G6PD_GLUOX
ID G6PD_GLUOX Reviewed; 489 AA.
AC Q5FUK8;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00966, ECO:0000303|PubMed:20676631};
DE Short=G6PD {ECO:0000255|HAMAP-Rule:MF_00966};
DE Short=G6PDH {ECO:0000303|PubMed:20676631};
DE EC=1.1.1.49 {ECO:0000255|HAMAP-Rule:MF_00966, ECO:0000269|PubMed:20676631};
GN Name=zwf {ECO:0000255|HAMAP-Rule:MF_00966};
GN OrderedLocusNames=GOX0145 {ECO:0000312|EMBL:AAW59938.1};
OS Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconobacter.
OX NCBI_TaxID=290633;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=621H;
RX PubMed=15665824; DOI=10.1038/nbt1062;
RA Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT oxydans.";
RL Nat. Biotechnol. 23:195-200(2005).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND
RP SUBUNIT.
RC STRAIN=621H;
RX PubMed=20676631; DOI=10.1007/s00253-010-2779-9;
RA Rauch B., Pahlke J., Schweiger P., Deppenmeier U.;
RT "Characterization of enzymes involved in the central metabolism of
RT Gluconobacter oxydans.";
RL Appl. Microbiol. Biotechnol. 88:711-718(2010).
CC -!- FUNCTION: Catalyzes the oxidation of glucose 6-phosphate to 6-
CC phosphogluconolactone. {ECO:0000255|HAMAP-Rule:MF_00966,
CC ECO:0000269|PubMed:20676631}.
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, ECO:0000269|PubMed:20676631};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.28 mM for glucose 6-phosphate {ECO:0000269|PubMed:20676631};
CC KM=26.4 uM for NADP(+) {ECO:0000269|PubMed:20676631};
CC KM=740 uM for NAD(+) {ECO:0000269|PubMed:20676631};
CC Vmax=47.6 umol/min/mg enzyme {ECO:0000269|PubMed:20676631};
CC Note=kcat is 44.1 sec(-1). Can use NAD or NADP in vitro, but
CC primarily functions in a NADP-dependent manner in vivo.
CC {ECO:0000269|PubMed:20676631};
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, ECO:0000305|PubMed:20676631}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20676631}.
CC -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family.
CC {ECO:0000255|HAMAP-Rule:MF_00966}.
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DR EMBL; CP000009; AAW59938.1; -; Genomic_DNA.
DR RefSeq; WP_011251741.1; NZ_LT900338.1.
DR AlphaFoldDB; Q5FUK8; -.
DR SMR; Q5FUK8; -.
DR STRING; 290633.GOX0145; -.
DR EnsemblBacteria; AAW59938; AAW59938; GOX0145.
DR KEGG; gox:GOX0145; -.
DR eggNOG; COG0364; Bacteria.
DR HOGENOM; CLU_013524_5_0_5; -.
DR OMA; PDEGIQM; -.
DR UniPathway; UPA00115; UER00408.
DR Proteomes; UP000006375; 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 1: Evidence at protein level;
KW Carbohydrate metabolism; Glucose metabolism; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..489
FT /note="Glucose-6-phosphate 1-dehydrogenase"
FT /id="PRO_0000434435"
FT ACT_SITE 243
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 50
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 151
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 181
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 219
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 238
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 341
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 346
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
SQ SEQUENCE 489 AA; 54478 MW; E72C4C4B31745C95 CRC64;
MEHFQQVEPF DYVIFGATGD LTMRKLLPAL YNRLRMGQIP DDACIIGAAR TELDREAYVA
RARDALERFL PSDILGPGLV ERFLARLDYV TLDSSREGPQ WDALKSLLAK AQPDRVRVYY
FATAPQLYGS ICENLNRYEL ITPTSRVVLE KPIGTNMATA TAINDGVGQY FPEKQIYRID
HYLGKETVQN VLALRFANPL MNAAWSGEHI ESVQITAVET VGVEGRAAYY DTSGALRDMI
QNHLLQVLCL VAMEAPDSLE ADAVRNAKLA VLNALRPITD ATAATETVRA QYTAGVVDGE
NVPGYLEELG KPSATETYAA IRAWVDTPRW KNVPFYIRTA KRSGKKVSEI VVTFRPAATT
MFGATPASNR LVLRIQPNEG VDLRLNVKNP ALDVFNLRTA DLDTSIRMEG GLPFPDSYER
LLLDAVRGDP VLFIRRDEVE AAWRWVEPIL EAWKHDKAPM QTYSAGSYGP EQATQLLASH
GDTWHEASE
