G6PD6_ARATH
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 03-AUG-2022, entry version 149.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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.AT5G40760.1; -.
DR iPTMnet; Q9FJI5; -.
DR PaxDb; Q9FJI5; -.
DR PRIDE; Q9FJI5; -.
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; locus:2154805; AT5G40760.
DR eggNOG; KOG0563; Eukaryota.
DR HOGENOM; CLU_013524_2_3_1; -.
DR InParanoid; Q9FJI5; -.
DR OMA; VEICVYE; -.
DR OrthoDB; 383995at2759; -.
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 Genevisible; Q9FJI5; AT.
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 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 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
