(data stored in ACNUC7421 zone)

SWISSPROT: C3MGK2_SINFN

ID   C3MGK2_SINFN            Unreviewed;       491 AA.
AC   C3MGK2;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   07-JUN-2017, entry version 56.
DE   RecName: Full=Glucose-6-phosphate 1-dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00966};
DE            Short=G6PD {ECO:0000256|HAMAP-Rule:MF_00966};
DE            EC=1.1.1.49 {ECO:0000256|HAMAP-Rule:MF_00966};
GN   Name=zwf {ECO:0000256|HAMAP-Rule:MF_00966};
GN   OrderedLocusNames=NGR_c03190 {ECO:0000313|EMBL:ACP24117.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP24117.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP24117.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
CC   -!- FUNCTION: Catalyzes the oxidation of glucose 6-phosphate to 6-
CC       phosphogluconolactone. {ECO:0000256|HAMAP-Rule:MF_00966}.
CC   -!- CATALYTIC ACTIVITY: D-glucose 6-phosphate + NADP(+) = 6-phospho-D-
CC       glucono-1,5-lactone + NADPH. {ECO:0000256|HAMAP-Rule:MF_00966}.
CC   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC       ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage):
CC       step 1/3. {ECO:0000256|HAMAP-Rule:MF_00966}.
CC   -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase
CC       family. {ECO:0000256|HAMAP-Rule:MF_00966}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00966}.
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DR   EMBL; CP001389; ACP24117.1; -; Genomic_DNA.
DR   RefSeq; WP_012706902.1; NC_012587.1.
DR   RefSeq; YP_002824870.1; NC_012587.1.
DR   STRING; 394.NGR_c03190; -.
DR   EnsemblBacteria; ACP24117; ACP24117; NGR_c03190.
DR   GeneID; 7790897; -.
DR   KEGG; rhi:NGR_c03190; -.
DR   PATRIC; fig|394.7.peg.3122; -.
DR   eggNOG; ENOG4105D8W; Bacteria.
DR   eggNOG; COG0364; LUCA.
DR   HOGENOM; HOG000046191; -.
DR   KO; K00036; -.
DR   OMA; FQLLAMV; -.
DR   OrthoDB; POG091H04ZM; -.
DR   UniPathway; UPA00115; UER00408.
DR   Proteomes; UP000001054; Chromosome.
DR   GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0050661; F:NADP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-HAMAP.
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; IPR016040; NAD(P)-bd_dom.
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;
DR   PRODOM; C3MGK2.
DR   SWISS-2DPAGE; C3MGK2.
KW   Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_00966};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
KW   Glucose metabolism {ECO:0000256|HAMAP-Rule:MF_00966};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_00966};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00966,
KW   ECO:0000313|EMBL:ACP24117.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054}.
FT   DOMAIN       14    189       G6PD_N. {ECO:0000259|Pfam:PF00479}.
FT   DOMAIN      191    488       G6PD_C. {ECO:0000259|Pfam:PF02781}.
FT   ACT_SITE    242    242       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00966}.
FT   BINDING      51     51       NADP. {ECO:0000256|HAMAP-Rule:MF_00966}.
FT   BINDING     150    150       NADP. {ECO:0000256|HAMAP-Rule:MF_00966}.
FT   BINDING     180    180       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00966}.
FT   BINDING     184    184       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00966}.
FT   BINDING     218    218       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00966}.
FT   BINDING     237    237       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00966}.
FT   BINDING     341    341       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00966}.
SQ   SEQUENCE   491 AA;  55014 MW;  2530A7F646899032 CRC64;
     MSSQIIPVEP FDYVVFGGTG DLAERKLLPA LYHRQIEGQF SEPTRIIGAS RAALTDGEYR
     QFASDALKEH LKPGEFDEAE VETFTSRLHY VSVDAKSEQG WDDLKKILDE GKDRTRAFYL
     AVGPAIFGDI SEKIRDHKLI TRNTRIVVEK PIGRDLASAT ELNDTIGKVF REEQIFRIDH
     YLGKETVQNL MALRFANALY EPLWNSAHID HVQITVAESV GLENRAGYYD KAGALRDMVQ
     NHILQLVCFV AMEAPTSMDA EAVRDEKLKV LRALKPITAA NVEQVTVRGQ YRAGASAGGP
     VKGYLEELEG GVSNTETFVA IKAEISNWRW AGVPFYIRTG KRMAGRMSEI VITFKQIPHS
     IFDNSAGRIS ANQLMIRLQP NEGVKQSLMI KDPGPGGMRL RNVPLDMSFA EAFGVRNADA
     YERLLLDVIR NNQTLFVRRD EVEAAWQWID PILKAWETAG QQVQGYTAGT WGPSQAIALI
     ERDGRTWNDT I
//

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