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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
 
 
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