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PYRF_CLOAB
ID   PYRF_CLOAB              Reviewed;         286 AA.
AC   Q97FS5;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   25-MAY-2022, entry version 104.
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=CA_C2652;
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS   / VKM B-1787).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA   Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA   Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA   Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA   Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
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   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       UMP from orotate: step 2/2.
CC   -!- SIMILARITY: Belongs to the OMP decarboxylase family. Type 2 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE001437; AAK80599.1; -; Genomic_DNA.
DR   PIR; D97226; D97226.
DR   RefSeq; NP_349259.1; NC_003030.1.
DR   RefSeq; WP_010965940.1; NC_003030.1.
DR   AlphaFoldDB; Q97FS5; -.
DR   SMR; Q97FS5; -.
DR   STRING; 272562.CA_C2652; -.
DR   DNASU; 1118835; -.
DR   EnsemblBacteria; AAK80599; AAK80599; CA_C2652.
DR   GeneID; 44999120; -.
DR   KEGG; cac:CA_C2652; -.
DR   PATRIC; fig|272562.8.peg.2841; -.
DR   eggNOG; COG0284; Bacteria.
DR   HOGENOM; CLU_060704_1_1_9; -.
DR   OMA; QSAFFER; -.
DR   OrthoDB; 1181405at2; -.
DR   UniPathway; UPA00070; UER00120.
DR   Proteomes; UP000000814; 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_01215; OMPdecase_type2; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR018089; OMPdecase_AS.
DR   InterPro; IPR011995; OMPdecase_type-2.
DR   InterPro; IPR001754; OMPdeCOase_dom.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   PANTHER; PTHR43375; PTHR43375; 1.
DR   Pfam; PF00215; OMPdecase; 1.
DR   SMART; SM00934; OMPdecase; 1.
DR   SUPFAM; SSF51366; SSF51366; 1.
DR   TIGRFAMs; TIGR02127; pyrF_sub2; 1.
DR   PROSITE; PS00156; OMPDECASE; 1.
PE   3: Inferred from homology;
KW   Decarboxylase; Lyase; Pyrimidine biosynthesis; Reference proteome.
FT   CHAIN           1..286
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /id="PRO_0000134622"
FT   ACT_SITE        97
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   286 AA;  32241 MW;  5BC7E3ACBD5FF2A4 CRC64;
     MIIDRLFDSV EKKGHVCLGL DTDITYVPEE FCKKFNSIED AIFNFNKKII DATLDVVSCY
     KVQIAYYEAY GLKGLLAYKR TLEYLREKKA IAIADIKRGD IAKTAEMYAK AHFEGDFEAD
     FVTLNPYMGL DGIEPYMPYI EKMEKGLFIL LRTSNKGAYD IQYIKTQGGK NVYDEVGEKI
     YDLGQKATGR SKYSSIGAVV GCTHVEEGVE IRNKFKNMFF LIPGYGAQGG TAKEVSLYLR
     EGNGGVVNSS RGILLAYKKE ENGEKIFDEC ARLAAINMRD EIRKTL
 
 
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