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Database: UniProt
Entry: A0A3Q7FYK7_SOLLC
LinkDB: A0A3Q7FYK7_SOLLC
Original site: A0A3Q7FYK7_SOLLC 
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
//
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