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G6PD_STRPN
ID   G6PD_STRPN              Reviewed;         495 AA.
AC   O54537;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   26-SEP-2001, sequence version 2.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Glucose-6-phosphate 1-dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00966};
DE            Short=G6PD {ECO:0000255|HAMAP-Rule:MF_00966};
DE            EC=1.1.1.49 {ECO:0000255|HAMAP-Rule:MF_00966};
GN   Name=zwf {ECO:0000255|HAMAP-Rule:MF_00966}; OrderedLocusNames=SP_1243;
OS   Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=170187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-334 / TIGR4;
RX   PubMed=11463916; DOI=10.1126/science.1061217;
RA   Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA   Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA   Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA   Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA   Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA   McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA   Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA   Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT   "Complete genome sequence of a virulent isolate of Streptococcus
RT   pneumoniae.";
RL   Science 293:498-506(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 281-433.
RC   STRAIN=ATCC 6323;
RX   PubMed=9466257; DOI=10.1046/j.1365-2958.1998.00658.x;
RA   Coffey T.J., Enright M.C., Daniels M., Morona J.K., Morona R.,
RA   Hryniewicz W., Paton J.C., Spratt B.G.;
RT   "Recombinational exchanges at the capsular polysaccharide biosynthetic
RT   locus lead to frequent serotype changes among natural isolates of
RT   Streptococcus pneumoniae.";
RL   Mol. Microbiol. 27:73-83(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 281-433.
RX   PubMed=9533725; DOI=10.1089/mdr.1998.4.51;
RA   Coffey T.J., Enright M.C., Daniels M., Wilkinson P., Berron S., Fenoll A.,
RA   Spratt B.G.;
RT   "Serotype 19A variants of the Spanish serotype 23F multiresistant clone of
RT   Streptococcus pneumoniae.";
RL   Microb. Drug Resist. 4:51-55(1998).
CC   -!- FUNCTION: Catalyzes the oxidation of glucose 6-phosphate to 6-
CC       phosphogluconolactone. {ECO:0000255|HAMAP-Rule:MF_00966}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-
CC         lactone + H(+) + NADPH; Xref=Rhea:RHEA:15841, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:57955, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:61548; EC=1.1.1.49; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00966};
CC   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC       ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC       1/3. {ECO:0000255|HAMAP-Rule:MF_00966}.
CC   -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00966}.
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DR   EMBL; AE005672; AAK75348.1; -; Genomic_DNA.
DR   EMBL; Z99802; CAB16927.1; -; Genomic_DNA.
DR   EMBL; Z99865; CAB16990.1; -; Genomic_DNA.
DR   PIR; C95144; C95144.
DR   RefSeq; WP_000096161.1; NZ_AKVY01000001.1.
DR   AlphaFoldDB; O54537; -.
DR   SMR; O54537; -.
DR   STRING; 170187.SP_1243; -.
DR   PRIDE; O54537; -.
DR   EnsemblBacteria; AAK75348; AAK75348; SP_1243.
DR   KEGG; spn:SP_1243; -.
DR   eggNOG; COG0364; Bacteria.
DR   OMA; VEICVYE; -.
DR   PhylomeDB; O54537; -.
DR   BioCyc; SPNE170187:G1FZB-1257-MON; -.
DR   UniPathway; UPA00115; UER00408.
DR   Proteomes; UP000000585; Chromosome.
DR   GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00966; G6PD; 1.
DR   InterPro; IPR001282; G6P_DH.
DR   InterPro; IPR019796; G6P_DH_AS.
DR   InterPro; IPR022675; G6P_DH_C.
DR   InterPro; IPR022674; G6P_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR23429; PTHR23429; 1.
DR   Pfam; PF02781; G6PD_C; 1.
DR   Pfam; PF00479; G6PD_N; 1.
DR   PIRSF; PIRSF000110; G6PD; 1.
DR   PRINTS; PR00079; G6PDHDRGNASE.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR00871; zwf; 1.
DR   PROSITE; PS00069; G6P_DEHYDROGENASE; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Glucose metabolism; NADP; Oxidoreductase.
FT   CHAIN           1..495
FT                   /note="Glucose-6-phosphate 1-dehydrogenase"
FT                   /id="PRO_0000068133"
FT   ACT_SITE        239
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT   BINDING         11..18
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT   BINDING         45
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT   BINDING         84..85
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT   BINDING         147
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT   BINDING         177
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT   BINDING         181
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT   BINDING         215
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT   BINDING         234
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT   BINDING         339
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT   BINDING         344
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT   CONFLICT        348
FT                   /note="V -> I (in Ref. 2 and 3)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   495 AA;  56790 MW;  99093E9C8929FFAF CRC64;
     MSSKVIVTIF GASGDLAKRK LYPSLFRLYQ SGNLSKHFAV IGTARRPWSK EYFESVVVES
     ILDLADSTEQ AQEFASHFYY QSHDVNDSEH YIALRQLQAE LNEKYQAEHN KLFFLSMAPQ
     FFGTIAKHLK SENIVDGKGF ERLIVEKPFG TDYATASKLN DELLATFDEE QIFRIDHYLG
     KEMIQSIFAV RFANLIFENV WNKDFIDNVQ ITFAERLGVE ERGGYYDQSG ALRDMVQNHT
     LQLLSLLAMD KPASFTKDEI RAEKIKVFKN LYHPTDEELK EHFIRGQYRS GKIDGMKYIS
     YRSEPNVNPE STTETFTSGA FFVDSDRFRG VPFFFRTGKR LTEKGTHVNI VFKQMDSIFG
     EPLAPNILTI YIQPTEGFSL SLNGKQVGEE FNLAPNSLDY RTDATATGAS PEPYEKLIYD
     VLNNNSTNFS HWDEVCASWK LIDRIEKLWA ENGAPLHDYK AGSMGPQASF DLLEKFGAKW
     TWQPDITYRQ DGRLE
 
 
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