ID E0SLJ7_DICD3 Unreviewed; 339 AA.
AC E0SLJ7;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(P)+] {ECO:0000256|HAMAP-Rule:MF_00394};
DE EC=1.1.1.94 {ECO:0000256|HAMAP-Rule:MF_00394};
DE AltName: Full=NAD(P)H-dependent glycerol-3-phosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00394};
GN Name=gpsA {ECO:0000256|HAMAP-Rule:MF_00394,
GN ECO:0000313|EMBL:ADN00519.1};
GN OrderedLocusNames=Dda3937_02048 {ECO:0000313|EMBL:ADN00519.1};
OS Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Dickeya.
OX NCBI_TaxID=198628 {ECO:0000313|EMBL:ADN00519.1, ECO:0000313|Proteomes:UP000006859};
RN [1] {ECO:0000313|EMBL:ADN00519.1, ECO:0000313|Proteomes:UP000006859}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3937 {ECO:0000313|EMBL:ADN00519.1,
RC ECO:0000313|Proteomes:UP000006859};
RX PubMed=21217001; DOI=10.1128/JB.01513-10;
RA Glasner J.D., Yang C.H., Reverchon S., Hugouvieux-Cotte-Pattat N.,
RA Condemine G., Bohin J.P., Van Gijsegem F., Yang S., Franza T., Expert D.,
RA Plunkett G. III, San Francisco M.J., Charkowski A.O., Py B., Bell K.,
RA Rauscher L., Rodriguez-Palenzuela P., Toussaint A., Holeva M.C., He S.Y.,
RA Douet V., Boccara M., Blanco C., Toth I., Anderson B.D., Biehl B.S.,
RA Mau B., Flynn S.M., Barras F., Lindeberg M., Birch P.R., Tsuyumu S.,
RA Shi X., Hibbing M., Yap M.N., Carpentier M., Dassa E., Umehara M.,
RA Kim J.F., Rusch M., Soni P., Mayhew G.F., Fouts D.E., Gill S.R.,
RA Blattner F.R., Keen N.T., Perna N.T.;
RT "Genome sequence of the plant-pathogenic bacterium Dickeya dadantii 3937.";
RL J. Bacteriol. 193:2076-2077(2011).
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=1.1.1.94; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00394};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate
CC + H(+) + NADPH; Xref=Rhea:RHEA:11096, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.1.1.94; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00394, ECO:0000256|RuleBase:RU000439};
CC -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism.
CC {ECO:0000256|HAMAP-Rule:MF_00394}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00394}.
CC -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00011009,
CC ECO:0000256|HAMAP-Rule:MF_00394, ECO:0000256|RuleBase:RU000437}.
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DR EMBL; CP002038; ADN00519.1; -; Genomic_DNA.
DR RefSeq; WP_013319916.1; NC_014500.1.
DR AlphaFoldDB; E0SLJ7; -.
DR STRING; 198628.Dda3937_02048; -.
DR GeneID; 9735820; -.
DR KEGG; ddd:Dda3937_02048; -.
DR PATRIC; fig|198628.6.peg.4270; -.
DR eggNOG; COG0240; Bacteria.
DR HOGENOM; CLU_033449_0_2_6; -.
DR OrthoDB; 9812273at2; -.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000006859; Chromosome.
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-UniRule.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0046167; P:glycerol-3-phosphate biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:InterPro.
DR GO; GO:0006650; P:glycerophospholipid metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-UniRule.
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; 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 {ECO:0000256|HAMAP-Rule:MF_00394};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW Rule:MF_00394};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW Rule:MF_00394};
KW NAD {ECO:0000256|HAMAP-Rule:MF_00394, ECO:0000256|PIRSR:PIRSR000114-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00394};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209,
KW ECO:0000256|HAMAP-Rule:MF_00394};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264, ECO:0000256|HAMAP-
KW Rule:MF_00394}; Reference proteome {ECO:0000313|Proteomes:UP000006859}.
FT DOMAIN 8..162
FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF01210"
FT DOMAIN 184..323
FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF07479"
FT ACT_SITE 195
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394,
FT ECO:0000256|PIRSR:PIRSR000114-1"
FT BINDING 12..17
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394,
FT ECO:0000256|PIRSR:PIRSR000114-3"
FT BINDING 110
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394"
FT BINDING 110
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394,
FT ECO:0000256|PIRSR:PIRSR000114-2"
FT BINDING 143
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394,
FT ECO:0000256|PIRSR:PIRSR000114-3"
FT BINDING 259..260
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394,
FT ECO:0000256|PIRSR:PIRSR000114-2"
FT BINDING 259
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394,
FT ECO:0000256|PIRSR:PIRSR000114-3"
FT BINDING 285
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394"
SQ SEQUENCE 339 AA; 35990 MW; 582840F494FAEF96 CRC64;
MNSSDAAMTV IGAGSYGTAL AITVARNGHR VVLWGHDPVH IQALQAARCN QAFLPDVPFP
DTLQLEADLS QALAASRNIL VVVPSHVFGD VLRQLKPHLR ADARLVWATK GLEAETGRLL
QDVAREALGN TIPLAVLSGP TFAKELAAGL PTAIALASTD QPFSDDLQHL LHCGKSFRVY
SNPDFVGVQL GGAVKNVIAI GAGMSDGMGF GANARTALIT RGLAEMTRLG VALGADPTTF
MGMAGLGDLV LTCTDNQSRN RRFGMMLGQG MDVVSAQNQI GQVVEGYRNT KEVMALAQRY
GVEMPITEQL WQVLYCGKDA REAALSLLGR ARKDESASL
//
