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Database: UniProt
Entry: A0A137SW39_9FIRM
LinkDB: A0A137SW39_9FIRM
Original site: A0A137SW39_9FIRM 
ID   A0A137SW39_9FIRM        Unreviewed;       285 AA.
AC   A0A137SW39;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Orotidine 5'-phosphate decarboxylase {ECO:0000256|HAMAP-Rule:MF_01215};
DE            EC=4.1.1.23 {ECO:0000256|HAMAP-Rule:MF_01215};
DE   AltName: Full=OMP decarboxylase {ECO:0000256|HAMAP-Rule:MF_01215};
DE            Short=OMPDCase {ECO:0000256|HAMAP-Rule:MF_01215};
DE            Short=OMPdecase {ECO:0000256|HAMAP-Rule:MF_01215};
GN   Name=pyrF {ECO:0000256|HAMAP-Rule:MF_01215};
GN   ORFNames=HMPREF3189_00675 {ECO:0000313|EMBL:KXO16620.1};
OS   Clostridiales bacterium KA00134.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales.
OX   NCBI_TaxID=1588750 {ECO:0000313|EMBL:KXO16620.1, ECO:0000313|Proteomes:UP000070500};
RN   [1] {ECO:0000313|EMBL:KXO16620.1, ECO:0000313|Proteomes:UP000070500}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KA00134 {ECO:0000313|EMBL:KXO16620.1,
RC   ECO:0000313|Proteomes:UP000070500};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-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, ECO:0000256|HAMAP-
CC         Rule:MF_01215};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       UMP from orotate: step 2/2. {ECO:0000256|ARBA:ARBA00004861,
CC       ECO:0000256|HAMAP-Rule:MF_01215}.
CC   -!- SIMILARITY: Belongs to the OMP decarboxylase family. Type 2 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008847, ECO:0000256|HAMAP-Rule:MF_01215}.
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:KXO16620.1}.
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DR   EMBL; LTAF01000014; KXO16620.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A137SW39; -.
DR   STRING; 1588750.HMPREF3189_00675; -.
DR   PATRIC; fig|1588750.3.peg.662; -.
DR   UniPathway; UPA00070; UER00120.
DR   Proteomes; UP000070500; Unassembled WGS sequence.
DR   GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IEA:UniProtKB-UniRule.
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   HAMAP; MF_01215; OMPdecase_type2; 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   Decarboxylase {ECO:0000256|HAMAP-Rule:MF_01215};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01215};
KW   Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01215};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070500}.
FT   DOMAIN          17..266
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /evidence="ECO:0000259|SMART:SM00934"
FT   ACT_SITE        97
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01215"
SQ   SEQUENCE   285 AA;  32084 MW;  0CC78CE8F19719B6 CRC64;
     MTSIMQSLYN RVKEKSNICV GLDTKLEYIP KSDRHLSVKD QLFNFNKRII DATSDLVSCF
     KPQIAYYEAC GIEGLMAYKE TLKYLKSKNL ISIGDIKRSD IASTGQMYAK AHFEGDFEAD
     IITLNPYMGF DSIKPYLPYF ESGQKGAFVL LRTSNPGAKD IEMLDHKGEA LFMTVGDGLK
     KISDSLKNDK NISPLGLVVG ATHEEEAKNI RQRFKDMFFL IPGYGAQGGR ADVVKKYLDE
     DLNMGVINSS RAIITNFKKY EDGEDKIGHY AREAVLAMKR DIYGE
//
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