GPDA2_ARATH
ID GPDA2_ARATH Reviewed; 420 AA.
AC Q949Q0;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)] 2, chloroplastic;
DE EC=1.1.1.8;
DE AltName: Full=Protein SUPPRESSOR OF FATTY ACID DESATURASE DEFICIENCY 1;
DE Flags: Precursor;
GN Name=GLY1; Synonyms=SFD1; OrderedLocusNames=At2g40690;
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=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 [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 FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=14729910; DOI=10.1105/tpc.016907;
RA Nandi A., Welti R., Shah J.;
RT "The Arabidopsis thaliana dihydroxyacetone phosphate reductase gene
RT SUPPRESSSOR OF FATTY ACID DESATURASE DEFICIENCY1 is required for
RT glycerolipid metabolism and for the activation of systemic acquired
RT resistance.";
RL Plant Cell 16:465-477(2004).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=15044700; DOI=10.1073/pnas.0401315101;
RA Kachroo A., Venugopal S.C., Lapchyk L., Falcone D., Hildebrand D.,
RA Kachroo P.;
RT "Oleic acid levels regulated by glycerolipid metabolism modulate defense
RT gene expression in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:5152-5157(2004).
RN [6]
RP FUNCTION.
RX PubMed=17431038; DOI=10.1073/pnas.0609259104;
RA Chandra-Shekara A.C., Venugopal S.C., Barman S.R., Kachroo A., Kachroo P.;
RT "Plastidial fatty acid levels regulate resistance gene-dependent defense
RT signaling in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7277-7282(2007).
RN [7]
RP FUNCTION.
RX PubMed=18088304; DOI=10.1111/j.1365-313x.2007.03400.x;
RA Chaturvedi R., Krothapalli K., Makandar R., Nandi A., Sparks A.A.,
RA Roth M.R., Welti R., Shah J.;
RT "Plastid omega3-fatty acid desaturase-dependent accumulation of a systemic
RT acquired resistance inducing activity in petiole exudates of Arabidopsis
RT thaliana is independent of jasmonic acid.";
RL Plant J. 54:106-117(2008).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF LYS-194; LYS-279 AND ASP-332.
RX PubMed=22645576; DOI=10.3389/fpls.2012.00026;
RA Lorenc-Kukula K., Chaturvedi R., Roth M., Welti R., Shah J.;
RT "Biochemical and molecular-genetic characterization of SFD1's involvement
RT in lipid metabolism and defense signaling.";
RL Front. Plant Sci. 3:26-26(2012).
CC -!- FUNCTION: Required to supply glycerol-3-phosphate in the chloroplast
CC for the synthesis of glycerolipids. Required for activation of systemic
CC acquired resistance (SAR). Provision of glycerol-3-phosphate may be
CC involved in generating lipid signals necessary for mediating defense
CC responses and SAR. {ECO:0000269|PubMed:14729910,
CC ECO:0000269|PubMed:15044700, ECO:0000269|PubMed:17431038,
CC ECO:0000269|PubMed:18088304, ECO:0000269|PubMed:22645576}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate
CC + H(+) + NADH; Xref=Rhea:RHEA:11092, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57597, ChEBI:CHEBI:57642,
CC ChEBI:CHEBI:57945; EC=1.1.1.8; Evidence={ECO:0000269|PubMed:14729910,
CC ECO:0000269|PubMed:15044700, ECO:0000269|PubMed:22645576};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.33 uM for glycerone phosphate {ECO:0000269|PubMed:22645576};
CC Vmax=49 umol/min/mg enzyme toward glycerone phosphate
CC {ECO:0000269|PubMed:22645576};
CC -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but leaves have decreased levels of hexadecatrienoic fatty
CC acid (16:3) and increased levels of oleic acid (18:1).
CC {ECO:0000269|PubMed:14729910, ECO:0000269|PubMed:15044700}.
CC -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; CP002685; AEC09864.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62576.1; -; Genomic_DNA.
DR EMBL; AY050968; AAK93645.1; -; mRNA.
DR EMBL; AY114078; AAM45126.1; -; mRNA.
DR RefSeq; NP_001324724.1; NM_001336858.1.
DR RefSeq; NP_565939.1; NM_129631.3.
DR AlphaFoldDB; Q949Q0; -.
DR SMR; Q949Q0; -.
DR STRING; 3702.AT2G40690.1; -.
DR PaxDb; Q949Q0; -.
DR PRIDE; Q949Q0; -.
DR ProteomicsDB; 248464; -.
DR EnsemblPlants; AT2G40690.1; AT2G40690.1; AT2G40690.
DR EnsemblPlants; AT2G40690.3; AT2G40690.3; AT2G40690.
DR GeneID; 818664; -.
DR Gramene; AT2G40690.1; AT2G40690.1; AT2G40690.
DR Gramene; AT2G40690.3; AT2G40690.3; AT2G40690.
DR KEGG; ath:AT2G40690; -.
DR Araport; AT2G40690; -.
DR TAIR; locus:2064849; AT2G40690.
DR eggNOG; KOG2711; Eukaryota.
DR HOGENOM; CLU_033449_6_2_1; -.
DR InParanoid; Q949Q0; -.
DR OrthoDB; 476066at2759; -.
DR PhylomeDB; Q949Q0; -.
DR BRENDA; 1.1.1.8; 399.
DR SABIO-RK; Q949Q0; -.
DR UniPathway; UPA00940; -.
DR PRO; PR:Q949Q0; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q949Q0; baseline and differential.
DR Genevisible; Q949Q0; AT.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0004367; F:glycerol-3-phosphate dehydrogenase [NAD+] activity; IBA:GO_Central.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:InterPro.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0045017; P:glycerolipid biosynthetic process; IMP:TAIR.
DR GO; GO:0046486; P:glycerolipid metabolic process; IMP:TAIR.
DR GO; GO:0006650; P:glycerophospholipid metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006116; P:NADH oxidation; IBA:GO_Central.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009627; P:systemic acquired resistance; IMP:TAIR.
DR Gene3D; 1.10.1040.10; -; 1.
DR HAMAP; MF_00394; NAD_Glyc3P_dehydrog; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR006168; G3P_DH_NAD-dep.
DR InterPro; IPR006109; G3P_DH_NAD-dep_C.
DR InterPro; IPR011128; G3P_DH_NAD-dep_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF07479; NAD_Gly3P_dh_C; 1.
DR Pfam; PF01210; NAD_Gly3P_dh_N; 1.
DR PRINTS; PR00077; GPDHDRGNASE.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00957; NAD_G3PDH; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Lipid biosynthesis; Lipid metabolism; NAD; Oxidoreductase;
KW Phospholipid biosynthesis; Phospholipid metabolism; Plant defense; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..45
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 46..420
FT /note="Glycerol-3-phosphate dehydrogenase [NAD(+)] 2,
FT chloroplastic"
FT /id="PRO_0000420174"
FT ACT_SITE 279
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 94..99
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 343..344
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 343
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 369
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT MUTAGEN 194
FT /note="K->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:22645576"
FT MUTAGEN 279
FT /note="K->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:22645576"
FT MUTAGEN 332
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:22645576"
SQ SEQUENCE 420 AA; 45092 MW; 3AACC248276BFC01 CRC64;
MAASVQPACL DLHFSGKHPP LLKHNAIIVR CVSSPNVIPE ADSISGPPDI INTNRDQRKV
VRIAWEKLVR WSRSLRAKAK TDVLERTRKV VVLGGGSFGT AMAAHVARRK EGLEVNMLVR
DSFVCQSINE NHHNCKYFPE HKLPENVIAT TDAKAALLDA DYCLHAVPVQ FSSSFLEGIA
DYVDPGLPFI SLSKGLELNT LRMMSQIIPI ALKNPRQPFV ALSGPSFALE LMNNLPTAMV
VASKDKKLAN AVQQLLASSY LRINTSSDVT GVEIAGALKN VLAIAAGIVD GMNLGNNSMA
ALVSQGCSEI RWLATKMGAK PTTITGLSGT GDIMLTCFVN LSRNRTVGVR LGSGETLDDI
LTSMNQVAEG VATAGAVIAL AQKYNVKLPV LTAVAKIIDN ELTPTKAVLE LMNLPQIEEV
