ID PYRF_STAAB Reviewed; 230 AA.
AC Q2YXG4;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 01-MAY-2013, entry version 57.
DE RecName: Full=Orotidine 5'-phosphate decarboxylase;
DE EC=4.1.1.23;
DE AltName: Full=OMP decarboxylase;
DE Short=OMPDCase;
DE Short=OMPdecase;
GN Name=pyrF; OrderedLocusNames=SAB1068;
OS Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus.
OX NCBI_TaxID=273036;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=bovine RF122 / ET3-1;
RX PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT "Molecular correlates of host specialization in Staphylococcus
RT aureus.";
RL PLoS ONE 2:E1120-E1120(2007).
CC -!- FUNCTION: Catalyzes the decarboxylation of orotidine 5'-
CC monophosphate (OMP) to uridine 5'-monophosphate (UMP) (By
CC similarity).
CC -!- CATALYTIC ACTIVITY: Orotidine 5'-phosphate = UMP + CO(2).
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC pathway; UMP from orotate: step 2/2.
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SIMILARITY: Belongs to the OMP decarboxylase family. Type 1
CC subfamily.
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DR EMBL; AJ938182; CAI80757.1; -; Genomic_DNA.
DR RefSeq; YP_416550.1; NC_007622.1.
DR ProteinModelPortal; Q2YXG4; -.
DR SMR; Q2YXG4; 1-228.
DR STRING; 273036.SAB1068; -.
DR EnsemblBacteria; CAI80757; CAI80757; SAB1068.
DR GeneID; 3794691; -.
DR KEGG; sab:SAB1068; -.
DR PATRIC; 19522973; VBIStaAur92441_1135.
DR eggNOG; COG0284; -.
DR HOGENOM; HOG000226071; -.
DR KO; K01591; -.
DR OMA; NFKIFLD; -.
DR ProtClustDB; PRK00230; -.
DR BioCyc; SAUR273036:GJVS-1090-MONOMER; -.
DR UniPathway; UPA00070; UER00120.
DR GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IEA:HAMAP.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_01200_B; OMPdecase_type1_B; 1; -.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR014732; OMPdecase.
DR InterPro; IPR018089; OMPdecase_AS.
DR InterPro; IPR001754; OMPdeCOase_dom.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR Pfam; PF00215; OMPdecase; 1.
DR SMART; SM00934; OMPdecase; 1.
DR SUPFAM; SSF51366; RibP_bind_barrel; 1.
DR TIGRFAMs; TIGR01740; pyrF; 1.
DR PROSITE; PS00156; OMPDECASE; 1.
PE 3: Inferred from homology;
KW Complete proteome; Decarboxylase; Lyase; Pyrimidine biosynthesis.
FT CHAIN 1 230 Orotidine 5'-phosphate decarboxylase.
FT /FTId=PRO_0000241910.
FT REGION 58 67 Substrate binding (By similarity).
FT ACT_SITE 60 60 Proton donor (By similarity).
FT BINDING 10 10 Substrate (By similarity).
FT BINDING 31 31 Substrate (By similarity).
FT BINDING 117 117 Substrate (By similarity).
FT BINDING 179 179 Substrate (By similarity).
FT BINDING 188 188 Substrate (By similarity).
FT BINDING 208 208 Substrate; via amide nitrogen (By
FT similarity).
FT BINDING 209 209 Substrate (By similarity).
SQ SEQUENCE 230 AA; 25648 MW; AAD97867A13382BA CRC64;
MKDLPIIALD FESKEKVNRF LDLFDESLFV KVGMELFYQE GPQLINEIKE RGHDVFLDLK
LHDIPNTVGK AMEGLAKLNV DLVNVHAAGG VKMMSEAIKG LRKHNEHTKI IAVTQLTSTT
EDMLRHEQNI QTSIEEAVLN YAKLANATGL DGVVCSPLES RMLTEKLGAS FLKVTPGIRP
KGASQDDQHR ITTPEEARQL GSTHIVVGRP ITQSDNPVES YHKIKESWLV
//
