ID B3RD98_CUPTR Unreviewed; 485 AA.
AC B3RD98;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 94.
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=zwf2 {ECO:0000313|EMBL:CAQ72873.1};
GN Synonyms=zwf {ECO:0000256|HAMAP-Rule:MF_00966};
GN OrderedLocusNames=RALTA_B2296 {ECO:0000313|EMBL:CAQ72873.1};
OS Cupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CCUG 44338 / CIP
OS 107171 / LMG 19424 / R1) (Ralstonia taiwanensis (strain LMG 19424)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=977880 {ECO:0000313|EMBL:CAQ72873.1, ECO:0000313|Proteomes:UP000001692};
RN [1] {ECO:0000313|EMBL:CAQ72873.1, ECO:0000313|Proteomes:UP000001692}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17343 / BCRC 17206 / CCUG 44338 / CIP 107171 / LMG 19424 /
RC R1 {ECO:0000313|Proteomes:UP000001692};
RX PubMed=18490699; DOI=10.1101/gr.076448.108;
RA Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D.,
RA Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V.,
RA Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C.,
RA Masson-Boivin C.;
RT "Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and
RT comparative genomics of rhizobia.";
RL Genome Res. 18:1472-1483(2008).
CC -!- FUNCTION: Catalyzes the oxidation of glucose 6-phosphate to 6-
CC phosphogluconolactone. {ECO:0000256|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:0000256|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:0000256|ARBA:ARBA00004937, ECO:0000256|HAMAP-Rule:MF_00966}.
CC -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009975, ECO:0000256|HAMAP-Rule:MF_00966}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00966}.
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DR EMBL; CU633750; CAQ72873.1; -; Genomic_DNA.
DR RefSeq; WP_012357085.1; NC_010530.1.
DR AlphaFoldDB; B3RD98; -.
DR GeneID; 29765607; -.
DR KEGG; cti:RALTA_B2296; -.
DR eggNOG; COG0364; Bacteria.
DR HOGENOM; CLU_013524_5_0_4; -.
DR BioCyc; CTAI977880:RALTA_RS26630-MONOMER; -.
DR UniPathway; UPA00115; UER00408.
DR Proteomes; UP000001692; Chromosome 2.
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 Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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 NCBIfam; TIGR00871; zwf; 1.
DR PANTHER; PTHR23429:SF0; GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE; 1.
DR PANTHER; PTHR23429; GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE G6PD; 1.
DR Pfam; PF02781; G6PD_C; 1.
DR Pfam; PF00479; G6PD_N; 1.
DR PIRSF; PIRSF000110; G6PD; 1.
DR PRINTS; PR00079; G6PDHDRGNASE.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00069; G6P_DEHYDROGENASE; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_00966};
KW Glucose metabolism {ECO:0000256|ARBA:ARBA00022526, ECO:0000256|HAMAP-
KW Rule:MF_00966}; NADP {ECO:0000256|HAMAP-Rule:MF_00966};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00966}.
FT DOMAIN 7..183
FT /note="Glucose-6-phosphate dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF00479"
FT DOMAIN 185..482
FT /note="Glucose-6-phosphate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02781"
FT ACT_SITE 236
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 10..17
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 44
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 144
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966,
FT ECO:0000256|PROSITE-ProRule:PRU10005"
FT BINDING 212
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 231
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT BINDING 336
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
SQ SEQUENCE 485 AA; 54339 MW; 59ED248ABD0BEAF6 CRC64;
MPDFDMVLFG GTGDLARRKL LPSLFDAHHA GLLHPAARIL ATGSQSMSSA DYVASLEQTV
RPALAHAPPE SWDRFCARIV YVQADARVPA HFDALAGQLL SRKPEVVVCY LATAPHLFVS
ICEQLARTGL NTRHAPNVRI VLEKPLGHDL ESNEAINSAV AKFFAEEQIY RIDHYLGKES
VQNLMAIRFG NALFEPLWRR EWVQDVQITI AEELGVETRG DFYDRTGALR DMVQNHLLQL
LCMVAMEPPA SLSEDAIRDE KIKILKALKP ITPQDVAEKT VRGQYRSGAI GGKPVPGYLE
EAGIAADSRT ETFVAIKAEI ANWRWEGVPF YLRTGKRMQS RVAEIVIHFR DVPHAIFPRP
LTQSPQNRLV IQLQPEESIR LYCLVKQPGD TLELTPTSLD LDFANSFKVR RAGAYERLLL
DVIRGRLGLF VRRDEQVQAW RWVEPILDTW EASTVPPKPY TAGTWGPAAS SALMSRDGGL
WHEEA
//
