ID A0A0R2FAQ9_9LACO Unreviewed; 239 AA.
AC A0A0R2FAQ9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 36.
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=FC75_GL000371 {ECO:0000313|EMBL:KRN25457.1};
OS Lacticaseibacillus camelliae DSM 22697 = JCM 13995.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=1423730 {ECO:0000313|EMBL:KRN25457.1, ECO:0000313|Proteomes:UP000050865};
RN [1] {ECO:0000313|EMBL:KRN25457.1, ECO:0000313|Proteomes:UP000050865}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22697 {ECO:0000313|EMBL:KRN25457.1,
RC ECO:0000313|Proteomes:UP000050865};
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:KRN25457.1}.
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DR EMBL; AYZJ01000010; KRN25457.1; -; Genomic_DNA.
DR RefSeq; WP_056988936.1; NZ_AYZJ01000010.1.
DR AlphaFoldDB; A0A0R2FAQ9; -.
DR STRING; 1423730.FC75_GL000371; -.
DR PATRIC; fig|1423730.4.peg.390; -.
DR UniPathway; UPA00070; UER00120.
DR Proteomes; UP000050865; 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:UP000050865}.
FT DOMAIN 2..230
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /evidence="ECO:0000259|SMART:SM00934"
FT ACT_SITE 61
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT BINDING 8
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT BINDING 31
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT BINDING 59..68
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT BINDING 123
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT BINDING 215
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
SQ SEQUENCE 239 AA; 24932 MW; 99DC553FBF1A4C66 CRC64;
MAPIIALDFP TLEDTTGFLK RFEGGEPLTV KIGMELFYAA GPAAIKAVRQ AHPVEIFLDL
KLHDIPHTVE RAAYQLGRLG VQLTTAHAAG GSAMLAAAKR GLVAGAASQG LPAPKLLAIT
QLTSTSATMM HQELQIEGPV VDSVQHLAAV AQAAGADGVV ASAQEAPLIR AITRPDFLIV
TPGIRPAGSQ KGDQVRITTP GQAAQLGSSA IVVGRPITQA ADPVLAYQHI TEEWRHANV
//
