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Database: UniProt/TrEMBL
Entry: E7A404_HAEIF
LinkDB: E7A404_HAEIF
Original site: E7A404_HAEIF 
ID   E7A404_HAEIF            Unreviewed;       230 AA.
AC   E7A404;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   19-FEB-2014, entry version 19.
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:UniProtKB-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; SSF51366; 1.
DR   TIGRFAMs; TIGR01740; pyrF; 1.
DR   PROSITE; PS00156; OMPDECASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; 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
//
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