ID   G6PD_BUCAI              Reviewed;         491 AA.
AC   P57405;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   27-MAR-2024, entry version 122.
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=BU320;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
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; BA000003; BAB13028.1; -; Genomic_DNA.
DR   RefSeq; NP_240142.1; NC_002528.1.
DR   RefSeq; WP_010896065.1; NC_002528.1.
DR   AlphaFoldDB; P57405; -.
DR   SMR; P57405; -.
DR   STRING; 563178.BUAP5A_313; -.
DR   EnsemblBacteria; BAB13028; BAB13028; BAB13028.
DR   KEGG; buc:BU320; -.
DR   PATRIC; fig|107806.10.peg.332; -.
DR   eggNOG; COG0364; Bacteria.
DR   HOGENOM; CLU_013524_5_0_6; -.
DR   UniPathway; UPA00115; UER00408.
DR   Proteomes; UP000001806; 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..491
FT                   /note="Glucose-6-phosphate 1-dehydrogenase"
FT                   /id="PRO_0000068112"
FT   ACT_SITE        238
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT   BINDING         49
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT   BINDING         91..92
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT   BINDING         146
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT   BINDING         176
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT   BINDING         180
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT   BINDING         214
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT   BINDING         233
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT   BINDING         338
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT   BINDING         343
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
SQ   SEQUENCE   491 AA;  57218 MW;  3DFAE2D26EB690F2 CRC64;
     MIIETNHACD LVIFGAKGDL TKRKLLPALY KLEKSKKIHK YTRIIASGRA DWSTEDYIEK
     IKTEVKNFLN EEINDLIWKN LSSRIFFCNI DVHEPLHFFR LKTILKQKKN IIVYYCAVPS
     NTLNSIFIGL GNAHLNSVPS RIVLEKPLGV CLKTSKKIND QISKYFLESQ IFRIDHYLGK
     ESILNLFALR FSNTCLFYNW NNKTIDHIQI TVSEEVGIED RWNYFNMMGQ MKDMVQNHLL
     QILTILTMDQ PKNISSESIQ HEKVKILRSL NPINIHNINK KTVRGQYCSG VINEKKVPSY
     LEENGANKNS LTETFVAIKV DLNNKQWSGV PFYLRTGKRL AHKYSEIVVF FKKKPTNLFK
     NLNSELLQNK LIIRLEPNPN IIFDFSVKAP GLEQEYKIEN SQLKSSQFSK KYSKNSIDAY
     ERLLFEIMRG VQSLFVCRDE IEAAWKWIDP IIHAWKNSKN NAPQLYMSGT WGPKNSDLLL
     AHDGRVWYEF H
//