ID   PYRF_PARMW              Reviewed;         246 AA.
AC   Q7U8P3;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 111.
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};
GN   OrderedLocusNames=SYNW0571;
OS   Parasynechococcus marenigrum (strain WH8102).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Prochlorococcaceae; Parasynechococcus; Parasynechococcus marenigrum.
OX   NCBI_TaxID=84588;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH8102;
RX   PubMed=12917641; DOI=10.1038/nature01943;
RA   Palenik B., Brahamsha B., Larimer F.W., Land M.L., Hauser L., Chain P.,
RA   Lamerdin J.E., Regala W., Allen E.E., McCarren J., Paulsen I.T.,
RA   Dufresne A., Partensky F., Webb E.A., Waterbury J.;
RT   "The genome of a motile marine Synechococcus.";
RL   Nature 424:1037-1042(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; BX569690; CAE07086.1; -; Genomic_DNA.
DR   RefSeq; WP_011127440.1; NC_005070.1.
DR   AlphaFoldDB; Q7U8P3; -.
DR   SMR; Q7U8P3; -.
DR   STRING; 84588.SYNW0571; -.
DR   KEGG; syw:SYNW0571; -.
DR   eggNOG; COG0284; Bacteria.
DR   HOGENOM; CLU_067069_1_0_3; -.
DR   UniPathway; UPA00070; UER00120.
DR   Proteomes; UP000001422; 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   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; Lyase; Pyrimidine biosynthesis; Reference proteome.
FT   CHAIN           1..246
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /id="PRO_0000134593"
FT   ACT_SITE        68
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT   BINDING         18
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT   BINDING         39
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT   BINDING         66..75
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT   BINDING         130
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT   BINDING         192
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT   BINDING         201
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT   BINDING         221
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT   BINDING         222
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
SQ   SEQUENCE   246 AA;  25234 MW;  5114744A09AECCD0 CRC64;
     MAPSLASGPA DRIIVALDGM APEQALRFAA QLDGLRWVKV GLELFVQAGP EVVAQLREQG
     LRVFLDLKFH DIPATMAGAC RRAAALGAEL ITVHACAGSE ALKAAQAAAV EGAQQAGLNP
     PTLLAVTVLT SWEEQRLQRE LAIQQSIGER VPALAQLSAT AGIGGCVCSP LEAAALRAQH
     PEPFALVTPG IRPKGSAVGD QARVMGPAEA IAAGASQLVI GRPITKADDP SAAFAACCTQ
     LLGSID
//