GPDH2_ARATH
ID GPDH2_ARATH Reviewed; 456 AA.
AC Q9S785; F4JFL8;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2015, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)] At3g07690, cytosolic;
DE Short=G3Pdh(At3g07690);
DE EC=1.1.1.8;
GN OrderedLocusNames=At3g07690 {ECO:0000312|EMBL:AEE74587.1};
GN ORFNames=F17A17.3 {ECO:0000312|EMBL:AAF21179.1},
GN MLP3.14 {ECO:0000312|EMBL:AAF13087.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=21441932; DOI=10.1038/ng.798;
RA Chanda B., Xia Y., Mandal M.K., Yu K., Sekine K.T., Gao Q.M., Selote D.,
RA Hu Y., Stromberg A., Navarre D., Kachroo A., Kachroo P.;
RT "Glycerol-3-phosphate is a critical mobile inducer of systemic immunity in
RT plants.";
RL Nat. Genet. 43:421-427(2011).
CC -!- FUNCTION: Required for glycerol-3-phosphate (G3P) accumulation during
CC systemic acquired resistance (SAR) establishment.
CC {ECO:0000269|PubMed:21441932}.
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;
CC Evidence={ECO:0000250|UniProtKB:P21695};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P21695}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8N335}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9S785-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9S785-2; Sequence=VSP_057920;
CC -!- DISRUPTION PHENOTYPE: Compromised in systemic acquired resistance (SAR)
CC triggered by Pseudomonas syringae DC3000 avrRpt2 probably because of a
CC reduced accumulation of glycerol-3-phosphate (G3P).
CC {ECO:0000269|PubMed:21441932}.
CC -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF13087.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAF21179.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC009176; AAF13087.1; ALT_INIT; Genomic_DNA.
DR EMBL; AC013483; AAF21179.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002686; AEE74587.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65682.1; -; Genomic_DNA.
DR RefSeq; NP_001327632.1; NM_001337728.1. [Q9S785-1]
DR RefSeq; NP_187426.3; NM_111648.6. [Q9S785-2]
DR AlphaFoldDB; Q9S785; -.
DR SMR; Q9S785; -.
DR STRING; 3702.AT3G07690.1; -.
DR PaxDb; Q9S785; -.
DR PRIDE; Q9S785; -.
DR ProteomicsDB; 247027; -. [Q9S785-1]
DR EnsemblPlants; AT3G07690.1; AT3G07690.1; AT3G07690. [Q9S785-2]
DR EnsemblPlants; AT3G07690.2; AT3G07690.2; AT3G07690. [Q9S785-1]
DR GeneID; 819960; -.
DR Gramene; AT3G07690.1; AT3G07690.1; AT3G07690. [Q9S785-2]
DR Gramene; AT3G07690.2; AT3G07690.2; AT3G07690. [Q9S785-1]
DR KEGG; ath:AT3G07690; -.
DR Araport; AT3G07690; -.
DR TAIR; locus:2077387; AT3G07690.
DR eggNOG; KOG2711; Eukaryota.
DR OMA; LRHLMGK; -.
DR OrthoDB; 476066at2759; -.
DR BioCyc; ARA:AT3G07690-MON; -.
DR PRO; PR:Q9S785; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9S785; baseline and differential.
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:0006116; P:NADH oxidation; IBA:GO_Central.
DR GO; GO:0009627; P:systemic acquired resistance; IMP:TAIR.
DR Gene3D; 1.10.1040.10; -; 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.
PE 3: Inferred from homology;
KW Alternative splicing; Cytoplasm; NAD; Oxidoreductase; Plant defense;
KW Reference proteome; Stress response.
FT CHAIN 1..456
FT /note="Glycerol-3-phosphate dehydrogenase [NAD(+)]
FT At3g07690, cytosolic"
FT /id="PRO_0000434271"
FT ACT_SITE 278
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P21695"
FT BINDING 41..46
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P21695"
FT BINDING 189
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P90551"
FT BINDING 189
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P21695"
FT BINDING 228
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P21695"
FT BINDING 340..341
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P21695"
FT BINDING 340
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P21695"
FT BINDING 368
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P21695"
FT VAR_SEQ 285
FT /note="A -> AVFVLAFLYST (in isoform 2)"
FT /id="VSP_057920"
SQ SEQUENCE 456 AA; 51396 MW; DFAABEDEE74C3283 CRC64;
MMDHLVETNS VPSRLVEERL DEIRRVMGKA DDDPLRIVGV GAGAWGSVFI AMLQENYGKF
RGKVSVRIWR RGGRAIDKAT AEHLFEVINS REELLRRLIR RCAYLKYVEA RLGDRVLYAD
EILKDGFCLN MIETPLCPLK VVTNLQEAVW DADIVINGLP STETFQVFNE ISKYWKERVN
APVIISLAKG VEAEFEPHPR IVTPTQMIHR ATGIPLENIL YLGGPNIASE VYNKEYANAR
ICGSEKWRKP LGKFLRQSHF IVWDNSDLIT HEVMGGLKNV YAIGAGMVAT LTKESATSKS
VYFAHCTSEM IFITHLLAKE PEKLAGPLLA DTYVTLLKGR NAWYGQKLAK GELSLEMGDS
IKGKGMIQGV SAVKAFFELL NQSSLSLQHP EEGKPVTPAE LCPILKMLYR ILITREFSCE
AILEALRDET MNDPRELIEI AHSHLFFQPW LLGQKP
