ID A0A0R2C4L1_9LACO Unreviewed; 244 AA.
AC A0A0R2C4L1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Orotidine 5'-phosphate decarboxylase {ECO:0000256|HAMAP-Rule:MF_01200};
DE EC=4.1.1.23 {ECO:0000256|HAMAP-Rule:MF_01200};
DE AltName: Full=OMP decarboxylase {ECO:0000256|HAMAP-Rule:MF_01200};
DE Short=OMPDCase {ECO:0000256|HAMAP-Rule:MF_01200};
DE Short=OMPdecase {ECO:0000256|HAMAP-Rule:MF_01200};
GN Name=pyrF {ECO:0000256|HAMAP-Rule:MF_01200};
GN ORFNames=FD19_GL000751 {ECO:0000313|EMBL:KRM86423.1};
OS Lacticaseibacillus thailandensis DSM 22698 = JCM 13996.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=1423810 {ECO:0000313|EMBL:KRM86423.1, ECO:0000313|Proteomes:UP000051789};
RN [1] {ECO:0000313|EMBL:KRM86423.1, ECO:0000313|Proteomes:UP000051789}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22698 {ECO:0000313|EMBL:KRM86423.1,
RC ECO:0000313|Proteomes:UP000051789};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
CC -!- FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate
CC (OMP) to uridine 5'-monophosphate (UMP).
CC {ECO:0000256|ARBA:ARBA00002356, ECO:0000256|HAMAP-Rule:MF_01200}.
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_01200, 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|HAMAP-Rule:MF_01200, ECO:0000256|RuleBase:RU000512}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01200}.
CC -!- SIMILARITY: Belongs to the OMP decarboxylase family. Type 1 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01200}.
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:KRM86423.1}.
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DR EMBL; AYZK01000010; KRM86423.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2C4L1; -.
DR STRING; 1423810.FD19_GL000751; -.
DR PATRIC; fig|1423810.4.peg.766; -.
DR UniPathway; UPA00070; UER00120.
DR Proteomes; UP000051789; 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_01200_B; OMPdecase_type1_B; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR014732; OMPdecase.
DR InterPro; IPR018089; OMPdecase_AS.
DR InterPro; IPR047596; OMPdecase_bac.
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, ECO:0000256|HAMAP-
KW Rule:MF_01200};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01200};
KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975, ECO:0000256|HAMAP-
KW Rule:MF_01200}; Reference proteome {ECO:0000313|Proteomes:UP000051789}.
FT DOMAIN 7..234
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /evidence="ECO:0000259|SMART:SM00934"
FT ACT_SITE 65
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT BINDING 13
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT BINDING 36
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT BINDING 63..72
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT BINDING 127
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT BINDING 189
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT BINDING 198
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT BINDING 218
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT BINDING 219
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
SQ SEQUENCE 244 AA; 25906 MW; 65F97686C7CCF9E3 CRC64;
MNQAEPPLII ALDFPTPDDA LAFVQRFDHP EELFCKVGME LYYQGGPAVV RQLQALGVRV
FLDLKLHDIP NTVERAARII GGLGVALTTV HAQGGRKMMA AAVRGVRAGA ADAGVQPAKV
LAITQLTSTS PAALRDEQQV AVPLPDSVNH LAQLAATSGL DGVVSSAAEV AGMRPHLPDD
FLFITPGIRL ADAHVDDQVR VMTPDAARRA GSSGIVVGRP ITQATDPVAA YQHIKSLWEE
PIHE
//
