ID   PYRF_VIBCH              Reviewed;         231 AA.
AC   Q9KQT7;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, 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}; OrderedLocusNames=VC_1911;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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; AE003852; AAF95059.1; -; Genomic_DNA.
DR   PIR; A82143; A82143.
DR   RefSeq; NP_231545.1; NC_002505.1.
DR   RefSeq; WP_000999562.1; NZ_LT906614.1.
DR   PDB; 3LDV; X-ray; 1.77 A; A/B=1-231.
DR   PDB; 3UWQ; X-ray; 1.80 A; A/B=1-231.
DR   PDBsum; 3LDV; -.
DR   PDBsum; 3UWQ; -.
DR   AlphaFoldDB; Q9KQT7; -.
DR   SMR; Q9KQT7; -.
DR   STRING; 243277.VC_1911; -.
DR   DNASU; 2613540; -.
DR   EnsemblBacteria; AAF95059; AAF95059; VC_1911.
DR   GeneID; 57740543; -.
DR   KEGG; vch:VC_1911; -.
DR   PATRIC; fig|243277.26.peg.1828; -.
DR   eggNOG; COG0284; Bacteria.
DR   HOGENOM; CLU_067069_0_0_6; -.
DR   OMA; NFKIFLD; -.
DR   BioCyc; VCHO:VC1911-MON; -.
DR   UniPathway; UPA00070; UER00120.
DR   EvolutionaryTrace; Q9KQT7; -.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IBA:GO_Central.
DR   GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IBA:GO_Central.
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   1: Evidence at protein level;
KW   3D-structure; Decarboxylase; Lyase; Pyrimidine biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..231
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /id="PRO_0000134596"
FT   ACT_SITE        62
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT   BINDING         11
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT   BINDING         33
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT   BINDING         60..69
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT   BINDING         120
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT   BINDING         181
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT   BINDING         190
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT   BINDING         210
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT   BINDING         211
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT   STRAND          6..10
FT                   /evidence="ECO:0007829|PDB:3LDV"
FT   HELIX           15..22
FT                   /evidence="ECO:0007829|PDB:3LDV"
FT   HELIX           27..29
FT                   /evidence="ECO:0007829|PDB:3LDV"
FT   STRAND          31..35
FT                   /evidence="ECO:0007829|PDB:3LDV"
FT   HELIX           36..52
FT                   /evidence="ECO:0007829|PDB:3LDV"
FT   STRAND          57..63
FT                   /evidence="ECO:0007829|PDB:3LDV"
FT   HELIX           67..79
FT                   /evidence="ECO:0007829|PDB:3LDV"
FT   STRAND          83..88
FT                   /evidence="ECO:0007829|PDB:3LDV"
FT   HELIX           89..91
FT                   /evidence="ECO:0007829|PDB:3LDV"
FT   HELIX           93..103
FT                   /evidence="ECO:0007829|PDB:3LDV"
FT   HELIX           104..109
FT                   /evidence="ECO:0007829|PDB:3LDV"
FT   STRAND          112..116
FT                   /evidence="ECO:0007829|PDB:3LDV"
FT   HELIX           124..129
FT                   /evidence="ECO:0007829|PDB:3LDV"
FT   HELIX           136..149
FT                   /evidence="ECO:0007829|PDB:3LDV"
FT   STRAND          153..156
FT                   /evidence="ECO:0007829|PDB:3LDV"
FT   HELIX           159..169
FT                   /evidence="ECO:0007829|PDB:3LDV"
FT   STRAND          173..178
FT                   /evidence="ECO:0007829|PDB:3LDV"
FT   STRAND          191..193
FT                   /evidence="ECO:0007829|PDB:3LDV"
FT   HELIX           196..201
FT                   /evidence="ECO:0007829|PDB:3LDV"
FT   STRAND          205..209
FT                   /evidence="ECO:0007829|PDB:3LDV"
FT   HELIX           211..214
FT                   /evidence="ECO:0007829|PDB:3LDV"
FT   HELIX           219..229
FT                   /evidence="ECO:0007829|PDB:3LDV"
SQ   SEQUENCE   231 AA;  25003 MW;  EB2E841A990B582C CRC64;
     MNDPKVIVAL DYDNLADALA FVDKIDPSTC RLKVGKEMFT LFGPDFVREL HKRGFSVFLD
     LKFHDIPNTC SKAVKAAAEL GVWMVNVHAS GGERMMAASR EILEPYGKER PLLIGVTVLT
     SMESADLQGI GILSAPQDHV LRLATLTKNA GLDGVVCSAQ EASLLKQHLG REFKLVTPGI
     RPAGSEQGDQ RRIMTPAQAI ASGSDYLVIG RPITQAAHPE VVLEEINSSL V