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Database: UniProt
Entry: A0A0M3APZ6_9SPHN
LinkDB: A0A0M3APZ6_9SPHN
Original site: A0A0M3APZ6_9SPHN 
ID   A0A0M3APZ6_9SPHN        Unreviewed;       224 AA.
AC   A0A0M3APZ6;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Orotidine 5'-phosphate decarboxylase {ECO:0000256|RuleBase:RU000512};
DE            EC=4.1.1.23 {ECO:0000256|RuleBase:RU000512};
GN   ORFNames=YP76_15390 {ECO:0000313|EMBL:KKW90996.1};
OS   Sphingobium chungbukense.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=56193 {ECO:0000313|EMBL:KKW90996.1, ECO:0000313|Proteomes:UP000033874};
RN   [1] {ECO:0000313|EMBL:KKW90996.1, ECO:0000313|Proteomes:UP000033874}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJ77 {ECO:0000313|EMBL:KKW90996.1,
RC   ECO:0000313|Proteomes:UP000033874};
RA   Kim Y.-C., Chae J.-C.;
RT   "Genome sequence of aromatic hydrocarbons-degrading Sphingobium
RT   chungbukense DJ77.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate
CC       (OMP) to uridine 5'-monophosphate (UMP).
CC       {ECO:0000256|ARBA:ARBA00002356}.
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         ECO:0000256|RuleBase:RU000512};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       UMP from orotate: step 2/2. {ECO:0000256|ARBA:ARBA00004861,
CC       ECO:0000256|RuleBase:RU000512}.
CC   -!- SIMILARITY: Belongs to the OMP decarboxylase family.
CC       {ECO:0000256|RuleBase:RU000512}.
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:KKW90996.1}.
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DR   EMBL; LBIC01000007; KKW90996.1; -; Genomic_DNA.
DR   RefSeq; WP_046764513.1; NZ_LBIC01000007.1.
DR   AlphaFoldDB; A0A0M3APZ6; -.
DR   STRING; 56193.YP76_15390; -.
DR   PATRIC; fig|56193.3.peg.3213; -.
DR   UniPathway; UPA00070; UER00120.
DR   Proteomes; UP000033874; 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; IPR014732; OMPdecase.
DR   InterPro; IPR018089; OMPdecase_AS.
DR   InterPro; IPR001754; OMPdeCOase_dom.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   NCBIfam; TIGR01740; pyrF; 1.
DR   PANTHER; PTHR32119; OROTIDINE 5'-PHOSPHATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR32119:SF2; OROTIDINE 5'-PHOSPHATE DECARBOXYLASE; 1.
DR   Pfam; PF00215; OMPdecase; 1.
DR   SMART; SM00934; OMPdecase; 1.
DR   SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
DR   PROSITE; PS00156; OMPDECASE; 1.
PE   3: Inferred from homology;
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793,
KW   ECO:0000256|RuleBase:RU000512};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000512};
KW   Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975,
KW   ECO:0000256|RuleBase:RU000512}.
FT   DOMAIN          4..220
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /evidence="ECO:0000259|SMART:SM00934"
SQ   SEQUENCE   224 AA;  23520 MW;  25E81DC894A84D11 CRC64;
     MTSPIYVAID TPDLRKAQDL AQQVRHHVGG LKLGLEFFCA HGHHGVHEMM KFGLPVFLDL
     KLHDIPNTVA KAVQALHMLE PAILTVHAAG GRAMLEDAKA AAGVNTKVVA VTVLTSLDNG
     DLLDIGVGGK AEDQVARLAD LARSAGLDGI VCSGEEVGLA KRAWPDGFFV VPGVRPAGGA
     MGDQKRAVTP REALDRGASI LVVGRPISLA EKPDLAAREI EATL
//
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