SDP6_ARATH
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 03-AUG-2022, entry version 121.
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 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, 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 [5]
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 = a quinol +
CC dihydroxyacetone phosphate; 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; 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 STRING; 3702.AT3G10370.1; -.
DR PaxDb; Q9SS48; -.
DR PRIDE; Q9SS48; -.
DR ProteomicsDB; 234480; -.
DR EnsemblPlants; AT3G10370.1; AT3G10370.1; AT3G10370.
DR GeneID; 820199; -.
DR Gramene; AT3G10370.1; AT3G10370.1; AT3G10370.
DR KEGG; ath:AT3G10370; -.
DR Araport; AT3G10370; -.
DR TAIR; locus:2076314; AT3G10370.
DR eggNOG; KOG0042; Eukaryota.
DR HOGENOM; CLU_015740_4_3_1; -.
DR InParanoid; Q9SS48; -.
DR OMA; CIVNAAG; -.
DR OrthoDB; 669193at2759; -.
DR PhylomeDB; Q9SS48; -.
DR BioCyc; ARA:AT3G10370-MON; -.
DR BioCyc; MetaCyc:AT3G10370-MON; -.
DR UniPathway; UPA00618; UER00673.
DR PRO; PR:Q9SS48; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SS48; baseline and differential.
DR Genevisible; Q9SS48; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IDA:TAIR.
DR GO; GO:0052591; F:sn-glycerol-3-phosphate:ubiquinone-8 oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0019563; P:glycerol catabolic process; IMP:TAIR.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:InterPro.
DR GO; GO:0006127; P:glycerophosphate shuttle; IMP:TAIR.
DR Gene3D; 1.10.8.870; -; 1.
DR Gene3D; 3.50.50.60; -; 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; PTHR11985; 1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF16901; DAO_C; 1.
DR PRINTS; PR01001; FADG3PDH.
DR SUPFAM; SSF51905; SSF51905; 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
