ID E7A404_HAEIF Unreviewed; 230 AA.
AC E7A404;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 06-MAR-2013, entry version 16.
DE RecName: Full=Orotidine 5'-phosphate decarboxylase;
DE EC=4.1.1.23;
DE AltName: Full=OMP decarboxylase;
GN Name=pyrF; ORFNames=HIBPF_06000;
OS Haemophilus influenzae F3031.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=866630;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=F3031;
RA Aslett M.;
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=F3031;
RX PubMed=22377449; DOI=10.3201/eid1803.110728;
RA Strouts F.R., Power P., Croucher N.J., Corton N., van Tonder A.,
RA Quail M.A., Langford P.R., Hudson M.J., Parkhill J., Kroll J.S.,
RA Bentley S.D.;
RT "Lineage-specific Virulence Determinants of Haemophilus influenzae
RT Biogroup aegyptius.";
RL Emerg. Infect. Dis. 18:449-457(2012).
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; FQ670178; CBY80777.1; -; Genomic_DNA.
DR RefSeq; YP_004135113.1; NC_014920.1.
DR ProteinModelPortal; E7A404; -.
DR GeneID; 10133372; -.
DR KEGG; hif:HIBPF06000; -.
DR PATRIC; 45230452; VBIHaeInf165906_0562.
DR HOGENOM; HOG000226071; -.
DR KO; K01591; -.
DR BioCyc; HINF866630:GJN7-541-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 Decarboxylase; Lyase; Pyrimidine biosynthesis.
FT REGION 59 68 Substrate binding (By similarity).
FT ACT_SITE 61 61 Proton donor (By similarity).
FT BINDING 10 10 Substrate (By similarity).
FT BINDING 32 32 Substrate (By similarity).
FT BINDING 119 119 Substrate (By similarity).
FT BINDING 180 180 Substrate (By similarity).
FT BINDING 189 189 Substrate (By similarity).
FT BINDING 209 209 Substrate; via amide nitrogen (By
FT similarity).
FT BINDING 210 210 Substrate (By similarity).
SQ SEQUENCE 230 AA; 25206 MW; 1967E5A7464867C6 CRC64;
MTSKIIVALD FEKEAEALAL VDQIDPSLCR LKVGKEMFTT LGINFIKQLH QRNFDVFLDL
KYHDIPNTVA RAVRSAADLG VWMVDLHASG GLRMMEDAKK ILEPYGKDAP LLIAVTVLTS
MEDLDLLQIG INASPMEQVL RLAHLTQRAG LDGVVCSPQE VEILRNACGE DFKLVTPGIR
PIGTDFGDQR RVMTPTAAIR AGSDYLVIGR PITQADNPAE VLRSINVSIG
//
