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Database: UniProt
Entry: A0A0E0HYC7_ORYNI
LinkDB: A0A0E0HYC7_ORYNI
Original site: A0A0E0HYC7_ORYNI 
ID   A0A0E0HYC7_ORYNI        Unreviewed;       455 AA.
AC   A0A0E0HYC7;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)] {ECO:0000256|RuleBase:RU361243};
DE            EC=1.1.1.8 {ECO:0000256|RuleBase:RU361243};
OS   Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4536 {ECO:0000313|EnsemblPlants:ONIVA07G06490.1};
RN   [1] {ECO:0000313|EnsemblPlants:ONIVA07G06490.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA07G06490.1};
RA   Wing R.A., Hsing Y.;
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:ONIVA07G06490.1}
RP   IDENTIFICATION.
RC   STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA07G06490.1};
RG   EnsemblPlants;
RL   Submitted (APR-2015) 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   AlphaFoldDB; A0A0E0HYC7; -.
DR   STRING; 4536.A0A0E0HYC7; -.
DR   EnsemblPlants; ONIVA07G06490.1; ONIVA07G06490.1; ONIVA07G06490.
DR   Gramene; ONIVA07G06490.1; ONIVA07G06490.1; ONIVA07G06490.
DR   eggNOG; KOG2711; Eukaryota.
DR   OMA; KYHVKMP; -.
DR   Proteomes; UP000006591; Unassembled WGS sequence.
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:0045017; P:glycerolipid biosynthetic process; IEA:EnsemblPlants.
DR   GO; GO:0009627; P:systemic acquired resistance; IEA:EnsemblPlants.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   HAMAP; MF_00394; NAD_Glyc3P_dehydrog; 1.
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:SF1; GLYCEROL-3-PHOSPHATE DEHYDROGENASE [NAD(+)] 2, CHLOROPLASTIC; 1.
DR   Pfam; PF07479; NAD_Gly3P_dh_C; 1.
DR   Pfam; PF01210; NAD_Gly3P_dh_N; 2.
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.
DR   PROSITE; PS00957; NAD_G3PDH; 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:UP000006591}.
FT   DOMAIN          109..184
FT                   /note="Glycerol-3-phosphate dehydrogenase NAD-dependent N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01210"
FT   DOMAIN          202..283
FT                   /note="Glycerol-3-phosphate dehydrogenase NAD-dependent N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01210"
FT   DOMAIN          303..443
FT                   /note="Glycerol-3-phosphate dehydrogenase NAD-dependent C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07479"
FT   REGION          57..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   455 AA;  48398 MW;  ADF56D51C92FEEA7 CRC64;
     MAAAAAATFL PHTPTPRRRL AVAVHSPTRR RLSLVFSGPP DGALSVAAAE EKADAGEEAA
     AAVSAPRGGG GGGGKERRRV VRKAWEKLVR WSRSWRRRNR SDVVETTRKV VVLGGGSFGT
     AMAVQVAAKK ADLEVSMLLR DDLVCRSINH SHINWLPENI TATTSASDAL AGADFCFHAV
     PVFRTVHYKS LFSAMGVPFP LVTLEFSSSF LEGISTHVDP KLPFISLSKG LELNTLRTMS
     QIIPQALGNP RQPFIVLSGP SFAIELMNKL PTAMVVASKD KKLAAAVQQL LASPNLRIST
     SNDVTGVEIA GALKNVLAIA AGIVEGMHLG NNCMAALVAQ GCSEIRWLAT KMGAKPTTLS
     GLSGSGDIML TCFVNLSRNR NVGLRLGSGE KLDEIMNSMN QVAEGVSTAG AVIALAQKYH
     VKMPVLTAVA RIIDNELTPK KAVMELMNLP QVEEV
//
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