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ULAD_SALPA
ID   ULAD_SALPA              Reviewed;         216 AA.
AC   Q5PJ63;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=3-keto-L-gulonate-6-phosphate decarboxylase UlaD {ECO:0000255|HAMAP-Rule:MF_01267};
DE            EC=4.1.1.85 {ECO:0000255|HAMAP-Rule:MF_01267};
DE   AltName: Full=3-dehydro-L-gulonate-6-phosphate decarboxylase {ECO:0000255|HAMAP-Rule:MF_01267};
DE   AltName: Full=KGPDC {ECO:0000255|HAMAP-Rule:MF_01267};
DE   AltName: Full=L-ascorbate utilization protein D {ECO:0000255|HAMAP-Rule:MF_01267};
GN   Name=ulaD {ECO:0000255|HAMAP-Rule:MF_01267}; OrderedLocusNames=SPA4203;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
CC   -!- FUNCTION: Catalyzes the decarboxylation of 3-keto-L-gulonate-6-P into
CC       L-xylulose-5-P. Is involved in the anaerobic L-ascorbate utilization.
CC       {ECO:0000255|HAMAP-Rule:MF_01267}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-dehydro-L-gulonate 6-phosphate + H(+) = CO2 + L-xylulose 5-
CC         phosphate; Xref=Rhea:RHEA:14353, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57829, ChEBI:CHEBI:58774; EC=4.1.1.85;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01267};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01267};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01267};
CC   -!- PATHWAY: Cofactor degradation; L-ascorbate degradation; D-xylulose 5-
CC       phosphate from L-ascorbate: step 2/4. {ECO:0000255|HAMAP-
CC       Rule:MF_01267}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01267}.
CC   -!- INDUCTION: Induced by L-ascorbate. Repressed by UlaR.
CC       {ECO:0000255|HAMAP-Rule:MF_01267}.
CC   -!- SIMILARITY: Belongs to the HPS/KGPDC family. KGPDC subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01267}.
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DR   EMBL; CP000026; AAV79940.1; -; Genomic_DNA.
DR   RefSeq; WP_000056761.1; NC_006511.1.
DR   AlphaFoldDB; Q5PJ63; -.
DR   SMR; Q5PJ63; -.
DR   EnsemblBacteria; AAV79940; AAV79940; SPA4203.
DR   KEGG; spt:SPA4203; -.
DR   HOGENOM; CLU_081825_0_0_6; -.
DR   OMA; WEQAQEW; -.
DR   UniPathway; UPA00263; UER00378.
DR   Proteomes; UP000008185; Chromosome.
DR   GO; GO:0033982; F:3-dehydro-L-gulonate-6-phosphate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IEA:InterPro.
DR   GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR   GO; GO:0019854; P:L-ascorbic acid catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd04726; KGPDC_HPS; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_01267; UlaD; 1.
DR   InterPro; IPR023942; 3-keto-L-gulonate6Pdecase_UlaD.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR041710; HPS/KGPDC.
DR   InterPro; IPR001754; OMPdeCOase_dom.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   Pfam; PF00215; OMPdecase; 1.
DR   SMART; SM00934; OMPdecase; 1.
DR   SUPFAM; SSF51366; SSF51366; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Decarboxylase; Lyase; Magnesium; Metal-binding.
FT   CHAIN           1..216
FT                   /note="3-keto-L-gulonate-6-phosphate decarboxylase UlaD"
FT                   /id="PRO_0000236092"
FT   BINDING         11
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01267"
FT   BINDING         33
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01267"
FT   BINDING         62
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01267"
FT   BINDING         192
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01267"
FT   SITE            64
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01267"
FT   SITE            67
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01267"
SQ   SEQUENCE   216 AA;  23706 MW;  CDF280DC1D1BAD68 CRC64;
     MSLPMLQVAL DNQTMDSAYE TTRLIAEEVD IIEVGTILCV GEGVRAVRDL KALYPHKIVL
     ADAKIADAGK ILSRMCFEAN ADWVTVICCA DINTAKGALD VAKEFNGDVQ IELTGYWTWE
     QAQQWRDAGI QQVVYHRSRD AQAAGVAWGE ADITAIKRLS DMGFKVTVTG GLALEDLPLF
     KGIPIHVFIA GRSIRDAESP VEAARQFKRS IAQLWG
 
 
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