PYRF_COXBU
ID PYRF_COXBU Reviewed; 236 AA.
AC Q83E06;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=CBU_0531;
OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=227377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSA 493 / Nine Mile phase I;
RX PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA Fraser C.M., Heidelberg J.F.;
RT "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(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; AE016828; AAO90077.1; -; Genomic_DNA.
DR RefSeq; NP_819563.1; NC_002971.3.
DR RefSeq; WP_005771152.1; NZ_CCYB01000050.1.
DR PDB; 3TR2; X-ray; 2.00 A; A/B=1-236.
DR PDBsum; 3TR2; -.
DR AlphaFoldDB; Q83E06; -.
DR SMR; Q83E06; -.
DR STRING; 227377.CBU_0531; -.
DR DNASU; 1208416; -.
DR EnsemblBacteria; AAO90077; AAO90077; CBU_0531.
DR GeneID; 1208416; -.
DR KEGG; cbu:CBU_0531; -.
DR PATRIC; fig|227377.7.peg.526; -.
DR eggNOG; COG0284; Bacteria.
DR HOGENOM; CLU_067069_0_0_6; -.
DR OMA; NFKIFLD; -.
DR UniPathway; UPA00070; UER00120.
DR EvolutionaryTrace; Q83E06; -.
DR Proteomes; UP000002671; Chromosome.
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..236
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /id="PRO_0000134538"
FT ACT_SITE 64
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 13
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 35
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 62..71
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 123
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 8..11
FT /evidence="ECO:0007829|PDB:3TR2"
FT HELIX 17..24
FT /evidence="ECO:0007829|PDB:3TR2"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:3TR2"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:3TR2"
FT HELIX 38..54
FT /evidence="ECO:0007829|PDB:3TR2"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:3TR2"
FT HELIX 69..81
FT /evidence="ECO:0007829|PDB:3TR2"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:3TR2"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:3TR2"
FT HELIX 95..106
FT /evidence="ECO:0007829|PDB:3TR2"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:3TR2"
FT HELIX 127..132
FT /evidence="ECO:0007829|PDB:3TR2"
FT HELIX 139..153
FT /evidence="ECO:0007829|PDB:3TR2"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:3TR2"
FT HELIX 162..169
FT /evidence="ECO:0007829|PDB:3TR2"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:3TR2"
FT HELIX 199..205
FT /evidence="ECO:0007829|PDB:3TR2"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:3TR2"
FT HELIX 214..217
FT /evidence="ECO:0007829|PDB:3TR2"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:3TR2"
FT HELIX 222..232
FT /evidence="ECO:0007829|PDB:3TR2"
SQ SEQUENCE 236 AA; 25849 MW; 6299A5996F538ECA CRC64;
MEKPDPKVIV AIDAGTVEQA RAQINPLTPE LCHLKIGSIL FTRYGPAFVE ELMQKGYRIF
LDLKFYDIPQ TVAGACRAVA ELGVWMMNIH ISGGRTMMET VVNALQSITL KEKPLLIGVT
ILTSLDGSDL KTLGIQEKVP DIVCRMATLA KSAGLDGVVC SAQEAALLRK QFDRNFLLVT
PGIRLETDEK GDQKRVMTPR AAIQAGSDYL VIGRPITQST DPLKALEAID KDIKTR