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Database: UniProt
Entry: M7N2J2_9BACT
LinkDB: M7N2J2_9BACT
Original site: M7N2J2_9BACT 
ID   M7N2J2_9BACT            Unreviewed;       277 AA.
AC   M7N2J2;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=orotidine-5'-phosphate decarboxylase {ECO:0000256|ARBA:ARBA00012321};
DE            EC=4.1.1.23 {ECO:0000256|ARBA:ARBA00012321};
GN   ORFNames=ADICEAN_03337 {ECO:0000313|EMBL:EMR01522.1};
OS   Cesiribacter andamanensis AMV16.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cesiribacteraceae;
OC   Cesiribacter.
OX   NCBI_TaxID=1279009 {ECO:0000313|EMBL:EMR01522.1, ECO:0000313|Proteomes:UP000011910};
RN   [1] {ECO:0000313|EMBL:EMR01522.1, ECO:0000313|Proteomes:UP000011910}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AMV16 {ECO:0000313|EMBL:EMR01522.1,
RC   ECO:0000313|Proteomes:UP000011910};
RX   PubMed=23682146;
RA   Shivaji S., Ara S., Begum Z., Srinivas T.N., Singh A., Kumar Pinnaka A.;
RT   "Draft Genome Sequence of Cesiribacter andamanensis Strain AMV16T, Isolated
RT   from a Soil Sample from a Mud Volcano in the Andaman Islands, India.";
RL   Genome Announc. 1:E00240-13(2013).
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:EMR01522.1}.
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DR   EMBL; AODQ01000108; EMR01522.1; -; Genomic_DNA.
DR   RefSeq; WP_009196720.1; NZ_AODQ01000108.1.
DR   AlphaFoldDB; M7N2J2; -.
DR   STRING; 1279009.ADICEAN_03337; -.
DR   PATRIC; fig|1279009.4.peg.3381; -.
DR   eggNOG; COG0284; Bacteria.
DR   OrthoDB; 9808470at2; -.
DR   UniPathway; UPA00070; UER00120.
DR   Proteomes; UP000011910; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011910}.
FT   DOMAIN          16..252
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /evidence="ECO:0000259|SMART:SM00934"
SQ   SEQUENCE   277 AA;  31231 MW;  3C57A7BE101B8654 CRC64;
     MTYQDLFETI RKKRSYLCVG LDTDPAKLPK HLLDHPNPVL EFNRRIIEAT APYCVAYKPN
     TAFYEAMGSQ GWELLRQTLE LIPRTHFSIA DAKRGDIGNT SKMYAKAFFE DMKADAITVA
     PYMGADSVQP FLEFEGKWTI LLALTSNSGS QDFQVLNVDE DHCLFERVIK TSQVWGDKHQ
     MMYVVGATQT TELQAVRKLA PDHFLLVPGV GAQGGSLEEV SKWGMNRHCG LLVNASRSIL
     WASDGEDFAE AAAAEARRLQ EHMSHYLEKY LPSQQHD
//
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