PYRF_THEMA
ID PYRF_THEMA Reviewed; 201 AA.
AC Q9WYG7;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Orotidine 5'-phosphate decarboxylase;
DE EC=4.1.1.23;
DE AltName: Full=OMP decarboxylase;
DE Short=OMPDCase;
DE Short=OMPdecase;
GN Name=pyrF; OrderedLocusNames=TM_0332;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND SUBUNIT.
RG Joint center for structural genomics (JCSG);
RT "Crystal Structure of orotidine 5'-phosphate decarboxylase (TM0332) from
RT Thermotoga maritima at 2.00 A resolution.";
RL Submitted (JAN-2005) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate
CC (OMP) to uridine 5'-monophosphate (UMP). {ECO:0000250}.
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|PROSITE-ProRule:PRU10110};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC UMP from orotate: step 2/2.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the OMP decarboxylase family. Type 1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AE000512; AAD35419.1; -; Genomic_DNA.
DR PIR; F72390; F72390.
DR RefSeq; NP_228143.1; NC_000853.1.
DR RefSeq; WP_004083099.1; NZ_CP011107.1.
DR PDB; 1VQT; X-ray; 2.00 A; A=1-201.
DR PDBsum; 1VQT; -.
DR AlphaFoldDB; Q9WYG7; -.
DR SMR; Q9WYG7; -.
DR STRING; 243274.THEMA_03060; -.
DR EnsemblBacteria; AAD35419; AAD35419; TM_0332.
DR KEGG; tma:TM0332; -.
DR eggNOG; COG0284; Bacteria.
DR InParanoid; Q9WYG7; -.
DR OMA; YVKVGHN; -.
DR OrthoDB; 1150446at2; -.
DR UniPathway; UPA00070; UER00120.
DR EvolutionaryTrace; Q9WYG7; -.
DR Proteomes; UP000008183; 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 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..201
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /id="PRO_0000134595"
FT ACT_SITE 54
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10110"
FT BINDING 8
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 26
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 52..61
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:1VQT"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:1VQT"
FT HELIX 12..19
FT /evidence="ECO:0007829|PDB:1VQT"
FT STRAND 23..27
FT /evidence="ECO:0007829|PDB:1VQT"
FT HELIX 29..32
FT /evidence="ECO:0007829|PDB:1VQT"
FT HELIX 37..43
FT /evidence="ECO:0007829|PDB:1VQT"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:1VQT"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:1VQT"
FT HELIX 59..69
FT /evidence="ECO:0007829|PDB:1VQT"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:1VQT"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:1VQT"
FT HELIX 85..94
FT /evidence="ECO:0007829|PDB:1VQT"
FT STRAND 96..102
FT /evidence="ECO:0007829|PDB:1VQT"
FT HELIX 112..124
FT /evidence="ECO:0007829|PDB:1VQT"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:1VQT"
FT HELIX 133..139
FT /evidence="ECO:0007829|PDB:1VQT"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:1VQT"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:1VQT"
FT HELIX 167..170
FT /evidence="ECO:0007829|PDB:1VQT"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:1VQT"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:1VQT"
FT HELIX 181..184
FT /evidence="ECO:0007829|PDB:1VQT"
FT HELIX 189..196
FT /evidence="ECO:0007829|PDB:1VQT"
SQ SEQUENCE 201 AA; 22809 MW; 4C2FAD77302F206D CRC64;
MTPVLSLDME DPIRFIDENG SFEVVKVGHN LAIHGKKIFD ELAKRNLKII LDLKFCDIPS
TVERSIKSWD HPAIIGFTVH SCAGYESVER ALSATDKHVF VVVKLTSMEG SLEDYMDRIE
KLNKLGCDFV LPGPWAKALR EKIKGKILVP GIRMEVKADD QKDVVTLEEM KGIANFAVLG
REIYLSENPR EKIKRIKEMR L
