GAPN_ARATH
ID GAPN_ARATH Reviewed; 496 AA.
AC Q1WIQ6; Q9ZUG8;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=NADP-dependent glyceraldehyde-3-phosphate dehydrogenase;
DE EC=1.2.1.9;
DE AltName: Full=Aldehyde dehydrogenase family 11 member A3;
DE AltName: Full=Glyceraldehyde-3-phosphate dehydrogenase [NADP(+)];
DE AltName: Full=Non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase;
DE AltName: Full=Triosephosphate dehydrogenase;
GN Name=ALDH11A3; Synonyms=GAPN; OrderedLocusNames=At2g24270;
GN ORFNames=F27D4.18;
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].
RC STRAIN=cv. Columbia;
RA Rius S.P., Iglesias A.A., Gomez-Casati D.F.;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 NOMENCLATURE.
RX PubMed=15358267; DOI=10.1016/j.tplants.2004.06.004;
RA Kirch H.-H., Bartels D., Wei Y., Schnable P.S., Wood A.J.;
RT "The ALDH gene superfamily of Arabidopsis.";
RL Trends Plant Sci. 9:371-377(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-4, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Important as a means of generating NADPH for biosynthetic
CC reactions.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + H2O + NADP(+) = (2R)-3-
CC phosphoglycerate + 2 H(+) + NADPH; Xref=Rhea:RHEA:14669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58272, ChEBI:CHEBI:58349, ChEBI:CHEBI:59776; EC=1.2.1.9;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q1WIQ6-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; DQ268762; ABB83822.1; -; mRNA.
DR EMBL; AC005967; AAD03388.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07553.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07554.1; -; Genomic_DNA.
DR EMBL; AY037205; AAK59790.1; -; mRNA.
DR EMBL; AY136409; AAM97075.1; -; mRNA.
DR EMBL; BT004551; AAO42797.1; -; mRNA.
DR PIR; F84634; F84634.
DR RefSeq; NP_001189589.1; NM_001202660.1. [Q1WIQ6-1]
DR RefSeq; NP_180004.1; NM_127989.4. [Q1WIQ6-1]
DR AlphaFoldDB; Q1WIQ6; -.
DR SMR; Q1WIQ6; -.
DR BioGRID; 2314; 5.
DR IntAct; Q1WIQ6; 1.
DR STRING; 3702.AT2G24270.4; -.
DR iPTMnet; Q1WIQ6; -.
DR PaxDb; Q1WIQ6; -.
DR PRIDE; Q1WIQ6; -.
DR ProteomicsDB; 248603; -. [Q1WIQ6-1]
DR EnsemblPlants; AT2G24270.1; AT2G24270.1; AT2G24270. [Q1WIQ6-1]
DR EnsemblPlants; AT2G24270.3; AT2G24270.3; AT2G24270. [Q1WIQ6-1]
DR GeneID; 816962; -.
DR Gramene; AT2G24270.1; AT2G24270.1; AT2G24270. [Q1WIQ6-1]
DR Gramene; AT2G24270.3; AT2G24270.3; AT2G24270. [Q1WIQ6-1]
DR KEGG; ath:AT2G24270; -.
DR Araport; AT2G24270; -.
DR eggNOG; KOG2450; Eukaryota.
DR HOGENOM; CLU_005391_1_0_1; -.
DR InParanoid; Q1WIQ6; -.
DR PhylomeDB; Q1WIQ6; -.
DR BioCyc; ARA:AT2G24270-MON; -.
DR BioCyc; MetaCyc:AT2G24270-MON; -.
DR PRO; PR:Q1WIQ6; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q1WIQ6; baseline and differential.
DR Genevisible; Q1WIQ6; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008886; F:glyceraldehyde-3-phosphate dehydrogenase (NADP+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0008911; F:lactaldehyde dehydrogenase activity; IBA:GO_Central.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; NADP; Oxidoreductase;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..496
FT /note="NADP-dependent glyceraldehyde-3-phosphate
FT dehydrogenase"
FT /id="PRO_0000256066"
FT ACT_SITE 264
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT ACT_SITE 298
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 169..170
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 230
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 245..249
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 297..299
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 391
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 451
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 169
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 4
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT CONFLICT 47
FT /note="V -> A (in Ref. 1; ABB83822)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="N -> Y (in Ref. 1; ABB83822)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 496 AA; 53060 MW; 9231656A951175D5 CRC64;
MAGTGLFAEI LDGEVYKYYA DGEWKTSSSG KSVAIMNPAT RKTQYKVQAC TQEEVNAVME
LAKSAQKSWA KTPLWKRAEL LHKAAAILKD NKAPMAESLV KEIAKPAKDS VTEVVRSGDL
ISYCAEEGVR ILGEGKFLLS DSFPGNDRTK YCLTSKIPLG VVLAIPPFNY PVNLAVSKIA
PALIAGNSLV LKPPTQGAVS CLHMVHCFHL AGFPKGLISC ITGKGSEIGD FLTMHPAVNC
ISFTGGDTGI SISKKAGMIP LQMELGGKDA CIVLDDADLD LVASNIIKGG FSYSGQRCTA
VKVVLVMESV ADELVEKVKA KVAKLTVGPP EENSDITAVV SESSANFIEG LVMDAKEKGA
TFCQEYKREG NLIWPLLLDN VRPDMRIAWE EPFGPVVPVL RINSVEEGIN HCNASNFGLQ
GCVFTKDINK AILISDAMET GTVQINSAPA RGPDHFPFQG LKDSGIGSQG VTNSINLMTK
VKTTVINLPT PSYSMG
