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Database: UniProt
Entry: Q9BLK4_9MUSC
LinkDB: Q9BLK4_9MUSC
Original site: Q9BLK4_9MUSC 
ID   Q9BLK4_9MUSC            Unreviewed;       143 AA.
AC   Q9BLK4;
DT   01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2001, sequence version 1.
DT   24-JAN-2024, entry version 109.
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:BAB39749.1,
GN   ECO:0000313|FlyBase:FBgn0044270};
OS   Drosophila lacteicornis.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=67531 {ECO:0000313|EMBL:BAB39749.1};
RN   [1] {ECO:0000313|EMBL:BAB39749.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Whole body {ECO:0000313|EMBL:BAB39749.1};
RX   PubMed=11277633; DOI=10.1006/mpev.2000.0893;
RA   Goto S.G., Kimura M.T.;
RT   "Phylogenetic utility of mitochondrial COI and nuclear Gpdh genes in
RT   Drosophila.";
RL   Mol. Phylogenet. Evol. 18:404-422(2001).
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; AB032142; BAB39749.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9BLK4; -.
DR   FlyBase; FBgn0044270; Dlar\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: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; 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: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          5..50
FT                   /note="Glycerol-3-phosphate dehydrogenase NAD-dependent N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01210"
FT   DOMAIN          71..143
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:BAB39749.1"
FT   NON_TER         143
FT                   /evidence="ECO:0000313|EMBL:BAB39749.1"
SQ   SEQUENCE   143 AA;  15306 MW;  06474D166952BBA4 CRC64;
     KAEGGGIDLI SHIITRHLKI PCAVLMGANL ANEVAEGNFC ETTIGCTDKK YGKVLRDLFQ
     ANHFRVVVVD DADAVEVCGA LKNIVACGAG FVDGLKLGDN TKAAVIRLGL MEMIRFVDVF
     YPGSKLSTFF ESCGVADLIT TCY
//
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