G3PA2_ARATH
ID G3PA2_ARATH Reviewed; 399 AA.
AC Q9LPW0; B3H4P2; C0Z2Y9;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase GAPA2, chloroplastic;
DE EC=1.2.1.13;
DE AltName: Full=NADP-dependent glyceraldehydephosphate dehydrogenase A subunit 2;
DE Flags: Precursor;
GN Name=GAPA2; OrderedLocusNames=At1g12900; ORFNames=F13K23.15;
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
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 stroma {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9LPW0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LPW0-2; Sequence=VSP_046526;
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}.
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; AC012187; AAF78494.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28944.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28946.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28947.1; -; Genomic_DNA.
DR EMBL; BT008637; AAP40454.1; -; mRNA.
DR EMBL; AK318953; BAH57068.1; -; mRNA.
DR EMBL; BT015867; AAU94430.1; -; mRNA.
DR PIR; F86262; F86262.
DR RefSeq; NP_001117276.1; NM_001123804.1. [Q9LPW0-2]
DR RefSeq; NP_001184977.1; NM_001198048.1. [Q9LPW0-2]
DR RefSeq; NP_172750.1; NM_101161.3. [Q9LPW0-1]
DR AlphaFoldDB; Q9LPW0; -.
DR SMR; Q9LPW0; -.
DR BioGRID; 23088; 9.
DR IntAct; Q9LPW0; 2.
DR MINT; Q9LPW0; -.
DR STRING; 3702.AT1G12900.1; -.
DR iPTMnet; Q9LPW0; -.
DR PaxDb; Q9LPW0; -.
DR PRIDE; Q9LPW0; -.
DR ProMEX; Q9LPW0; -.
DR ProteomicsDB; 228753; -. [Q9LPW0-1]
DR EnsemblPlants; AT1G12900.1; AT1G12900.1; AT1G12900. [Q9LPW0-1]
DR EnsemblPlants; AT1G12900.3; AT1G12900.3; AT1G12900. [Q9LPW0-2]
DR EnsemblPlants; AT1G12900.4; AT1G12900.4; AT1G12900. [Q9LPW0-2]
DR GeneID; 837848; -.
DR Gramene; AT1G12900.1; AT1G12900.1; AT1G12900. [Q9LPW0-1]
DR Gramene; AT1G12900.3; AT1G12900.3; AT1G12900. [Q9LPW0-2]
DR Gramene; AT1G12900.4; AT1G12900.4; AT1G12900. [Q9LPW0-2]
DR KEGG; ath:AT1G12900; -.
DR Araport; AT1G12900; -.
DR TAIR; locus:2010361; AT1G12900.
DR eggNOG; KOG0657; Eukaryota.
DR InParanoid; Q9LPW0; -.
DR PhylomeDB; Q9LPW0; -.
DR UniPathway; UPA00116; -.
DR PRO; PR:Q9LPW0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LPW0; baseline and differential.
DR Genevisible; Q9LPW0; 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:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005576; C:extracellular region; HDA: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; IEA:UniProtKB-UniPathway.
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 PIRSF; PIRSF000149; GAP_DH; 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 2: Evidence at transcript level;
KW Alternative splicing; Calvin cycle; Chloroplast; NADP; Oxidoreductase;
KW Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..48
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 49..399
FT /note="Glyceraldehyde-3-phosphate dehydrogenase GAPA2,
FT chloroplastic"
FT /id="PRO_0000422409"
FT ACT_SITE 216
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10009"
FT BINDING 74..75
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 215..217
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 274..275
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 297
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 379
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT SITE 243
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..49
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_046526"
FT CONFLICT 119
FT /note="D -> G (in Ref. 4; BAH57068)"
FT /evidence="ECO:0000305"
FT CONFLICT 387
FT /note="V -> D (in Ref. 4; BAH57068)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 399 AA; 42847 MW; EC5EDDFA8A58295D CRC64;
MASATFSVAK PSLQGFSEFS GLRNSSALPF AKRSSSDEFV SFVSFQTSAM RSNGGYRKGV
TEAKIKVAIN GFGRIGRNFL RCWHGRKDSP LDVVVINDTG GVKQASHLLK YDSTLGIFDA
DVKPSGDSAL SVDGKIIKIV SDRNPSNLPW GELGIDLVIE GTGVFVDRDG AGKHLQAGAK
KVLITAPGKG DIPTYVVGVN AELYSHEDTI ISNASCTTNC LAPFVKVLDQ KFGIIKGTMT
TTHSYTGDQR LLDASHRDLR RARAAALNIV PTSTGAAKAV ALVLPNLKGK LNGIALRVPT
PNVSVVDLVV QVSKKTFAEE VNAAFRDAAE KELKGILDVC DEPLVSVDFR CSDVSSTIDS
SLTMVMGDDM VKVIAWYDNE WGYSQRVVDL ADIVANNWK
