GPDA_DROEZ
ID GPDA_DROEZ Reviewed; 350 AA.
AC Q27567;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)], cytoplasmic;
DE Short=GPD-C;
DE Short=GPDH-C;
DE EC=1.1.1.8;
GN Name=Gpdh1; Synonyms=Gpdh;
OS Drosophila ezoana (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=47313;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8522168; DOI=10.1007/bf01439583;
RA Tominaga H., Narise S.;
RT "Sequence evolution of the Gpdh gene in the Drosophila virilis species
RT group.";
RL Genetica 96:293-302(1995).
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 -!- PATHWAY: Phospholipid metabolism; alpha-glycerophosphate cycle.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; D50091; BAA20288.1; -; Genomic_DNA.
DR AlphaFoldDB; Q27567; -.
DR SMR; Q27567; -.
DR FlyBase; FBgn0015644; Dezo\Gpdh1.
DR UniPathway; UPA00086; -.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0004367; F:glycerol-3-phosphate dehydrogenase [NAD+] 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 GO; GO:0006650; P:glycerophospholipid metabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.1040.10; -; 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 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; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR03376; glycerol3P_DH; 1.
DR PROSITE; PS00957; NAD_G3PDH; 1.
PE 3: Inferred from homology;
KW Cytoplasm; NAD; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..350
FT /note="Glycerol-3-phosphate dehydrogenase [NAD(+)],
FT cytoplasmic"
FT /id="PRO_0000138073"
FT ACT_SITE 206
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"
FT BINDING 98
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
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 155
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 270..271
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 270
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 299
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 350 AA; 38339 MW; 817BD7351301BF55 CRC64;
MAEKVNVCIV GSGNWGSAIA KIVGANASAL PEFEERVTMF VYEEMIDGKK LTEIINETHE
NVKYLKGHKL PTNVVAVPDL VEAAKNADIL IFVVPHQFIP NFCKQLLGKI KPNAIAISLI
KGFDKAEGGG IDLISHIITR HLKIPCAVLM GANLANEVAE GNFCETTIGC TDKKYGKVLR
DLFQANHFRV VVVEDADAVE VCGALKNIVA CGAGFVDGLK LGDNTKAAVI RLGLMEMIRF
VDVFYPGSKL STFFESCGVA DLITTCYGGR NRRVSEAFVT SGKTIEELEK EMLNGQKLQG
PPTAEEVNYM LKNKGLEDKF PLFTAIHKIC TNQLKPKDLI DCIRNHPEHM
