ID R9LML8_9FIRM Unreviewed; 232 AA.
AC R9LML8;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 51.
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=C815_01868 {ECO:0000313|EMBL:EOS60015.1};
OS Firmicutes bacterium M10-2.
OC Bacteria; Bacillota.
OX NCBI_TaxID=1235796 {ECO:0000313|EMBL:EOS60015.1, ECO:0000313|Proteomes:UP000014154};
RN [1] {ECO:0000313|EMBL:EOS60015.1, ECO:0000313|Proteomes:UP000014154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M10-2 {ECO:0000313|EMBL:EOS60015.1,
RC ECO:0000313|Proteomes:UP000014154};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Firmicutes bacterium M10-2.";
RL Submitted (APR-2013) 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, 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:EOS60015.1}.
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DR EMBL; ASTB01000037; EOS60015.1; -; Genomic_DNA.
DR AlphaFoldDB; R9LML8; -.
DR STRING; 1235796.C815_01868; -.
DR PATRIC; fig|1235796.3.peg.1885; -.
DR eggNOG; COG0284; Bacteria.
DR HOGENOM; CLU_067069_1_1_9; -.
DR OrthoDB; 9806203at2; -.
DR UniPathway; UPA00070; UER00120.
DR Proteomes; UP000014154; 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:UP000014154}.
FT DOMAIN 3..226
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /evidence="ECO:0000259|SMART:SM00934"
FT ACT_SITE 59
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT BINDING 9
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT BINDING 30
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT BINDING 57..66
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT BINDING 181
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT BINDING 210
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT BINDING 211
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
SQ SEQUENCE 232 AA; 25134 MW; 097C484E129E7355 CRC64;
MSKTIVALDF SNKEEVIKFL EQFDKPIYVK IGMELTYACG LDIVKTIKEM GHQIFLDLKL
HDIPNTVKGG MKNLAKLGVD MTNVHCSGGI TMMKAAVEGL KEGAKDGQRP LCIGVTQLTS
TSQKAMNDEL GISGSVIDCV IHYAKNAKEA GLDGVVCSVH EAKAIHEACG EDFLTVTPGI
RLASDSVDDQ KRVATPQLAK EEGCDYIVVG RSITKAENPK MVFDQIETIM EG
//
