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Database: UniProt
Entry: Q9SS48
LinkDB: Q9SS48
Original site: Q9SS48 
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   16-JAN-2019, entry version 107.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase SDP6, mitochondrial;
DE            EC=1.1.5.3;
DE   AltName: Full=Protein SUGAR-DEPENDENT 6;
DE   Flags: Precursor;
GN   Name=SDP6; OrderedLocusNames=At3g10370; ORFNames=F14P13.3;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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.,
RA   Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
RA   Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
RA   De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
RA   Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
RA   Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
RA   Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
RA   Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
RA   Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
RA   Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
RA   Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
RA   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.,
RA   Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
RA   Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
RA   Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
RA   Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
RA   Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
RA   Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
RA   Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
RA   Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
RA   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
RT   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
RT   reference 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.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE 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
RT   from Arabidopsis thaliana: evidence for a mitochondrial glycerol-3-
RT   phosphate shuttle in plants.";
RL   FEBS Lett. 536:92-96(2003).
RN   [5]
RP   FUNCTION, 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
CC       NADH/NAD(+) homeostasis. Essential for postgerminative growth and
CC       seedling establishment. {ECO:0000269|PubMed:12586344,
CC       ECO:0000269|PubMed:18599644}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + sn-glycerol 3-phosphate = a quinol +
CC         dihydroxyacetone phosphate; Xref=Rhea:RHEA:18977,
CC         ChEBI:CHEBI:24646, ChEBI:CHEBI:57597, ChEBI:CHEBI:57642,
CC         ChEBI:CHEBI:132124; EC=1.1.5.3;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC   -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol
CC       kinase pathway; glycerone phosphate from sn-glycerol 3-phosphate
CC       (anaerobic route): step 1/1.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:12586344}.
CC   -!- TISSUE SPECIFICITY: Expressed in germinating seedlings. Also
CC       detected in roots, leaves, flowers, developing siliques and
CC       germinating seeds. {ECO:0000269|PubMed:12586344}.
CC   -!- MISCELLANEOUS: Plants lacking SDP6 are impaired in gluconeogenesis
CC       during postgerminative growth.
CC   -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000305}.
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   UniGene; At.18427; -.
DR   ProteinModelPortal; Q9SS48; -.
DR   SMR; Q9SS48; -.
DR   BioGrid; 5533; 1.
DR   STRING; 3702.AT3G10370.1; -.
DR   PaxDb; Q9SS48; -.
DR   PRIDE; Q9SS48; -.
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   eggNOG; COG0578; LUCA.
DR   HOGENOM; HOG000004813; -.
DR   InParanoid; Q9SS48; -.
DR   KO; K00111; -.
DR   OMA; MDNPTVK; -.
DR   OrthoDB; 669193at2759; -.
DR   PhylomeDB; Q9SS48; -.
DR   BioCyc; ARA:AT3G10370-MONOMER; -.
DR   BioCyc; MetaCyc:AT3G10370-MONOMER; -.
DR   Reactome; R-ATH-1483166; Synthesis of PA.
DR   Reactome; R-ATH-163560; Triglyceride catabolism.
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: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; IDA:TAIR.
DR   GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IDA:TAIR.
DR   GO; GO:0004367; F:glycerol-3-phosphate dehydrogenase [NAD+] activity; IBA:GO_Central.
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:0046168; P:glycerol-3-phosphate catabolic process; IBA:GO_Central.
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   Complete proteome; FAD; Flavoprotein; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Oxidoreductase; Reference proteome;
KW   Transit peptide.
FT   TRANSIT       1      ?       Mitochondrion. {ECO:0000255}.
FT   CHAIN         ?    629       Glycerol-3-phosphate dehydrogenase SDP6,
FT                                mitochondrial.
FT                                /FTId=PRO_0000355965.
FT   NP_BIND      75    103       FAD. {ECO:0000255}.
FT   MUTAGEN      86     86       S->F: In spd6-2; loss of 90% of activity.
FT   MUTAGEN     546    546       E->G: In spd6-1; loss of 90% of activity.
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
//
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