ID Q6VNX5_DROST Unreviewed; 255 AA.
AC Q6VNX5;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 24-JAN-2024, entry version 99.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)] {ECO:0000256|RuleBase:RU361243};
DE EC=1.1.1.8 {ECO:0000256|RuleBase:RU361243};
DE Flags: Fragment;
GN Name=Gpdh {ECO:0000313|EMBL:AAR05887.1,
GN ECO:0000313|FlyBase:FBgn0068581};
OS Drosophila sturtevanti (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=30047 {ECO:0000313|EMBL:AAR05887.1};
RN [1] {ECO:0000313|EMBL:AAR05887.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Drosophila Resource Center 14043-9871.0
RC {ECO:0000313|EMBL:AAR05887.1};
RX PubMed=15008418; DOI=10.1007/s00239-003-0030-3;
RA Powell J.R., Sezzi E., Moriyama E.N., Gleason J.M., Caccone A.;
RT "Analysis of a shift in codon usage in Drosophila.";
RL J. Mol. Evol. 57:S214-S225(2003).
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|ARBA:ARBA00001662,
CC ECO:0000256|RuleBase:RU361243};
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- PATHWAY: Phospholipid metabolism; alpha-glycerophosphate cycle.
CC {ECO:0000256|ARBA:ARBA00005192}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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 EMBL; AY335217; AAR05887.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6VNX5; -.
DR FlyBase; FBgn0068581; Dstu\Gpdh.
DR UniPathway; UPA00086; -.
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: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:UniProtKB-UniRule.
DR GO; GO:0006650; P:glycerophospholipid metabolic process; IEA:UniProtKB-UniPathway.
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:SF8; GLYCEROL-3-PHOSPHATE DEHYDROGENASE [NAD(+)]-RELATED; 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.
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}.
FT DOMAIN 1..88
FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF01210"
FT DOMAIN 109..254
FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF07479"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAR05887.1"
FT NON_TER 255
FT /evidence="ECO:0000313|EMBL:AAR05887.1"
SQ SEQUENCE 255 AA; 27867 MW; 00349C28452D43F6 CRC64;
ADILIFVVPH QFIPNFCKQL LGKIKPNAIA ISLIKGFDKA EGGGIDLISH IITRHLKIPC
AVLMGANLAN EVAEGNFCET TIGCTDKKYG KVLRDLFQAN HFRVVVVEDA DAVEVCGALK
NIVACGAGFV DGLKLGDNTK AAVIRLGLME MIRFVDVFYP GSKLSTFFES CGVADLITTC
YGGRNRRVSE AFVTSGKTIE ELEKEMLNGQ KLQGPPTAEE VNYMLKNKGL EDKFPLFTAI
HKICTNQLKP KDLID
//