ID   G6PD_MEDSA              Reviewed;         515 AA.
AC   Q42919;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Glucose-6-phosphate 1-dehydrogenase, cytoplasmic isoform;
DE            Short=G6PD;
DE            EC=1.1.1.49 {ECO:0000250|UniProtKB:Q9LK23};
OS   Medicago sativa (Alfalfa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX   NCBI_TaxID=3879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Apollo;
RX   PubMed=7640360; DOI=10.1007/bf00042073;
RA   Fahrendorf T., Ni W., Shorrosh B.S., Dixon R.A.;
RT   "Stress responses in alfalfa (Medicago sativa L.) XIX. Transcriptional
RT   activation of oxidative pentose phosphate pathway genes at the onset of the
RT   isoflavonoid phytoalexin response.";
RL   Plant Mol. Biol. 28:885-900(1995).
CC   -!- FUNCTION: Catalyzes the rate-limiting step of the oxidative pentose-
CC       phosphate pathway, which represents a route for the dissimilation of
CC       carbohydrates besides glycolysis. The main function of this enzyme is
CC       to provide reducing power (NADPH) and pentose phosphates for fatty acid
CC       and nucleic acid synthesis (By similarity).
CC       {ECO:0000250|UniProtKB:Q9LK23}.
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;
CC         Evidence={ECO:0000250|UniProtKB:Q9LK23};
CC   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC       ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC       1/3. {ECO:0000305}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P11411}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q9LK23}.
CC   -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; U18238; AAB41552.1; -; mRNA.
DR   PIR; S57785; S57785.
DR   AlphaFoldDB; Q42919; -.
DR   SMR; Q42919; -.
DR   UniPathway; UPA00115; UER00408.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IEA:UniProt.
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   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Cytoplasm; Glucose metabolism; NADP;
KW   Oxidoreductase.
FT   CHAIN           1..515
FT                   /note="Glucose-6-phosphate 1-dehydrogenase, cytoplasmic
FT                   isoform"
FT                   /id="PRO_0000068100"
FT   ACT_SITE        274
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P11411"
FT   BINDING         36..43
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P11413"
FT   BINDING         71
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P11413"
FT   BINDING         155
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P11413"
FT   BINDING         182
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P11413"
FT   BINDING         182
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P11413"
FT   BINDING         212..216
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P11413"
FT   BINDING         250
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P11413"
FT   BINDING         269
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P11413"
FT   BINDING         360
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P11413"
FT   BINDING         365
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P11413"
FT   BINDING         396
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P11413"
SQ   SEQUENCE   515 AA;  58923 MW;  836C1B96F2709FC7 CRC64;
     MGTNEWHVER RDSIGTESPV AREVLETGTL SIVVLGASGD LAKKKTFPAL FHLYKQELLP
     PDEVHIFGYA RSKISDDELR NKLRSYLVPE KGASPKQLDD VSKFLQLVKY VSGPYDSEDG
     FRLLDKEISE HEYLKNSKEG SSRRLFYLAL PPSVYPSVCK MIKTCCMNKS DLGGWTRVVV
     EKPFGRDLES AEELSTQIGE LFEEPQIYRI DHYLGKELVQ NMLVLRFANR FFLPLWNHNH
     IDNVQIVFRE DFGTDGRGGY FDQYGIIRDI IPNHLLQVLC LIAMEKPVSL KPEHIRDEKV
     KVLESVLPIR DDEVVLGQYE GYTDDPTVPD DSNTPTFATT ILRIHNERWE GVPFIVKAGK
     ALNSRKAEIR VQFKDVPGDI FRSKKQGRNE FVIRLQPSEA IYMKLTVKQP GLEMSAVQSE
     LDLSYGQRYQ GITIPEAYER LILDTIRGDQ QHFVRRDELK ASWQIFTPLL HKIDRGELKP
     VPYNPGSRGP AEADELLEKA GYVQTPGYIW IPPTL