G6PD5_ARATH
ID G6PD5_ARATH Reviewed; 516 AA.
AC Q9LK23; Q8VZD0; Q9SUK0;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase 5, cytoplasmic {ECO:0000305};
DE Short=AtG6PD5 {ECO:0000303|PubMed:15634201};
DE Short=G6PDH5 {ECO:0000305};
DE EC=1.1.1.49 {ECO:0000269|PubMed:15634201};
GN Name=G6PD5 {ECO:0000303|PubMed:15634201};
GN Synonyms=ACG9 {ECO:0000303|PubMed:10437832};
GN OrderedLocusNames=At3g27300 {ECO:0000312|Araport:AT3G27300};
GN ORFNames=K17E12.12 {ECO:0000312|EMBL:BAB02125.1};
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [3]
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 [4]
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 [5]
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 [6]
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=19 uM for NADP {ECO:0000269|PubMed:15634201};
CC pH dependence:
CC Optimum pH is 8.5. {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 leaves and stems.
CC {ECO:0000269|PubMed:15634201}.
CC -!- MISCELLANEOUS: There are 6 glucose-6-phosphate 1-dehydrogenase genes in
CC A.thaliana. {ECO:0000303|PubMed:15634201}.
CC -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AJ010970; CAB52674.1; -; mRNA.
DR EMBL; AP000381; BAB02125.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77290.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77291.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77292.1; -; Genomic_DNA.
DR EMBL; AY065054; AAL57688.1; -; mRNA.
DR PIR; T52611; T52611.
DR RefSeq; NP_001030780.1; NM_001035703.3.
DR RefSeq; NP_001078214.1; NM_001084745.1.
DR RefSeq; NP_189366.1; NM_113644.5.
DR AlphaFoldDB; Q9LK23; -.
DR SMR; Q9LK23; -.
DR STRING; 3702.AT3G27300.2; -.
DR iPTMnet; Q9LK23; -.
DR PaxDb; Q9LK23; -.
DR PRIDE; Q9LK23; -.
DR ProteomicsDB; 247383; -.
DR EnsemblPlants; AT3G27300.1; AT3G27300.1; AT3G27300.
DR EnsemblPlants; AT3G27300.2; AT3G27300.2; AT3G27300.
DR EnsemblPlants; AT3G27300.3; AT3G27300.3; AT3G27300.
DR GeneID; 822349; -.
DR Gramene; AT3G27300.1; AT3G27300.1; AT3G27300.
DR Gramene; AT3G27300.2; AT3G27300.2; AT3G27300.
DR Gramene; AT3G27300.3; AT3G27300.3; AT3G27300.
DR KEGG; ath:AT3G27300; -.
DR Araport; AT3G27300; -.
DR TAIR; locus:2086558; AT3G27300.
DR eggNOG; KOG0563; Eukaryota.
DR HOGENOM; CLU_013524_2_3_1; -.
DR InParanoid; Q9LK23; -.
DR PhylomeDB; Q9LK23; -.
DR BRENDA; 1.1.1.49; 399.
DR UniPathway; UPA00115; UER00408.
DR PRO; PR:Q9LK23; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LK23; baseline and differential.
DR Genevisible; Q9LK23; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
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..516
FT /note="Glucose-6-phosphate 1-dehydrogenase 5, cytoplasmic"
FT /id="PRO_0000068097"
FT ACT_SITE 275
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P11411"
FT BINDING 38..45
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P11413"
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 156
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 183
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 213..217
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 251
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 270
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 361
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 397
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT CONFLICT 26
FT /note="V -> I (in Ref. 1; CAB52674)"
FT /evidence="ECO:0000305"
FT CONFLICT 376
FT /note="D -> G (in Ref. 4; AAL57688)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 516 AA; 59157 MW; 407E42590EFC20E2 CRC64;
MGSGQWHMEK RSTLKNDSFV KEYNPVTETG SLSIIVLGAS GDLAKKKTFP ALFNLFHQGF
LNPDEVHIFG YARSKITDEE LRDKIRGYLV DEKNASKKTE ALSKFLKLIK YVSGPYDSEE
GFKRLDKAIL EHEISKKTAE GSSRRLFYLA LPPSVYPPVS KMIKAWCTNK SDLGGWTRIV
VEKPFGKDLE SAEQLSSQIG ALFEEPQIYR IDHYLGKELV QNMLVLRFAN RLFLPLWNRD
NIANVQIVFR EDFGTEGRGG YFDEYGIIRD IIQNHLLQVL CLVAMEKPIS LKPEHIRDEK
VKVLQSVIPI KDEEVVLGQY EGYRDDPTVP NDSNTPTFAT TILRINNERW EGVPFILKAG
KAMSSKKADI RIQFKDVPGD IFKCQNQGRN EFVIRLQPSE AMYMKLTVKQ PGLEMQTVQS
ELDLSYKQRY QDVSIPEAYE RLILDTIRGD QQHFVRRDEL KAAWEIFTPL LHRIDKGEVK
SVPYKQGSRG PAEADQLLKK AGYMQTHGYI WIPPTL
