GPDHC_ARATH
ID GPDHC_ARATH Reviewed; 462 AA.
AC O22216; B9DH11;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)] GPDHC1, cytosolic;
DE EC=1.1.1.8;
GN Name=GPDHC1; OrderedLocusNames=At2g41540;
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], FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=16415206; DOI=10.1105/tpc.105.039750;
RA Shen W., Wei Y., Dauk M., Tan Y., Taylor D.C., Selvaraj G., Zou J.;
RT "Involvement of a glycerol-3-phosphate dehydrogenase in modulating the
RT NADH/NAD+ ratio provides evidence of a mitochondrial glycerol-3-phosphate
RT shuttle in Arabidopsis.";
RL Plant Cell 18:422-441(2006).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
CC -!- FUNCTION: Involved in cell redox homeostasis. Required for maintaining
CC a steady state cellular NADH/NAD(+) ratio through a mitochondrial
CC glycerol-3-phosphate redox shuttle. May function with the mitochondrial
CC FAD-dependent glycerol-3-phosphate dehydrogenase SDP6 to shuttle
CC reducing equivalents into the mitochondria for respiration.
CC {ECO:0000269|PubMed:16415206}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, flowers and siliques.
CC {ECO:0000269|PubMed:16415206}.
CC -!- INDUCTION: By abscisic acid and salt and dehydration treatments. Down-
CC regulated by hypoxia. {ECO:0000269|PubMed:16415206}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants have increased NADH/NAD(+) ratios,
CC decreased levels of glycerol-3-phosphate, and produce constitutive high
CC levels of reactive oxygen species (ROS). {ECO:0000269|PubMed:16415206}.
CC -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; AJ347019; CAC69665.1; -; mRNA.
DR EMBL; AC002510; AAB84336.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09996.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09997.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09998.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM63134.1; -; Genomic_DNA.
DR EMBL; AY063920; AAL36276.1; -; mRNA.
DR EMBL; AY091247; AAM14186.1; -; mRNA.
DR EMBL; AK317356; BAH20028.1; -; mRNA.
DR PIR; T00810; T00810.
DR RefSeq; NP_001031525.1; NM_001036448.2.
DR RefSeq; NP_001325243.1; NM_001336924.1.
DR RefSeq; NP_181685.1; NM_129717.5.
DR RefSeq; NP_850352.1; NM_180021.5.
DR AlphaFoldDB; O22216; -.
DR SMR; O22216; -.
DR BioGRID; 4089; 3.
DR STRING; 3702.AT2G41540.2; -.
DR PaxDb; O22216; -.
DR PRIDE; O22216; -.
DR ProteomicsDB; 248507; -.
DR EnsemblPlants; AT2G41540.1; AT2G41540.1; AT2G41540.
DR EnsemblPlants; AT2G41540.2; AT2G41540.2; AT2G41540.
DR EnsemblPlants; AT2G41540.3; AT2G41540.3; AT2G41540.
DR EnsemblPlants; AT2G41540.4; AT2G41540.4; AT2G41540.
DR GeneID; 818752; -.
DR Gramene; AT2G41540.1; AT2G41540.1; AT2G41540.
DR Gramene; AT2G41540.2; AT2G41540.2; AT2G41540.
DR Gramene; AT2G41540.3; AT2G41540.3; AT2G41540.
DR Gramene; AT2G41540.4; AT2G41540.4; AT2G41540.
DR KEGG; ath:AT2G41540; -.
DR Araport; AT2G41540; -.
DR TAIR; locus:2062734; AT2G41540.
DR eggNOG; KOG2711; Eukaryota.
DR HOGENOM; CLU_029303_2_0_1; -.
DR InParanoid; O22216; -.
DR OMA; RICGAAK; -.
DR OrthoDB; 476066at2759; -.
DR PhylomeDB; O22216; -.
DR BioCyc; ARA:AT2G41540-MON; -.
DR BRENDA; 1.1.1.8; 399.
DR PRO; PR:O22216; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22216; baseline and differential.
DR Genevisible; O22216; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
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; TAS:TAIR.
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 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 2: Evidence at transcript level;
KW Cytoplasm; NAD; Oxidoreductase; Reference proteome; Stress response.
FT CHAIN 1..462
FT /note="Glycerol-3-phosphate dehydrogenase [NAD(+)] GPDHC1,
FT cytosolic"
FT /id="PRO_0000420176"
FT ACT_SITE 285
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 48..53
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 235
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 347..348
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 347
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 375
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT CONFLICT 316
FT /note="E -> G (in Ref. 5; BAH20028)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 462 AA; 51491 MW; AD40AF1F464C4908 CRC64;
MVGSIEAKSL QSNGSVHHIG LNLEEKLDEF RRLLGKSEKD PLRIVSVGAG AWGSVFAALL
QESYGGFRDK FQIRIWRRAG RAVDRETAEH LFEVINSRED ILRRLIRRCA YLKYVEARLG
DRTLYADEIL KDGFCLNMVD TPLCPLKVVT NLQEAVWDAD IVVNGLPSTE TREVFEEISK
YWKERITVPI IISLSKGIET ALEPVPHIIT PTKMIHQATG VPIDNVLYLG GPNIAAEIYN
KEYANARICG AAKWRKPLAK FLRQPHFIVW DNSDLVTHEV MGGLKNVYAI GAGMVAALTN
ESATSKSVYF AHCTSEMIFI THLLAEEPEK LAGPLLADTY VTLLKGRNAW YGQMLAKGEI
NRDMGDSISG KGMIQGVSAV GAFYQLLSQS SLSILPSEEK KPVAPVESCP ILKTLYKILI
TREQSTQAIL QALRDETLND PRDRIEIAQS HAFYRPSLLG QP
