ID A0A1Q3WWS9_9BACT Unreviewed; 273 AA.
AC A0A1Q3WWS9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=orotidine-5'-phosphate decarboxylase {ECO:0000256|ARBA:ARBA00012321};
DE EC=4.1.1.23 {ECO:0000256|ARBA:ARBA00012321};
GN ORFNames=BGO59_00345 {ECO:0000313|EMBL:OJW79738.1};
OS Spirosoma sp. 48-14.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae; Spirosoma.
OX NCBI_TaxID=1895854 {ECO:0000313|EMBL:OJW79738.1, ECO:0000313|Proteomes:UP000186057};
RN [1] {ECO:0000313|EMBL:OJW79738.1, ECO:0000313|Proteomes:UP000186057}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=48-14 {ECO:0000313|EMBL:OJW79738.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) 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:OJW79738.1}.
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DR EMBL; MKUD01000003; OJW79738.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3WWS9; -.
DR STRING; 1895854.BGO59_00345; -.
DR UniPathway; UPA00070; UER00120.
DR Proteomes; UP000186057; 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}.
FT DOMAIN 16..255
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /evidence="ECO:0000259|SMART:SM00934"
SQ SEQUENCE 273 AA; 29707 MW; 411B55FFBD4A1051 CRC64;
MTYSELSSQI LQKQSYLCVG LDTDLRKIPT HLLAEKDPVF AFNKAIIDAT AAYTVAYKPN
IAFYEAQGPR GWESLQKTLD YIPADCFTIA DAKRGDIGNT SDLYARTFFE PTAAGLSFDS
VTVAPYMGHD SVTPFLAYEG KWVILLALTS NPGSADFQRQ AVADQELFET VIETAQTWAG
PDKLMFVVGA TQAKELGRIR TLAPKNFLLV PGVGAQGGSL ADVSRYGLTA DGGLLVNASR
SILYASTGTD FAEQARAEAK RLQQEMKSYL GRM
//