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Database: UniProt
Entry: A0A249JXT1_9ACTN
LinkDB: A0A249JXT1_9ACTN
Original site: A0A249JXT1_9ACTN 
ID   A0A249JXT1_9ACTN        Unreviewed;       230 AA.
AC   A0A249JXT1;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Orotidine 5'-phosphate decarboxylase {ECO:0000256|RuleBase:RU000512};
DE            EC=4.1.1.23 {ECO:0000256|RuleBase:RU000512};
GN   ORFNames=B1s21122_03155 {ECO:0000313|EMBL:ASY09343.1};
OS   Candidatus Nanopelagicus limnes.
OC   Bacteria; Actinomycetota; Actinomycetes; Candidatus Nanopelagicales;
OC   Candidatus Nanopelagicaceae; Nanopelagicus.
OX   NCBI_TaxID=1884634 {ECO:0000313|EMBL:ASY09343.1, ECO:0000313|Proteomes:UP000217153};
RN   [1] {ECO:0000313|Proteomes:UP000217153}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Neuenschwander S.M., Salcher M., Ghai R., Pernthaler J.;
RT   "High microdiversification within the ubiquitous acI lineage of
RT   Actinobacteria.";
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; CP016768; ASY09343.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A249JXT1; -.
DR   KEGG; abam:B1s21122_03155; -.
DR   OrthoDB; 9806203at2; -.
DR   UniPathway; UPA00070; UER00120.
DR   Proteomes; UP000217153; Chromosome.
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..222
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /evidence="ECO:0000259|SMART:SM00934"
SQ   SEQUENCE   230 AA;  24766 MW;  21EB51BE91BE31D3 CRC64;
     MSLPIILALD TKDLNQAGQW IKASSDQIDH FKIGLEFYLQ HGSEGIMQLR EICDFKLFLD
     LKLYDIPNTV KGAVESVAKL SPKFLTVHAS GGAKMIEAAS QAFPNGSITA VTVLTSFSED
     EFSKMGYRCS IADTTNLWAS VAIKAGATSL VCSPFEVSSL RNQFKDAVLI TPGVRVAGDD
     LGDQSRVMSA PDAISAGADF VVIGRSITSQ WDGSDLKMRR KIDLIANSLG
//
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