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   24-JAN-2024, entry version 159.
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.O22216; -.
DR   PaxDb; 3702-AT2G41540-2; -.
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; AT2G41540; GPDHC1.
DR   eggNOG; KOG2711; Eukaryota.
DR   HOGENOM; CLU_029303_2_0_1; -.
DR   InParanoid; O22216; -.
DR   OMA; SKCSAQH; -.
DR   OrthoDB; 1201464at2759; -.
DR   PhylomeDB; O22216; -.
DR   BioCyc; ARA:AT2G41540-MONOMER; -.
DR   BRENDA; 1.1.1.8; 399.
DR   PRO; PR:O22216; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O22216; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:TAIR.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0047952; F:glycerol-3-phosphate dehydrogenase [NAD(P)+] activity; IEA:UniProtKB-EC.
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   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
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   PANTHER; PTHR11728; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11728:SF30; GLYCEROL-3-PHOSPHATE DEHYDROGENASE [NAD(+)] GPDHC1, CYTOSOLIC; 1.
DR   Pfam; PF07479; NAD_Gly3P_dh_C; 1.
DR   Pfam; PF01210; NAD_Gly3P_dh_N; 1.
DR   PRINTS; PR00077; GPDHDRGNASE.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   Genevisible; O22216; AT.
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
//