G3PB_ARATH
ID G3PB_ARATH Reviewed; 447 AA.
AC P25857; Q0WL92; Q9C7S2;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase GAPB, chloroplastic;
DE EC=1.2.1.13;
DE AltName: Full=NADP-dependent glyceraldehydephosphate dehydrogenase B;
DE Flags: Precursor;
GN Name=GAPB; OrderedLocusNames=At1g42970; ORFNames=F13A11.3;
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 [GENOMIC DNA / MRNA].
RC TISSUE=Leaf;
RX PubMed=1916285; DOI=10.1016/0378-1119(91)90242-4;
RA Shih M.-C., Heinrich P., Goodman H.M.;
RT "Cloning and chromosomal mapping of nuclear genes encoding chloroplast and
RT cytosolic glyceraldehyde-3-phosphate-dehydrogenase from Arabidopsis
RT thaliana.";
RL Gene 104:133-138(1991).
RN [2]
RP ERRATUM OF PUBMED:1916285.
RX PubMed=1398114; DOI=10.1016/0378-1119(92)90290-6;
RA Shih M.-C., Heinrich P., Goodman H.M.;
RL Gene 119:317-319(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=15533878; DOI=10.1093/jxb/eri020;
RA Marri L., Sparla F., Pupillo P., Trost P.;
RT "Co-ordinated gene expression of photosynthetic glyceraldehyde-3-phosphate
RT dehydrogenase, phosphoribulokinase, and CP12 in Arabidopsis thaliana.";
RL J. Exp. Bot. 56:73-80(2005).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
CC -!- FUNCTION: Involved in the photosynthetic reductive pentose phosphate
CC pathway (Calvin-Benson cycle). Catalyzes the reduction of 1,3-
CC diphosphoglycerate by NADPH (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + NADP(+) + phosphate = (2R)-3-
CC phospho-glyceroyl phosphate + H(+) + NADPH; Xref=Rhea:RHEA:10296,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57604,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:59776; EC=1.2.1.13;
CC -!- PATHWAY: Carbohydrate biosynthesis; Calvin cycle.
CC -!- SUBUNIT: Tetramer of either four A chains (GAPDH 2) or two A and two B
CC chains (GAPDH 1). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC {ECO:0000250|UniProtKB:P25856}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P25856}. Plastid, chloroplast stroma
CC {ECO:0000250|UniProtKB:P25856}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves and stems.
CC {ECO:0000269|PubMed:15533878}.
CC -!- INDUCTION: Repressed by darkness and sucrose.
CC {ECO:0000269|PubMed:15533878}.
CC -!- MISCELLANEOUS: Plants contain three types of GAPDH: NAD-dependent
CC cytosolic forms which participate in glycolysis, NAD-dependent
CC chloroplastic forms which participate in plastidic glycolysis and NADP-
CC dependent chloroplastic forms which participate in the photosynthetic
CC reductive pentose phosphate pathway (Calvin-Benson cycle). All the
CC forms are encoded by distinct genes.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; M64115; AAD10210.1; -; mRNA.
DR EMBL; M64118; AAA32795.1; -; Genomic_DNA.
DR EMBL; AC068324; AAG51517.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31933.1; -; Genomic_DNA.
DR EMBL; AY039961; AAK64065.1; -; mRNA.
DR EMBL; AY039539; AAK62594.1; -; mRNA.
DR EMBL; AY079402; AAL85133.1; -; mRNA.
DR EMBL; AY095991; AAM19948.1; -; mRNA.
DR EMBL; AY140091; AAM98232.1; -; mRNA.
DR EMBL; BT002267; AAN72278.1; -; mRNA.
DR EMBL; AK230314; BAF02115.1; -; mRNA.
DR PIR; C96497; C96497.
DR PIR; JQ1286; JQ1286.
DR RefSeq; NP_174996.1; NM_103456.4.
DR AlphaFoldDB; P25857; -.
DR SMR; P25857; -.
DR BioGRID; 26120; 10.
DR IntAct; P25857; 3.
DR MINT; P25857; -.
DR STRING; 3702.AT1G42970.1; -.
DR iPTMnet; P25857; -.
DR MetOSite; P25857; -.
DR SWISS-2DPAGE; P25857; -.
DR PaxDb; P25857; -.
DR PRIDE; P25857; -.
DR ProteomicsDB; 248556; -.
DR EnsemblPlants; AT1G42970.1; AT1G42970.1; AT1G42970.
DR GeneID; 840895; -.
DR Gramene; AT1G42970.1; AT1G42970.1; AT1G42970.
DR KEGG; ath:AT1G42970; -.
DR Araport; AT1G42970; -.
DR TAIR; locus:2009864; AT1G42970.
DR eggNOG; KOG0657; Eukaryota.
DR HOGENOM; CLU_030140_0_2_1; -.
DR InParanoid; P25857; -.
DR OMA; VYGVNHF; -.
DR OrthoDB; 945145at2759; -.
DR PhylomeDB; P25857; -.
DR BRENDA; 1.2.1.13; 399.
DR UniPathway; UPA00116; -.
DR PRO; PR:P25857; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P25857; baseline and differential.
DR Genevisible; P25857; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0010319; C:stromule; IDA:TAIR.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IBA:GO_Central.
DR GO; GO:0047100; F:glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0051287; F:NAD binding; IBA:GO_Central.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:1901149; F:salicylic acid binding; HDA:TAIR.
DR GO; GO:0006006; P:glucose metabolic process; IBA:GO_Central.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; NAS:TAIR.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR GO; GO:0009416; P:response to light stimulus; IEP:TAIR.
DR GO; GO:0009744; P:response to sucrose; IEP:TAIR.
DR InterPro; IPR020831; GlycerAld/Erythrose_P_DH.
DR InterPro; IPR020830; GlycerAld_3-P_DH_AS.
DR InterPro; IPR020829; GlycerAld_3-P_DH_cat.
DR InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd.
DR InterPro; IPR006424; Glyceraldehyde-3-P_DH_1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43148; PTHR43148; 1.
DR Pfam; PF02800; Gp_dh_C; 1.
DR Pfam; PF00044; Gp_dh_N; 1.
DR PRINTS; PR00078; G3PDHDRGNASE.
DR SMART; SM00846; Gp_dh_N; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01534; GAPDH-I; 1.
DR PROSITE; PS00071; GAPDH; 1.
PE 1: Evidence at protein level;
KW Calvin cycle; Chloroplast; Membrane; NADP; Oxidoreductase; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..80
FT /note="Chloroplast"
FT /evidence="ECO:0000250"
FT CHAIN 81..447
FT /note="Glyceraldehyde-3-phosphate dehydrogenase GAPB,
FT chloroplastic"
FT /id="PRO_0000010417"
FT ACT_SITE 235
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10009"
FT BINDING 91..92
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 115
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 234..236
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 265
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 280
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 293..294
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 316
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 399
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT SITE 262
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 447 AA; 47660 MW; E7DBD59915560EF3 CRC64;
MATHAALAVS RIPVTQRLQS KSAIHSFPAQ CSSKRLEVAE FSGLRMSSIG GEASFFDAVA
AQIIPKAVTT STPVRGETVA KLKVAINGFG RIGRNFLRCW HGRKDSPLEV VVLNDSGGVK
NASHLLKYDS MLGTFKAEVK IVDNETISVD GKLIKVVSNR DPLKLPWAEL GIDIVIEGTG
VFVDGPGAGK HIQAGASKVI ITAPAKGADI PTYVMGVNEQ DYGHDVANII SNASCTTNCL
APFAKVLDEE FGIVKGTMTT THSYTGDQRL LDASHRDLRR ARAAALNIVP TSTGAAKAVS
LVLPQLKGKL NGIALRVPTP NVSVVDLVIN VEKKGLTAED VNEAFRKAAN GPMKGILDVC
DAPLVSVDFR CSDVSTTIDS SLTMVMGDDM VKVVAWYDNE WGYSQRVVDL AHLVASKWPG
AEAVGSGDPL EDFCKTNPAD EECKVYD
