G3PP2_ARATH
ID G3PP2_ARATH Reviewed; 420 AA.
AC Q5E924; Q84WR0; Q8L8W7; Q9SA29;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase GAPCP2, chloroplastic;
DE EC=1.2.1.12;
DE AltName: Full=Glyceraldehyde-3-phosphate dehydrogenase of plastid 2;
DE AltName: Full=NAD-dependent glyceraldehydephosphate dehydrogenase chloroplastic 2;
DE Flags: Precursor;
GN Name=GAPCP2; OrderedLocusNames=At1g16300; ORFNames=F3O9.10;
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].
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].
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=19675149; DOI=10.1104/pp.109.143701;
RA Munoz-Bertomeu J., Cascales-Minana B., Mulet J.M., Baroja-Fernandez E.,
RA Pozueta-Romero J., Kuhn J.M., Segura J., Ros R.;
RT "Plastidial glyceraldehyde-3-phosphate dehydrogenase deficiency leads to
RT altered root development and affects the sugar and amino acid balance in
RT Arabidopsis.";
RL Plant Physiol. 151:541-558(2009).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20107025; DOI=10.1104/pp.109.150458;
RA Munoz-Bertomeu J., Cascales-Minana B., Irles-Segura A., Mateu I.,
RA Nunes-Nesi A., Fernie A.R., Segura J., Ros R.;
RT "The plastidial glyceraldehyde-3-phosphate dehydrogenase is critical for
RT viable pollen development in Arabidopsis.";
RL Plant Physiol. 152:1830-1841(2010).
CC -!- FUNCTION: Involved in plastidial glycolytic pathway and plays a
CC specific role in glycolytic energy production in non-green plastids and
CC chloroplasts. Essential for breakdown of starch to form sucrose for
CC export to non-photosynthetic tissues, and to generate primary
CC metabolites for anabolic pathways such as fatty acid and amino acid
CC synthesis. Plays an important role in plant development by providing
CC substrates for the phosphorylated pathway of serine biosynthesis in
CC roots. Plays a crucial role in pollen development. Functionally
CC redundant with GAPCP1. {ECO:0000269|PubMed:19675149,
CC ECO:0000269|PubMed:20107025}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-
CC phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.12;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10009};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000305|PubMed:19675149}.
CC -!- TISSUE SPECIFICITY: Expressed in shoot and root vasculature, leaf veins
CC and vascular tissue of flowers and siliques.
CC {ECO:0000269|PubMed:19675149}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. Gapcp1 and gapcp2 double mutants have severe dwarf
CC phenotypes with arrested root development and male sterility. Pollen
CC grains show shrunken and collapsed forms and cannot germinate.
CC {ECO:0000269|PubMed:19675149, ECO:0000269|PubMed:20107025}.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD34682.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC006341; AAD34682.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29433.1; -; Genomic_DNA.
DR EMBL; BT002867; AAO22684.1; -; mRNA.
DR EMBL; BT021096; AAX12866.1; -; mRNA.
DR EMBL; AY088762; AAM67077.1; -; mRNA.
DR PIR; A86298; A86298.
DR RefSeq; NP_173080.1; NM_101496.3.
DR AlphaFoldDB; Q5E924; -.
DR SMR; Q5E924; -.
DR STRING; 3702.AT1G16300.1; -.
DR iPTMnet; Q5E924; -.
DR PaxDb; Q5E924; -.
DR PRIDE; Q5E924; -.
DR ProteomicsDB; 230480; -.
DR EnsemblPlants; AT1G16300.1; AT1G16300.1; AT1G16300.
DR GeneID; 838199; -.
DR Gramene; AT1G16300.1; AT1G16300.1; AT1G16300.
DR KEGG; ath:AT1G16300; -.
DR Araport; AT1G16300; -.
DR TAIR; locus:2032810; AT1G16300.
DR eggNOG; KOG0657; Eukaryota.
DR HOGENOM; CLU_030140_0_3_1; -.
DR InParanoid; Q5E924; -.
DR OMA; NCVAPMA; -.
DR OrthoDB; 945145at2759; -.
DR PhylomeDB; Q5E924; -.
DR BRENDA; 1.2.1.12; 399.
DR PRO; PR:Q5E924; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q5E924; baseline and differential.
DR Genevisible; Q5E924; AT.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0009536; C:plastid; IDA:TAIR.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IMP:TAIR.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0080144; P:amino acid homeostasis; IMP:TAIR.
DR GO; GO:0005975; P:carbohydrate metabolic process; IMP:TAIR.
DR GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR GO; GO:0080022; P:primary root development; IMP: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; PTHR10836; PTHR10836; 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 2: Evidence at transcript level;
KW Chloroplast; Glycolysis; NAD; Oxidoreductase; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..66
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 67..420
FT /note="Glyceraldehyde-3-phosphate dehydrogenase GAPCP2,
FT chloroplastic"
FT /id="PRO_0000422408"
FT ACT_SITE 234
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10009"
FT BINDING 94..95
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 233..235
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 264
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 398
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 261
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250"
FT CONFLICT 58
FT /note="N -> S (in Ref. 3; AAO22684)"
FT /evidence="ECO:0000305"
FT CONFLICT 336
FT /note="S -> T (in Ref. 5; AAM67077)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 420 AA; 44846 MW; E9FF3D655F281B63 CRC64;
MALSSLLRSA ATSAAAPRVE LYPSSSYNHS QVTSSLGFSH SLTSSRFSGA AVSTGKYNAK
RVQPIKATAT EAPPAVHRSR SSGKTKVGIN GFGRIGRLVL RIATFRDDIE VVAVNDPFID
AKYMAYMFKY DSTHGNYKGT INVIDDSTLE INGKQVKVVS KRDPAEIPWA DLGAEYVVES
SGVFTTVGQA SSHLKGGAKK VIISAPSADA PMFVVGVNEK TYLPNMDIVS NASCTTNCLA
PLAKVVHEEF GILEGLMTTV HATTATQKTV DGPSMKDWRG GRGASQNIIP SSTGAAKAVG
KVLPELNGKL TGMAFRVPTP NVSVVDLTCR LEKDASYEDV KAAIKFASEG PLRGILGYTE
EDVVSNDFLG DSRSSIFDAN AGIGLSKSFM KLVSWYDNEW GYSNRVLDLI EHMALVAASR
