ID A0A3Q7FYK7_SOLLC Unreviewed; 464 AA.
AC A0A3Q7FYK7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)] {ECO:0000256|RuleBase:RU361243};
DE EC=1.1.1.8 {ECO:0000256|RuleBase:RU361243};
GN Name=101260923 {ECO:0000313|EnsemblPlants:Solyc04g016330.3.1};
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081 {ECO:0000313|EnsemblPlants:Solyc04g016330.3.1};
RN [1] {ECO:0000313|EnsemblPlants:Solyc04g016330.3.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Heinz 1706 {ECO:0000313|EnsemblPlants:Solyc04g016330.3.1};
RX PubMed=22660326; DOI=10.1038/nature11119;
RG Tomato Genome Consortium;
RT "The tomato genome sequence provides insights into fleshy fruit
RT evolution.";
RL Nature 485:635-641(2012).
RN [2] {ECO:0000313|EnsemblPlants:Solyc04g016330.3.1}
RP IDENTIFICATION.
RC STRAIN=cv. Heinz 1706 {ECO:0000313|EnsemblPlants:Solyc04g016330.3.1};
RG EnsemblPlants;
RL Submitted (JAN-2019) to UniProtKB.
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 Evidence={ECO:0000256|RuleBase:RU361243};
CC -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00011009,
CC ECO:0000256|RuleBase:RU000437}.
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DR RefSeq; XP_004236586.1; XM_004236538.3.
DR AlphaFoldDB; A0A3Q7FYK7; -.
DR STRING; 4081.A0A3Q7FYK7; -.
DR PaxDb; 4081-Solyc04g016330-2-1; -.
DR EnsemblPlants; Solyc04g016330.3.1; Solyc04g016330.3.1; Solyc04g016330.3.
DR GeneID; 101260923; -.
DR Gramene; Solyc04g016330.3.1; Solyc04g016330.3.1; Solyc04g016330.3.
DR KEGG; sly:101260923; -.
DR InParanoid; A0A3Q7FYK7; -.
DR OMA; SVHNHNG; -.
DR OrthoDB; 1201464at2759; -.
DR Proteomes; UP000004994; Chromosome 4.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0047952; F:glycerol-3-phosphate dehydrogenase [NAD(P)+] activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:UniProtKB-UniRule.
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; 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.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|RuleBase:RU000437};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000437};
KW Reference proteome {ECO:0000313|Proteomes:UP000004994}.
FT DOMAIN 148..249
FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF01210"
FT DOMAIN 276..426
FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF07479"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 464 AA; 51761 MW; 90694B7FB414AB5E CRC64;
MVGSIEVKSG NSVYSNGSVH NHNGPEEKLD ELRHILGKSD GDLLRIVCVG AGAWGSVFAA
LLQDSYGQFR DKVQIRIWRR SGRAVDRATA EHLFEVINSR EDVLRRLIRR CAYLKYVEAR
LGDRTLYADE ILKDGFCLNM IDTPFCPLKV VTNLQEAVWD ADLVINGLPS TETREVFKEI
SKYWKERLTV PIIISLAKGI EAELDPVPHI ITPTQMINRA TGVPVENILY LGGPNIASEI
YNKEYANARI CGSEKWRKPL AKFLRQPHFI VWDNSDLVTH EVMGGLKNVY AIGAGMVAAL
TNESATSKSV YFAHCTSEMI FITYLLTEEP ERLAGPLLAD TYVTLLKGRN SWYGQMIAKG
ELSLDMGDSI SGKGTIQGVS AVEAFYELLS QSSLNVLHPG DNKPVAPVEL CPILKTLYKI
LIKREQGTMA ILQALRDENL NDPRDRIEIA QSHAFYRPSL LGQP
//