GAPN_APIGR
ID GAPN_APIGR Reviewed; 496 AA.
AC Q9SNX8;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=NADP-dependent glyceraldehyde-3-phosphate dehydrogenase;
DE EC=1.2.1.9;
DE AltName: Full=Glyceraldehyde-3-phosphate dehydrogenase [NADP(+)];
DE AltName: Full=Non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase;
DE AltName: Full=Triosephosphate dehydrogenase;
DE AltName: Full=nr-G3PDH;
OS Apium graveolens (Celery).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Apiaceae; Apioideae; apioid superclade;
OC Apieae; Apium.
OX NCBI_TaxID=4045;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, DEVELOPMENTAL STAGE, AND INDUCTION.
RC STRAIN=cv. Giant Pascal; TISSUE=Leaf;
RX PubMed=10982446; DOI=10.1104/pp.124.1.321;
RA Gao Z., Loescher W.H.;
RT "NADPH supply and mannitol biosynthesis. Characterization, cloning, and
RT regulation of the non-reversible glyceraldehyde-3-phosphate dehydrogenase
RT in celery leaves.";
RL Plant Physiol. 124:321-330(2000).
CC -!- FUNCTION: Important as a means of generating NADPH for biosynthetic
CC reactions. May be a main source of cytosolic NADPH for mannitol
CC biosynthesis in leaves. {ECO:0000269|PubMed:10982446}.
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 -!- ACTIVITY REGULATION: Competitive inhibition by NADPH, 3-phospho-D-
CC glycerate and ATP. {ECO:0000269|PubMed:10982446}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.8 uM for NADP(+) {ECO:0000269|PubMed:10982446};
CC KM=29 uM for D-glyceraldehyde 3-phosphate
CC {ECO:0000269|PubMed:10982446};
CC Note=Measured at pH 7.7 and 30 degrees Celsius for all experiments.;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol.
CC -!- DEVELOPMENTAL STAGE: Expression increases during leaf development. Not
CC expressed in senescent leaves. {ECO:0000269|PubMed:10982446}.
CC -!- INDUCTION: By salt stress. {ECO:0000269|PubMed:10982446}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AF196292; AAF08296.1; -; mRNA.
DR AlphaFoldDB; Q9SNX8; -.
DR SMR; Q9SNX8; -.
DR PRIDE; Q9SNX8; -.
DR SABIO-RK; Q9SNX8; -.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0008886; F:glyceraldehyde-3-phosphate dehydrogenase (NADP+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
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 Cytoplasm; NADP; Oxidoreductase; Stress response.
FT CHAIN 1..496
FT /note="NADP-dependent glyceraldehyde-3-phosphate
FT dehydrogenase"
FT /id="PRO_0000256065"
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"
SQ SEQUENCE 496 AA; 53174 MW; D86AE4C01E0A3642 CRC64;
MAGSGVYADI IEGDVFKYYS DGEWKKSSSG KSVAIINPTT RMTQFKVQAC TQEEVNKAME
TAKKVQKQWA KTPLWKRAEL LHKAAAILKE HKAAIADCLV KEIAKPAKDS VTEVVRSGDL
VSYCAEEGVR LLGEGKFLVS DSFPGNERTK YCLTSKIPLG VILAIPPFNY PVNLAVSKIG
PALIAGNALV LKPPTQGAVA CLHMVHCFHL AGFPKGLISC ITGKGSEIGD FLTMHPGVNC
ISFTGGDTGI AISKKAGMVP LQMELGGKDA CIVLEDADLD LVASNVIKGG FSYSGQRCTA
IKVILVMQSV ADTLVEKVNA KVAKLTVGPP EDNSDITPVV SESSANFIEG LVKDAKEKGA
TFCQEYKREG NLIWPLLLDN VKPDMRIAWE EPFGPILPVI RINSAEEGIH HCNASNFGLQ
GCVFTRDINK AMLISDAMES GTIQINSAPA RGPDHFPFQG LKDSGIGSQG ITNSINMMTK
IKTTVINLPS PSYTMG
