ID   G6PD6_ARATH             Reviewed;         515 AA.
AC   Q9FJI5; Q9SUJ9;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   27-MAR-2024, entry version 155.
DE   RecName: Full=Glucose-6-phosphate 1-dehydrogenase 6, cytoplasmic {ECO:0000305};
DE            Short=AtG6PD6 {ECO:0000303|PubMed:15634201};
DE            Short=G6PDH6 {ECO:0000305};
DE            EC=1.1.1.49 {ECO:0000269|PubMed:15634201};
GN   Name=G6PD6 {ECO:0000303|PubMed:15634201};
GN   Synonyms=ACG12 {ECO:0000303|PubMed:10437832};
GN   OrderedLocusNames=At5g40760 {ECO:0000312|EMBL:BAB08837.1};
GN   ORFNames=K1B16.1, MNF13.6;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10437832; DOI=10.1023/a:1006257230779;
RA   Wendt U.K., Hauschild R., Lange C., Pietersma M., Wenderoth I.,
RA   von Schaewen A.;
RT   "Evidence for functional convergence of redox regulation in G6PDH isoforms
RT   of cyanobacteria and higher plants.";
RL   Plant Mol. Biol. 40:487-494(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9872454; DOI=10.1093/dnares/5.5.297;
RA   Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT   features of the regions of 1,013,767 bp covered by sixteen physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:297-308(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA   Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT   features of the regions of 1,456,315 bp covered by nineteen physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:41-54(1998).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=15634201; DOI=10.1111/j.1365-313x.2004.02293.x;
RA   Wakao S., Benning C.;
RT   "Genome-wide analysis of glucose-6-phosphate dehydrogenases in
RT   Arabidopsis.";
RL   Plant J. 41:243-256(2005).
RN   [7]
RP   SUBCELLULAR LOCATION.
RX   PubMed=21309870; DOI=10.1111/j.1365-313x.2011.04535.x;
RA   Meyer T., Hoelscher C., Schwoeppe C., von Schaewen A.;
RT   "Alternative targeting of Arabidopsis plastidic glucose-6-phosphate
RT   dehydrogenase G6PD1 involves cysteine-dependent interaction with G6PD4 in
RT   the cytosol.";
RL   Plant J. 66:745-758(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:0000269|PubMed:15634201}.
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:0000269|PubMed:15634201};
CC   -!- ACTIVITY REGULATION: Regulated by metabolites.
CC       {ECO:0000250|UniProtKB:Q43839}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=6.5 mM for NADP {ECO:0000269|PubMed:15634201};
CC       pH dependence:
CC         Optimum pH is 8.0. {ECO:0000269|PubMed:15634201};
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: Forms homodimer. {ECO:0000250|UniProtKB:P11411}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:21309870}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, buds, flowers
CC       and siliques. {ECO:0000269|PubMed:15634201}.
CC   -!- MISCELLANEOUS: There are 6 glucose-6-phosphate 1-dehydrogenase genes in
CC       A.thaliana. {ECO:0000303|PubMed:14593172}.
CC   -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; AJ010971; CAB52675.1; -; mRNA.
DR   EMBL; AB015470; BAB08837.1; -; Genomic_DNA.
DR   EMBL; AB009052; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CP002688; AED94591.1; -; Genomic_DNA.
DR   EMBL; CP002688; ANM68628.1; -; Genomic_DNA.
DR   EMBL; BT004633; AAO42879.1; -; mRNA.
DR   PIR; T52610; T52610.
DR   RefSeq; NP_001330361.1; NM_001344352.1.
DR   RefSeq; NP_198892.1; NM_123441.3.
DR   AlphaFoldDB; Q9FJI5; -.
DR   SMR; Q9FJI5; -.
DR   STRING; 3702.Q9FJI5; -.
DR   iPTMnet; Q9FJI5; -.
DR   PaxDb; 3702-AT5G40760-1; -.
DR   ProteomicsDB; 248601; -.
DR   EnsemblPlants; AT5G40760.1; AT5G40760.1; AT5G40760.
DR   EnsemblPlants; AT5G40760.2; AT5G40760.2; AT5G40760.
DR   GeneID; 834076; -.
DR   Gramene; AT5G40760.1; AT5G40760.1; AT5G40760.
DR   Gramene; AT5G40760.2; AT5G40760.2; AT5G40760.
DR   KEGG; ath:AT5G40760; -.
DR   Araport; AT5G40760; -.
DR   TAIR; AT5G40760; G6PD6.
DR   eggNOG; KOG0563; Eukaryota.
DR   HOGENOM; CLU_013524_2_3_1; -.
DR   InParanoid; Q9FJI5; -.
DR   OMA; ERAGYYE; -.
DR   OrthoDB; 312822at2759; -.
DR   PhylomeDB; Q9FJI5; -.
DR   BRENDA; 1.1.1.49; 399.
DR   UniPathway; UPA00115; UER00408.
DR   PRO; PR:Q9FJI5; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FJI5; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:TAIR.
DR   GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IDA:TAIR.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0006006; P:glucose metabolic process; IDA:TAIR.
DR   GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IDA:TAIR.
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.
DR   Genevisible; Q9FJI5; AT.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cytoplasm; Glucose metabolism; NADP;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..515
FT                   /note="Glucose-6-phosphate 1-dehydrogenase 6, cytoplasmic"
FT                   /id="PRO_0000068098"
FT   ACT_SITE        274
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P11411"
FT   BINDING         38..45
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P11413"
FT   BINDING         73
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                   /ligand_label="1"
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"
FT   CONFLICT        361
FT                   /note="A -> S (in Ref. 1; CAB52675)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   515 AA;  59116 MW;  E8F7B88A52825C14 CRC64;
     MGSGQWHVEK RSTFRNDSFV REYGIVPETG CLSIIVLGAS GDLAKKKTFP ALFNLYRQGF
     LNPDEVHIFG YARTKISDEE LRDRIRGYLV DEKNAEQAEA LSKFLQLIKY VSGPYDAEEG
     FQRLDKAISE HEISKNSTEG SSRRLFYLAL PPSVYPSVCK MIKTCCMNKS DLGGWTRIVV
     EKPFGKDLES AEQLSSQIGE LFDESQIYRI DHYLGKELVQ NMLVLRFANR FFLPLWNRDN
     IENVQIVFRE DFGTEGRGGY FDEYGIIRDI IQNHLLQVLC LVAMEKPISL KPEHIRDEKV
     KVLQSVVPIS DDEVVLGQYE GYRDDDTVPN DSNTPTFATT ILRIHNERWE GVPFILKAGK
     ALNSRKAEIR IQFKDVPGDI FRCQKQGRNE FVIRLQPSEA MYMKLTVKQP GLDMNTVQSE
     LDLSYGQRYQ GVAIPEAYER LILDTIKGDQ QHFVRRDELK VAWEIFTPLL HRIDKGEVKS
     IPYKPGSRGP KEADQLLEKA GYLQTHGYIW IPPTL
//