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Database: UniProt/SWISS-PROT
Entry: PYRF_HALHL
LinkDB: PYRF_HALHL
Original site: PYRF_HALHL 
ID   PYRF_HALHL              Reviewed;         236 AA.
AC   A1WUI3;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   19-FEB-2014, entry version 50.
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=Hhal_0559;
OS   Halorhodospira halophila (strain DSM 244 / SL1) (Ectothiorhodospira
OS   halophila (strain DSM 244 / SL1)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Halorhodospira.
OX   NCBI_TaxID=349124;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 244 / SL1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Hoff W., Richardson P.;
RT   "Complete sequence of Halorhodospira halophila SL1.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000544; ABM61345.1; -; Genomic_DNA.
DR   RefSeq; YP_001002147.1; NC_008789.1.
DR   ProteinModelPortal; A1WUI3; -.
DR   STRING; 349124.Hhal_0559; -.
DR   EnsemblBacteria; ABM61345; ABM61345; Hhal_0559.
DR   GeneID; 4709653; -.
DR   KEGG; hha:Hhal_0559; -.
DR   PATRIC; 22095409; VBIHalHal112047_0569.
DR   eggNOG; COG0284; -.
DR   HOGENOM; HOG000226070; -.
DR   KO; K01591; -.
DR   OMA; NFKIFLD; -.
DR   OrthoDB; EOG651SX7; -.
DR   ProtClustDB; CLSK727277; -.
DR   BioCyc; HHAL349124:GI3I-570-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   CHAIN         1    236       Orotidine 5'-phosphate decarboxylase.
FT                                /FTId=PRO_1000073089.
FT   REGION       63     72       Substrate binding (By similarity).
FT   ACT_SITE     65     65       Proton donor (By similarity).
FT   BINDING      14     14       Substrate (By similarity).
FT   BINDING      36     36       Substrate (By similarity).
FT   BINDING     122    122       Substrate (By similarity).
FT   BINDING     183    183       Substrate (By similarity).
FT   BINDING     192    192       Substrate (By similarity).
FT   BINDING     212    212       Substrate; via amide nitrogen (By
FT                                similarity).
FT   BINDING     213    213       Substrate (By similarity).
SQ   SEQUENCE   236 AA;  23797 MW;  0A45C4571EAC9D98 CRC64;
     MSVPGPPRLV VALDFPAAAP AEALAAQLDP RLCRLKVGKE LFTRAGPQLV ERLHARGFEV
     FLDLKYHDIP NTVAGACRAA ADLGVWMVNV HALGGRRMLE AAAEAVAAAE GRTLITAVTV
     LTSHDAATLE EIGLAGPPRE AVLRLAGLAQ ASGLDGVVCS PEEAAAIGER FGAGLLRVTP
     GVRPAGAALG DQQRIATPAA AVAAGCDHLV VGRPITAAED PAAAAAAIAA EIAAAG
//
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