ID   PYRF_PROMP              Reviewed;         239 AA.
AC   Q7V0D8;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Orotidine 5'-phosphate decarboxylase {ECO:0000255|HAMAP-Rule:MF_01200};
DE            EC=4.1.1.23 {ECO:0000255|HAMAP-Rule:MF_01200};
DE   AltName: Full=OMP decarboxylase {ECO:0000255|HAMAP-Rule:MF_01200};
DE            Short=OMPDCase {ECO:0000255|HAMAP-Rule:MF_01200};
DE            Short=OMPdecase {ECO:0000255|HAMAP-Rule:MF_01200};
GN   Name=pyrF {ECO:0000255|HAMAP-Rule:MF_01200}; OrderedLocusNames=PMM1328;
OS   Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / NIES-2087 /
OS   MED4).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=59919;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1986 / NIES-2087 / MED4;
RX   PubMed=12917642; DOI=10.1038/nature01947;
RA   Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA   Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA   Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA   Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA   Chisholm S.W.;
RT   "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT   differentiation.";
RL   Nature 424:1042-1047(2003).
CC   -!- FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate
CC       (OMP) to uridine 5'-monophosphate (UMP). {ECO:0000255|HAMAP-
CC       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:0000255|HAMAP-Rule:MF_01200};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       UMP from orotate: step 2/2. {ECO:0000255|HAMAP-Rule:MF_01200}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01200}.
CC   -!- SIMILARITY: Belongs to the OMP decarboxylase family. Type 1 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01200}.
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DR   EMBL; BX548174; CAE19787.1; -; Genomic_DNA.
DR   RefSeq; WP_011132962.1; NC_005072.1.
DR   AlphaFoldDB; Q7V0D8; -.
DR   SMR; Q7V0D8; -.
DR   STRING; 59919.PMM1328; -.
DR   EnsemblBacteria; CAE19787; CAE19787; PMM1328.
DR   KEGG; pmm:PMM1328; -.
DR   eggNOG; COG0284; Bacteria.
DR   HOGENOM; CLU_067069_1_0_3; -.
DR   OMA; NFKIFLD; -.
DR   OrthoDB; 1150446at2; -.
DR   UniPathway; UPA00070; UER00120.
DR   Proteomes; UP000001026; Chromosome.
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   Gene3D; 3.20.20.70; -; 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; IPR001754; OMPdeCOase_dom.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   PANTHER; PTHR32119:SF2; PTHR32119:SF2; 1.
DR   Pfam; PF00215; OMPdecase; 1.
DR   SMART; SM00934; OMPdecase; 1.
DR   SUPFAM; SSF51366; SSF51366; 1.
DR   TIGRFAMs; TIGR01740; pyrF; 1.
DR   PROSITE; PS00156; OMPDECASE; 1.
PE   3: Inferred from homology;
KW   Decarboxylase; Lyase; Pyrimidine biosynthesis.
FT   CHAIN           1..239
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /id="PRO_0000134564"
FT   ACT_SITE        65
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT   BINDING         15
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT   BINDING         36
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT   BINDING         63..72
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT   BINDING         127
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT   BINDING         189
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT   BINDING         198
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT   BINDING         218
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT   BINDING         219
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
SQ   SEQUENCE   239 AA;  26275 MW;  EDE058FD602A8A18 CRC64;
     MKKFNTEEKI ILAIDGLDIF QAKVLLERCP NIKWVKVGLE LFTREGPSVI KILKNLNKKI
     FLDLKFHDIP NTMSAACYEV SKLGVDIISV HASAGSKALT ASKKASLEGA KIATVNAPCV
     IGITVLTSLS SEEFQTDLDR KNSIEENVIR LAKLSFDAGL DGCVCSPLEA KILRSMYKNN
     FELITPGIRT NIQKKDDQNR IMTPFEAISN GSSKLVIGRA ITKAKDPNKA FLDICESIC