ID   SDP6_ARATH              Reviewed;         629 AA.
AC   Q9SS48;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   02-SEP-2026, entry version 138.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase SDP6, mitochondrial {ECO:0000303|PubMed:18599644};
DE            EC=1.1.5.3 {ECO:0000269|PubMed:12586344, ECO:0000269|PubMed:18599644};
DE   AltName: Full=Protein SUGAR-DEPENDENT 6 {ECO:0000303|PubMed:18599644};
DE   Flags: Precursor;
GN   Name=SDP6 {ECO:0000303|PubMed:18599644};
GN   OrderedLocusNames=At3g10370 {ECO:0000312|Araport:AT3G10370};
GN   ORFNames=F14P13.3 {ECO:0000312|EMBL:AAF02807.1};
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;
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   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RT   "Community-consensus reference genome of Arabidopsis thaliana Col-0.";
RL   Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases.
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   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=12586344; DOI=10.1016/s0014-5793(03)00033-4;
RA   Shen W., Wei Y., Dauk M., Zheng Z., Zou J.;
RT   "Identification of a mitochondrial glycerol-3-phosphate dehydrogenase from
RT   Arabidopsis thaliana: evidence for a mitochondrial glycerol-3-phosphate
RT   shuttle in plants.";
RL   FEBS Lett. 536:92-96(2003).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, AND MUTANTS SPD6-1 AND SPD6-2.
RX   PubMed=18599644; DOI=10.1104/pp.108.123703;
RA   Quettier A.-L., Shaw E., Eastmond P.J.;
RT   "SUGAR-DEPENDENT6 encodes a mitochondrial flavin adenine dinucleotide-
RT   dependent glycerol-3-p dehydrogenase, which is required for glycerol
RT   catabolism and post germinative seedling growth in Arabidopsis.";
RL   Plant Physiol. 148:519-528(2008).
CC   -!- FUNCTION: Required for glycerol catabolism and involved in NADH/NAD(+)
CC       homeostasis (PubMed:12586344, PubMed:18599644). Essential for
CC       postgerminative growth and seedling establishment (PubMed:18599644).
CC       {ECO:0000269|PubMed:12586344, ECO:0000269|PubMed:18599644}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + sn-glycerol 3-phosphate = dihydroxyacetone
CC         phosphate + a quinol; Xref=Rhea:RHEA:18977, ChEBI:CHEBI:24646,
CC         ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, ChEBI:CHEBI:132124; EC=1.1.5.3;
CC         Evidence={ECO:0000269|PubMed:12586344, ECO:0000269|PubMed:18599644};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18978;
CC         Evidence={ECO:0000269|PubMed:12586344, ECO:0000269|PubMed:18599644};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000269|PubMed:12586344};
CC   -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase
CC       pathway; glycerone phosphate from sn-glycerol 3-phosphate (anaerobic
CC       route): step 1/1. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:12586344}; Peripheral membrane protein
CC       {ECO:0000305|PubMed:12586344}.
CC   -!- TISSUE SPECIFICITY: Expressed in germinating seedlings. Also detected
CC       in roots, leaves, flowers, developing siliques and germinating seeds.
CC       {ECO:0000269|PubMed:12586344}.
CC   -!- MISCELLANEOUS: Plants lacking SDP6 are impaired in gluconeogenesis
CC       during postgerminative growth. {ECO:0000269|PubMed:18599644}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000305}.
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DR   EMBL; AC009400; AAF02807.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE74897.1; -; Genomic_DNA.
DR   EMBL; OZ408685; CAO7040339.1; -; Genomic_DNA.
DR   EMBL; AY063863; AAL36219.1; -; mRNA.
DR   EMBL; AY096363; AAM20004.1; -; mRNA.
DR   RefSeq; NP_187648.1; NM_111872.6.
DR   AlphaFoldDB; Q9SS48; -.
DR   SMR; Q9SS48; -.
DR   BioGRID; 5533; 1.
DR   FunCoup; Q9SS48; 2567.
DR   STRING; 3702.Q9SS48; -.
DR   PaxDb; 3702-Q9SS48; -.
DR   ProteomicsDB; 234480; -.
DR   GeneID; 820199; -.
DR   KEGG; ath:AT3G10370; -.
DR   Araport; AT3G10370; -.
DR   TAIR; AT3G10370; SDP6.
DR   eggNOG; KOG0042; Eukaryota.
DR   HOGENOM; CLU_015740_4_3_1; -.
DR   InParanoid; Q9SS48; -.
DR   OMA; PHIVKPM; -.
DR   OrthoDB; 264015at2759; -.
DR   PhylomeDB; Q9SS48; -.
DR   BioCyc; ARA:AT3G10370-MONOMER; -.
DR   BioCyc; MetaCyc:AT3G10370-MONOMER; -.
DR   UniPathway; UPA00618; UER00673.
DR   PRO; PR:Q9SS48; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9SS48; baseline and differential.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005743; C:mitochondrial inner membrane; EXP:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR   GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IDA:TAIR.
DR   GO; GO:0019563; P:glycerol catabolic process; IMP:TAIR.
DR   GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IBA:GO_Central.
DR   GO; GO:0006127; P:glycerol-3-phosphate shuttle; IMP:TAIR.
DR   FunFam; 1.10.8.870:FF:000004; Glycerol-3-phosphate dehydrogenase; 1.
DR   Gene3D; 1.10.8.870; Alpha-glycerophosphate oxidase, cap domain; 1.
DR   Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR031656; DAO_C.
DR   InterPro; IPR038299; DAO_C_sf.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000447; G3P_DH_FAD-dep.
DR   PANTHER; PTHR11985; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11985:SF15; GLYCEROL-3-PHOSPHATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF16901; DAO_C; 1.
DR   PRINTS; PR01001; FADG3PDH.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00977; FAD_G3PDH_1; 1.
DR   PROSITE; PS00978; FAD_G3PDH_2; 1.
PE   1: Evidence at protein level;
KW   FAD; Flavoprotein; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Oxidoreductase; Reference proteome; Transit peptide.
FT   TRANSIT         1..48
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           49..629
FT                   /note="Glycerol-3-phosphate dehydrogenase SDP6,
FT                   mitochondrial"
FT                   /id="PRO_0000355965"
FT   BINDING         75..103
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         86
FT                   /note="S->F: In spd6-2; loss of 90% of activity."
FT                   /evidence="ECO:0000269|PubMed:18599644"
FT   MUTAGEN         546
FT                   /note="E->G: In spd6-1; loss of 90% of activity."
FT                   /evidence="ECO:0000269|PubMed:18599644"
SQ   SEQUENCE   629 AA;  68451 MW;  CBEA821F268B7DE9 CRC64;
     MSLASIRRLA AGAAVIAAAS GGAVYLSPSV ASSDKGGGPI LDSLRRRLGD PTASVPSRSA
     QESALIAATA SDPLDVLVIG GGATGSGVAL DAVTRGLRVG LVEREDFSSG TSSRSTKLIH
     GGVRYLEKAV FNLDYGQLKL VFHALEERKQ LIENAPHLCH ALPCMTPCFD WFEVIYFWMG
     LKMYDLVAGP RLLHLSRYYS AKESIELFPT LARKGKDKNL RGTVVYYDGQ MNDSRLNVGL
     ACTAALAGAA VLNHAEVVSL ITDDATKRII GARIRNNLTG QEFNSYAKVV VNAAGPFCDS
     IRKMIDEDTK PMICPSSGVH IVLPDYYSPE GMGLIVPKTK DGRVVFMLPW LGRTVAGTTD
     SNTSITSLPE PHEDEIQFIL DAISDYLNIK VRRTDVLSAW SGIRPLAMDP TAKSTESISR
     DHVVFEENPG LVTITGGKWT TYRSMAEDAV DAAIKSGQLK PTNECVTQKL QLLGSYGWEP
     SSFTTLAQQY VRMKKTYGGK VVPGAMDTAA AKHLSHAYGS MADRVATIAQ EEGLGKRLAH
     GHPFLEAEVA YCARHEYCES AVDFIARRCR IAFLDTDAAA RALQRVVEIL ASEHKWDKSR
     QKQELQKAKE FLETFKSSKN AQFNDGKHN
//