ID Z4WX99_9PORP Unreviewed; 278 AA.
AC Z4WX99;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=orotidine-5'-phosphate decarboxylase {ECO:0000256|ARBA:ARBA00012321};
DE EC=4.1.1.23 {ECO:0000256|ARBA:ARBA00012321};
GN Name=pyrF {ECO:0000313|EMBL:EWC92109.1};
GN ORFNames=HMPREF0636_0840 {ECO:0000313|EMBL:EWC92109.1};
OS Porphyromonas catoniae ATCC 51270.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=887901 {ECO:0000313|EMBL:EWC92109.1, ECO:0000313|Proteomes:UP000023482};
RN [1] {ECO:0000313|EMBL:EWC92109.1, ECO:0000313|Proteomes:UP000023482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51270 {ECO:0000313|EMBL:EWC92109.1,
RC ECO:0000313|Proteomes:UP000023482};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Haft D.H., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + orotidine 5'-phosphate = CO2 + UMP;
CC Xref=Rhea:RHEA:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57538, ChEBI:CHEBI:57865; EC=4.1.1.23;
CC Evidence={ECO:0000256|ARBA:ARBA00001419};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC UMP from orotate: step 2/2. {ECO:0000256|ARBA:ARBA00004861}.
CC -!- SIMILARITY: Belongs to the OMP decarboxylase family. Type 2 subfamily.
CC {ECO:0000256|ARBA:ARBA00008847}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EWC92109.1}.
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DR EMBL; JDFF01000018; EWC92109.1; -; Genomic_DNA.
DR RefSeq; WP_044168881.1; NZ_JDFF01000018.1.
DR AlphaFoldDB; Z4WX99; -.
DR PATRIC; fig|887901.3.peg.1008; -.
DR OrthoDB; 9808470at2; -.
DR UniPathway; UPA00070; UER00120.
DR Proteomes; UP000023482; Unassembled WGS sequence.
DR GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IEA:UniProtKB-EC.
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 CDD; cd04725; OMP_decarboxylase_like; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR011995; OMPdecase_type-2.
DR InterPro; IPR001754; OMPdeCOase_dom.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR NCBIfam; TIGR02127; pyrF_sub2; 1.
DR PANTHER; PTHR43375; OROTIDINE 5'-PHOSPHATE DECARBOXYLASE; 1.
DR PANTHER; PTHR43375:SF1; OROTIDINE 5'-PHOSPHATE DECARBOXYLASE; 1.
DR Pfam; PF00215; OMPdecase; 1.
DR SMART; SM00934; OMPdecase; 1.
DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:EWC92109.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000023482}.
FT DOMAIN 16..255
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /evidence="ECO:0000259|SMART:SM00934"
SQ SEQUENCE 278 AA; 30886 MW; CE5AD7CD4E6E9DD1 CRC64;
MTKEELFDNI RRKKSFLCIG LDTDVRKIPQ FLLSEDDPIF AFNKRIIDAT AHLCVAYKPN
LAFYESMGSF GILAFEKTIE YLRQQYPDQF IIADAKRGDI GNTSDMYARS FFEHLKVDAL
TVAPYMGSDS VLPFLKYTHH WVVLLALTSN EGAEDFQLTK TEDGDALFEL VLKKSLAWGG
SDQLMYVVGA TKASMLERVR AIVPESFLLV PGVGSQNGSL EEVALHGLNS QCGLLVNASR
SIIYADNTEA FASGAAAEAE KLRHQMADIL IKNKLVEA
//
