ID D7MHW1_ARALL Unreviewed; 578 AA.
AC D7MHW1;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 13-SEP-2023, entry version 64.
DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase {ECO:0000256|RuleBase:RU362120};
DE EC=1.1.1.49 {ECO:0000256|RuleBase:RU362120};
GN Name=G6PD1 {ECO:0000313|EMBL:EFH46708.1};
GN ORFNames=ARALYDRAFT_493636 {ECO:0000313|EMBL:EFH46708.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
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 (PubMed:15634201). The main function
CC of this enzyme is to provide reducing power (NADPH) and pentose
CC phosphates for fatty acid and nucleic acid synthesis which are involved
CC in membrane synthesis and cell division (PubMed:15634201).
CC {ECO:0000256|ARBA:ARBA00003940}.
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:0000256|ARBA:ARBA00000740,
CC ECO:0000256|RuleBase:RU362120};
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|RuleBase:RU362120}.
CC -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009975, ECO:0000256|RuleBase:RU362120}.
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DR EMBL; GL348719; EFH46708.1; -; Genomic_DNA.
DR RefSeq; XP_002870449.1; XM_002870403.1.
DR AlphaFoldDB; D7MHW1; -.
DR STRING; 81972.D7MHW1; -.
DR EnsemblPlants; fgenesh2_kg.7__3069__AT5G35790.1; fgenesh2_kg.7__3069__AT5G35790.1; fgenesh2_kg.7__3069__AT5G35790.1.
DR GeneID; 9306520; -.
DR Gramene; fgenesh2_kg.7__3069__AT5G35790.1; fgenesh2_kg.7__3069__AT5G35790.1; fgenesh2_kg.7__3069__AT5G35790.1.
DR KEGG; aly:9306520; -.
DR eggNOG; KOG0563; Eukaryota.
DR HOGENOM; CLU_013524_2_3_1; -.
DR OrthoDB; 312822at2759; -.
DR UniPathway; UPA00115; UER00408.
DR Proteomes; UP000008694; Unassembled WGS sequence.
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:EnsemblPlants.
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:SF13; GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE 1, CHLOROPLASTIC; 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|RuleBase:RU362120};
KW Glucose metabolism {ECO:0000256|ARBA:ARBA00022526,
KW ECO:0000256|RuleBase:RU362120}; NADP {ECO:0000256|RuleBase:RU362120};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362120};
KW Reference proteome {ECO:0000313|Proteomes:UP000008694}.
FT DOMAIN 97..275
FT /note="Glucose-6-phosphate dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF00479"
FT DOMAIN 278..572
FT /note="Glucose-6-phosphate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02781"
FT BINDING 270
FT /ligand="substrate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10005"
SQ SEQUENCE 578 AA; 65572 MW; 788342152D1688B0 CRC64;
MATHSMIIPS SSSSSSSALA AAATSPFKET LPLFGRSLTF QRKSCFSQVR LRFFAEKHSQ
LESSNGCATN FASLQDSEDH LTEEHVTKGE STLSITVVGA SGDLAKKKIF PALFALFYEG
CLPQDFSVFG YARSKLTHEE LRDMISSTLT CRIDQRENCA DKMDQFLKRC FYHSGQYNSE
EDFAELNTKL KEKEVGKLAN RLYYLSIPPN IFVDVVRCAS LRASSENGWT RVIVEKPFGR
DSESSGELTR CLKQYLTEEQ IFRIDHYLGK ELVENLSVLR FSNLVFEPLW SRNYIRNVQL
IFSEDFGTEG RGGYFDQYGI IRDIMQNHLL QILALFAMET PVSLDAEDIR SEKVKVLRSM
KPLLLENVVV GQYKGHNKGG KTYPGYTDDP TVPNHSLTPT FAAAAMFINN ARWDGVPFLM
KAGKALHTRG AEIRVQFRHV PGNLYKKNFA TNLDNATNEL VIRVQPDEGI YLRINNKVPG
LGMRLDRSDL NLLYRSRYPR EIPDAYERLL LDAIEGERRL FIRSDELDAA WDLFTPALKE
LEEKKIIPEL YPYGSRGPVG AHYLASKYNV RWGDLGEA
//
