ID R6EL23_9FIRM Unreviewed; 232 AA.
AC R6EL23;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 43.
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=BN553_01625 {ECO:0000313|EMBL:CDA90647.1};
OS Firmicutes bacterium CAG:238.
OC Bacteria; Bacillota.
OX NCBI_TaxID=1263011 {ECO:0000313|EMBL:CDA90647.1, ECO:0000313|Proteomes:UP000018260};
RN [1] {ECO:0000313|EMBL:CDA90647.1, ECO:0000313|Proteomes:UP000018260}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:238 {ECO:0000313|Proteomes:UP000018260};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CDA90647.1}.
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DR EMBL; CBCS010000085; CDA90647.1; -; Genomic_DNA.
DR AlphaFoldDB; R6EL23; -.
DR UniPathway; UPA00070; UER00120.
DR Proteomes; UP000018260; 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:UP000018260}.
FT DOMAIN 4..226
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 10
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT BINDING 32
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 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; 25308 MW; 018BB1B3C377D665 CRC64;
MGKDVIIACD FASAEETLAF LDKFTAEKPY VKIGMELYYA EGPQIVKKIK ERGHKIFLDL
KLHDIPNTVK KAMKVLSALD VDMCNLHAAG TAAMMEAALE GLTREDGTRP LLIAVTQLTS
TDQERMEKDL LIEKPLEEVV DHYAANAKKA GLDGVVCSPL EAARVHELCG EGFLTVTPGV
RFADGDAGDQ VRVTTPQRAK EIGSDYIVVG RPITQAEDPV AAYRRCVSEF VG
//
