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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   26-NOV-2014, entry version 24.
DE   RecName: Full=Orotidine 5'-phosphate decarboxylase {ECO:0000256|HAMAP-Rule:MF_01200, ECO:0000256|SAAS:SAAS00032256};
DE            EC=4.1.1.23 {ECO:0000256|HAMAP-Rule:MF_01200, ECO:0000256|SAAS:SAAS00032220};
DE   AltName: Full=OMP decarboxylase {ECO:0000256|HAMAP-Rule:MF_01200};
GN   Name=pyrF {ECO:0000256|HAMAP-Rule:MF_01200};
GN   ORFNames=HIBPF_06000 {ECO:0000313|EMBL:CBY80777.1};
OS   Haemophilus influenzae F3031.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=866630 {ECO:0000313|EMBL:CBY80777.1, ECO:0000313|Proteomes:UP000006795};
RN   [1] {ECO:0000313|EMBL:CBY80777.1, ECO:0000313|Proteomes:UP000006795}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F3031 {ECO:0000313|EMBL:CBY80777.1};
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).
CC       {ECO:0000256|HAMAP-Rule:MF_01200, ECO:0000256|SAAS:SAAS00044996}.
CC   -!- CATALYTIC ACTIVITY: Orotidine 5'-phosphate = UMP + CO(2).
CC       {ECO:0000256|HAMAP-Rule:MF_01200}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; UMP from orotate: step 2/2. {ECO:0000256|HAMAP-
CC       Rule:MF_01200}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01200,
CC       ECO:0000256|SAAS:SAAS00044981}.
CC   -!- SIMILARITY: Belongs to the OMP decarboxylase family. Type 1
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01200}.
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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 {ECO:0000313|Proteomes:UP000006795};
KW   Decarboxylase {ECO:0000256|HAMAP-Rule:MF_01200};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01200};
KW   Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01200}.
FT   REGION       59     68       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01200}.
FT   ACT_SITE     61     61       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01200}.
FT   BINDING      10     10       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01200}.
FT   BINDING      32     32       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01200}.
FT   BINDING     119    119       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01200}.
FT   BINDING     180    180       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01200}.
FT   BINDING     189    189       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01200}.
FT   BINDING     209    209       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01200}.
FT   BINDING     210    210       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01200}.
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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