PYRF_GEOKA
ID PYRF_GEOKA Reviewed; 244 AA.
AC Q5L0U0;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=GK1155;
OS Geobacillus kaustophilus (strain HTA426).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=235909;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTA426;
RX PubMed=15576355; DOI=10.1093/nar/gkh970;
RA Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA Matsui S., Uchiyama I.;
RT "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT Geobacillus kaustophilus.";
RL Nucleic Acids Res. 32:6292-6303(2004).
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; BA000043; BAD75440.1; -; Genomic_DNA.
DR RefSeq; WP_011230655.1; NC_006510.1.
DR PDB; 2YYT; X-ray; 2.30 A; A/B/C/D=1-244.
DR PDB; 2YYU; X-ray; 2.20 A; A/B=1-244.
DR PDBsum; 2YYT; -.
DR PDBsum; 2YYU; -.
DR AlphaFoldDB; Q5L0U0; -.
DR SMR; Q5L0U0; -.
DR STRING; 235909.GK1155; -.
DR EnsemblBacteria; BAD75440; BAD75440; GK1155.
DR KEGG; gka:GK1155; -.
DR PATRIC; fig|235909.7.peg.1256; -.
DR eggNOG; COG0284; Bacteria.
DR HOGENOM; CLU_067069_1_1_9; -.
DR OMA; NFKIFLD; -.
DR UniPathway; UPA00070; UER00120.
DR EvolutionaryTrace; Q5L0U0; -.
DR Proteomes; UP000001172; 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 1: Evidence at protein level;
KW 3D-structure; Decarboxylase; Lyase; Pyrimidine biosynthesis;
KW Reference proteome.
FT CHAIN 1..244
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /id="PRO_0000241860"
FT ACT_SITE 61
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 10
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 32
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 59..68
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 213
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:2YYU"
FT HELIX 14..21
FT /evidence="ECO:0007829|PDB:2YYU"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:2YYU"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:2YYU"
FT HELIX 35..41
FT /evidence="ECO:0007829|PDB:2YYU"
FT HELIX 43..51
FT /evidence="ECO:0007829|PDB:2YYU"
FT STRAND 55..62
FT /evidence="ECO:0007829|PDB:2YYU"
FT HELIX 66..78
FT /evidence="ECO:0007829|PDB:2YYU"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:2YYU"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:2YYU"
FT HELIX 92..105
FT /evidence="ECO:0007829|PDB:2YYU"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:2YYU"
FT STRAND 114..120
FT /evidence="ECO:0007829|PDB:2YYU"
FT HELIX 126..131
FT /evidence="ECO:0007829|PDB:2YYU"
FT HELIX 139..153
FT /evidence="ECO:0007829|PDB:2YYU"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:2YYU"
FT HELIX 162..172
FT /evidence="ECO:0007829|PDB:2YYU"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:2YYU"
FT HELIX 199..205
FT /evidence="ECO:0007829|PDB:2YYU"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:2YYU"
FT HELIX 214..217
FT /evidence="ECO:0007829|PDB:2YYU"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:2YYU"
FT HELIX 222..232
FT /evidence="ECO:0007829|PDB:2YYU"
SQ SEQUENCE 244 AA; 26751 MW; 41AB5BFD1923C349 CRC64;
MHTPFIVALD FPSKQEVERF LRPFAGTPLF VKVGMELYYQ EGPAIVAFLK EQGHAVFLDL
KLHDIPNTVK QAMKGLARVG ADLVNVHAAG GRRMMEAAIE GLDAGTPSGR MRPRCIAVTQ
LTSTDERMLH EELWISRPLV ETVAHYAALA KESGLDGVVC SANEAAFIKE RCGASFLAVT
PGIRFADDAA HDQVRVVTPR KARALGSDYI VIGRSLTRAA DPLRTYARLQ HEWNGGERES
TTPT
