ID G6PD_BUCBP Reviewed; 490 AA.
AC Q89AI7;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 121.
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=bbp_298;
OS Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=224915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bp;
RX PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT "Reductive genome evolution in Buchnera aphidicola.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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; AE016826; AAO27023.1; -; Genomic_DNA.
DR RefSeq; WP_011091424.1; NC_004545.1.
DR AlphaFoldDB; Q89AI7; -.
DR SMR; Q89AI7; -.
DR STRING; 224915.bbp_298; -.
DR KEGG; bab:bbp_298; -.
DR eggNOG; COG0364; Bacteria.
DR HOGENOM; CLU_013524_5_0_6; -.
DR OrthoDB; 9802739at2; -.
DR UniPathway; UPA00115; UER00408.
DR Proteomes; UP000000601; 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 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; Glucose metabolism; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..490
FT /note="Glucose-6-phosphate 1-dehydrogenase"
FT /id="PRO_0000068114"
FT ACT_SITE 237
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 48
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 90..91
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 145
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 179
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 213
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 232
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 340
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 345
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
SQ SEQUENCE 490 AA; 57318 MW; F5EE7D9055965AD9 CRC64;
MKNKNSGYDL VIFGAKGDLS CRKLLPSLYQ LEKKNKLCTH TRIIGVGRAN WDKIIYTNVV
YKSLIKFLNE TIIESIWKKF SSRLEFCNLD INCLHNFKKL KQIIQQNNNI IINYLAMPPH
TFGNICLGLE SINLNLEPTR IIIEKPLGSS LKTSININNK IGKFFKEKQI FRIDHYLGKE
TIQNLLAFRF SNSLFYYNWN NKFIDHVQIT VSETIGVEGR FNYFDTVGQI KDMVQNHLLQ
ILTITTMSTP IDCHENSIRD EKVKILKSLR PFNINNIHKN VILGQYTSGI INQKKVKSYL
DETNNQEYQM NKYTETFVSM KIYIDNDQWS GVPFYLRTGK RLPKKCSEIV IFFKTPPLNI
FSKNYNTLSK NKLILSLQPN EAIKIYILNK KPKLTSQYKL DLITLDFNYS KFYKKIQLSD
AYEKLLLESM KGIQSLFVRR DEVELAWKWI DSTLQCLHLK PRLPDLYPAG TWGPARSKTM
INNDGYEWNE
//
