ID   A0A136NBW2_9BACT        Unreviewed;       246 AA.
AC   A0A136NBW2;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=orotidine-5'-phosphate decarboxylase {ECO:0000256|ARBA:ARBA00012321};
DE            EC=4.1.1.23 {ECO:0000256|ARBA:ARBA00012321};
GN   ORFNames=UZ11_BCD004000570 {ECO:0000313|EMBL:KXK43639.1};
OS   Bacteroidetes bacterium OLB11.
OC   Bacteria; Bacteroidota.
OX   NCBI_TaxID=1617422 {ECO:0000313|EMBL:KXK43639.1, ECO:0000313|Proteomes:UP000070496};
RN   [1] {ECO:0000313|EMBL:KXK43639.1, ECO:0000313|Proteomes:UP000070496}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OLB11 {ECO:0000313|EMBL:KXK43639.1};
RA   Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT   "Genome based microbial ecology of anammox granules in a full-scale
RT   wastewater treatment system.";
RL   Submitted (NOV-2015) 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:KXK43639.1}.
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DR   EMBL; LNFQ01000019; KXK43639.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A136NBW2; -.
DR   STRING; 1617422.UZ11_BCD004000570; -.
DR   PATRIC; fig|1617422.3.peg.623; -.
DR   UniPathway; UPA00070; UER00120.
DR   Proteomes; UP000070496; 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          9..231
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /evidence="ECO:0000259|SMART:SM00934"
SQ   SEQUENCE   246 AA;  28106 MW;  E6FA8DD84B4543AF CRC64;
     MIPIFQKSRV FLLKEKDPIF EFNKQIIDST KDICVSYKIN TAFYEANGVD GWQSMQKTID
     YIPKNIFTIA DAKRGDIGNT STQYAKAFFQ NMNFDSVTVA PYMGKDSVSP FLQFEGKWAI
     VLGLTSNEGA FDFQYLKQND VFLFESVIKK VSEWGNEQNL MFVIGATQTE QLQRIRQIIP
     RHFLLIPGVG TQGGSLQQVC QYGMNEDFGI LINVSRQIIY ASNQEDFAAK AHEAALKFKK
     EMEVYF
//