PYRC_STAAC
ID PYRC_STAAC Reviewed; 424 AA.
AC Q5HGN1;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=SACOL1213;
OS Staphylococcus aureus (strain COL).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93062;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
RN [2] {ECO:0007744|PDB:3GRI}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH ZINC, AND COFACTOR.
RC STRAIN=COL;
RA Brunzelle J.S., Wawrzak Z., Skarina T., Onopriyenko O., Savchenko A.,
RA Anderson W.F.;
RT "The crystal structure of a dihydroorotase from Staphylococcus aureus.";
RL Submitted (MAR-2009) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate
CC to dihydroorotate. {ECO:0000255|HAMAP-Rule:MF_00220}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate;
CC Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00220};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00220, ECO:0000269|Ref.2};
CC Note=Binds 1 Zn(2+) ions per subunit. {ECO:0000269|Ref.2};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 3/3. {ECO:0000255|HAMAP-
CC Rule:MF_00220}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC DHOase family. Class I DHOase subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_00220, ECO:0000305}.
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DR EMBL; CP000046; AAW38050.1; -; Genomic_DNA.
DR RefSeq; WP_000767028.1; NC_002951.2.
DR PDB; 3GRI; X-ray; 2.00 A; A/B=1-424.
DR PDBsum; 3GRI; -.
DR AlphaFoldDB; Q5HGN1; -.
DR SMR; Q5HGN1; -.
DR EnsemblBacteria; AAW38050; AAW38050; SACOL1213.
DR KEGG; sac:SACOL1213; -.
DR HOGENOM; CLU_015572_1_0_9; -.
DR OMA; QHAQEPR; -.
DR UniPathway; UPA00070; UER00117.
DR Proteomes; UP000000530; Chromosome.
DR GO; GO:0004151; F:dihydroorotase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
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; -; 2.
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; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR PROSITE; PS00482; DIHYDROOROTASE_1; 1.
DR PROSITE; PS00483; DIHYDROOROTASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Metal-binding; Pyrimidine biosynthesis; Zinc.
FT CHAIN 1..424
FT /note="Dihydroorotase"
FT /id="PRO_0000147246"
FT ACT_SITE 303
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 58
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:3GRI"
FT BINDING 60..62
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:3GRI"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 276
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 303
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:3GRI"
FT BINDING 307
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 321..322
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-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
