GenomeNet

Database: UniProt
Entry: P65906
LinkDB: P65906
Original site: P65906 
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   30-AUG-2017, entry version 91.
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}; OrderedLocusNames=SA1044;
OS   Staphylococcus aureus (strain N315).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   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   -!- 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; BA000018; BAB42296.1; -; Genomic_DNA.
DR   PIR; D89892; D89892.
DR   RefSeq; WP_000767028.1; NC_002745.2.
DR   ProteinModelPortal; P65906; -.
DR   SMR; P65906; -.
DR   EnsemblBacteria; BAB42296; BAB42296; BAB42296.
DR   GeneID; 31213961; -.
DR   KEGG; sau:SA1044; -.
DR   HOGENOM; HOG000219142; -.
DR   KO; K01465; -.
DR   OMA; EYVKAFD; -.
DR   UniPathway; UPA00070; UER00117.
DR   Proteomes; UP000000751; 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   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   REGION       60     62       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00220}.
FT   REGION      321    322       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00220}.
FT   ACT_SITE    303    303       {ECO:0000255|HAMAP-Rule:MF_00220}.
FT   METAL        58     58       Zinc 1; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00220}.
FT   METAL        60     60       Zinc 1; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00220}.
FT   METAL       150    150       Zinc 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_00220}.
FT   METAL       150    150       Zinc 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00220}.
FT   METAL       177    177       Zinc 2; via pros nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00220}.
FT   METAL       230    230       Zinc 2; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00220}.
FT   METAL       303    303       Zinc 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_00220}.
FT   BINDING      92     92       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00220}.
FT   BINDING     276    276       Substrate; via amide nitrogen and
FT                                carbonyl oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00220}.
FT   BINDING     307    307       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00220}.
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
//
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