(data stored in ACNUC7421 zone)

SWISSPROT: C6B1I7_RHILS

ID   C6B1I7_RHILS            Unreviewed;       491 AA.
AC   C6B1I7;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 60.
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=Rleg_0395 {ECO:0000313|EMBL:ACS54706.1};
OS   Rhizobium leguminosarum bv. trifolii (strain WSM1325).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=395491 {ECO:0000313|EMBL:ACS54706.1, ECO:0000313|Proteomes:UP000002256};
RN   [1] {ECO:0000313|EMBL:ACS54706.1, ECO:0000313|Proteomes:UP000002256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM1325 {ECO:0000313|EMBL:ACS54706.1,
RC   ECO:0000313|Proteomes:UP000002256};
RX   PubMed=21304718;
RA   Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K.,
RA   Tiwari R., Copeland A., Nolan M., Han C., Brettin T., Land M.,
RA   Ovchinikova G., Ivanova N., Mavromatis K., Markowitz V., Kyrpides N.,
RA   Melino V., Denton M., Yates R., Howieson J.;
RT   "Complete genome sequence of Rhizobium leguminosarum bv. trifolii
RT   strain WSM1325, an effective microsymbiont of annual Mediterranean
RT   clovers.";
RL   Stand. Genomic Sci. 2:347-356(2010).
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; CP001622; ACS54706.1; -; Genomic_DNA.
DR   RefSeq; WP_012756097.1; NC_012850.1.
DR   ProteinModelPortal; C6B1I7; -.
DR   EnsemblBacteria; ACS54706; ACS54706; Rleg_0395.
DR   KEGG; rlg:Rleg_0395; -.
DR   HOGENOM; HOG000046192; -.
DR   KO; K00036; -.
DR   OMA; VEICVYE; -.
DR   OrthoDB; POG091H04ZM; -.
DR   UniPathway; UPA00115; UER00408.
DR   Proteomes; UP000002256; 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; C6B1I7.
DR   SWISS-2DPAGE; C6B1I7.
KW   Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_00966};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002256};
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:ACS54706.1}.
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;  55271 MW;  89F5E0F45416A736 CRC64;
     MSSQIIPVEP FDYVVFGGSG DLAERKLLPA LYHRQIEGQF SEPTRVIGAS RSPLTHEEYR
     KFAKDALNEH LKKGEYDEAE VEKFCARLYY VSVDARTDAG WDQLKKLLDE GKDRVRAFYL
     AVAPGIFGDI SQKIHDHKLI TKSTRIVVEK PIGRDLASAL QLNDTIGRAF KEEQIFRIDH
     YLGKETVQNL MALRFANALY EPLWNANYID HVQITVAESV GLEGRAGYYD TAGALRDMVQ
     NHILQLLCLT AMEVPSSMDS EAVRDEKLKV LRALKPLNAS NVEQATVRGQ YRAGASGSGP
     VKGYLEELEG GVSNTETFVA IKAEINNWRW AGVPFYIRTG KRLTGRMSEI VITFKPIPHA
     IFDQAAGRIN ANQLIIRLQP DEGVKQSLMI KDPGPGGMRL RNVSLDMSFA QAFNVRNPDA
     YERLLMDVIR SNQTLFMRRD EVEAAWKWVD PILKGWETTG QQVQGYTAGT WGPSQAIALI
     ERDGRTWHDE I
//

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