ID GPDA_TAKRU Reviewed; 351 AA.
AC O57656;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 24-JAN-2024, entry version 131.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)], cytoplasmic;
DE Short=GPD-C;
DE Short=GPDH-C;
DE EC=1.1.1.8 {ECO:0000250|UniProtKB:P21695};
GN Name=gpd1; Synonyms=lg3p;
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Riboldi Tunnicliffe G.R., Nyakatura G., Bauer D., Elgar G.S., Perret X.,
RA Brenner S., Rosenthal A.;
RT "Sequencing of a 62kb region of Fugu rubripes around the G6PD locus.";
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Has glycerol-3-phosphate dehydrogenase activity.
CC {ECO:0000250|UniProtKB:P21695}.
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:0000250|UniProtKB:P21695};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11093;
CC Evidence={ECO:0000250|UniProtKB:P21695};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P21695}.
CC -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; U72484; AAB96364.1; -; Genomic_DNA.
DR RefSeq; XP_003963492.1; XM_003963443.2.
DR AlphaFoldDB; O57656; -.
DR SMR; O57656; -.
DR STRING; 31033.ENSTRUP00000070996; -.
DR Ensembl; ENSTRUT00000091626.1; ENSTRUP00000064491.1; ENSTRUG00000001679.3.
DR GeneID; 101071719; -.
DR KEGG; tru:101071719; -.
DR eggNOG; KOG2711; Eukaryota.
DR GeneTree; ENSGT00390000003114; -.
DR HOGENOM; CLU_033449_2_2_1; -.
DR InParanoid; O57656; -.
DR OrthoDB; 3675564at2759; -.
DR TreeFam; TF300836; -.
DR Proteomes; UP000005226; Chromosome 3.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0047952; F:glycerol-3-phosphate dehydrogenase [NAD(P)+] activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; IPR017751; G3P_DH_NAD-dep_euk.
DR InterPro; IPR011128; G3P_DH_NAD-dep_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR03376; glycerol3P_DH; 1.
DR PANTHER; PTHR11728; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11728:SF32; GLYCEROL-3-PHOSPHATE DEHYDROGENASE [NAD(+)], CYTOPLASMIC; 1.
DR Pfam; PF07479; NAD_Gly3P_dh_C; 1.
DR Pfam; PF01210; NAD_Gly3P_dh_N; 1.
DR PIRSF; PIRSF000114; Glycerol-3-P_dh; 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.
DR PROSITE; PS00957; NAD_G3PDH; 1.
PE 3: Inferred from homology;
KW Cytoplasm; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..351
FT /note="Glycerol-3-phosphate dehydrogenase [NAD(+)],
FT cytoplasmic"
FT /id="PRO_0000138078"
FT ACT_SITE 205
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 11..16
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P21695"
FT BINDING 121
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P21695"
FT BINDING 271..272
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 271
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P21695"
FT BINDING 298
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P21695"
FT BINDING 300
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P21695"
SQ SEQUENCE 351 AA; 38078 MW; 4A56E07FE3A5D966 CRC64;
MAAPKKVCII GSGNWGSAIA KIVGANAAQN SKFDKTVKMW VFEETVNGRK LTEIINTEHE
NVKYLPGHKL PTNVLAVPDL VEASKDADIL VFVIPHQFIG KVCDTMSGNI KKEAIGISLI
KGVDEGPDGL KLISDVIQEK LGITMSVLMG ANIANEVADE KFCETTIGCK NKSHGPLLKE
LMQTINFRVT VVEEYDVVEI CGALKNIVAV GAGFCDGLGF GDNTKAAVIR LGLMEMIAFA
RIFCTAGPVS SATFLESCGV ADLITTCYGG RNRKVAKAFV KTGKSIEELE KEMLEGQKLQ
GPATAAEVYR ILKHKNLIDK FPLFNAVYQI CYQGHPVSEF ISCLQNHPEH M
//
