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 01-MAY-2013, entry version 46.
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 ProtClustDB; CLSK727277; -.
DR BioCyc; HHAL349124:GI3I-613-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 1 236 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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