248.
FT METAL 58 58 Zinc 1 (By similarity).
FT METAL 60 60 Zinc 1 (By similarity).
FT METAL 177 177 Zinc 2 (By similarity).
FT METAL 230 230 Zinc 2 (By similarity).
FT METAL 303 303 Zinc 1 (By similarity).
SQ SEQUENCE 424 AA; 46372 MW; 8EC9B615ED8FFAB2 CRC64;
MKLIKNGKVL QNGELQQADI LIDGKVIKQI APAIEPSNGV DIIDAKGHFV SPGFVDVHVH
LREPGGEYKE TIETGTKAAA RGGFTTVCPM PNTRPVPDSV EHFEALQKLI DDNAQVRVLP
YASITTRQLG KELVDFPALV KEGAFAFTDD GVGVQTASMM YEGMIEAAKV NKAIVAHCED
NSLIYGGAMH EGKRSKELGI PGIPNICESV QIARDVLLAE AAGCHYHVCH VSTKESVRVI
RDAKRAGIHV TAEVTPHHLL LTEDDIPGNN AIYKMNPPLR STEDREALLE GLLDGTIDCI
ATDHAPHARD EKAQPMEKAP FGIVGSETAF PLLYTHFVKN GDWTLQQLVD YLTIKPCETF
NLEYGTLKEN GYADLTIIDL DSEQEIKGED FLSKADNTPF IGYKVYGNPI LTMVEGEVKF
EGDK
//
