ID A0A0G0LJL7_9BACT Unreviewed; 276 AA.
AC A0A0G0LJL7;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 22-FEB-2023, entry version 34.
DE SubName: Full=Glycerol-3-phosphate dehydrogenase [NAD(P)+] {ECO:0000313|EMBL:KKQ88135.1};
GN ORFNames=UT09_C0003G0037 {ECO:0000313|EMBL:KKQ88135.1};
OS Parcubacteria group bacterium GW2011_GWF2_38_8.
OC Bacteria.
OX NCBI_TaxID=1618961 {ECO:0000313|EMBL:KKQ88135.1, ECO:0000313|Proteomes:UP000034262};
RN [1] {ECO:0000313|EMBL:KKQ88135.1, ECO:0000313|Proteomes:UP000034262}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00011009}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKQ88135.1}.
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DR EMBL; LBVM01000003; KKQ88135.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0LJL7; -.
DR Proteomes; UP000034262; Unassembled WGS sequence.
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:InterPro.
DR GO; GO:0051287; F:NAD binding; 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:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
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: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; 2.
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 Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW NAD {ECO:0000256|PIRSR:PIRSR000114-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264}.
FT DOMAIN 30..114
FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF01210"
FT DOMAIN 135..270
FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF07479"
FT ACT_SITE 146
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-1"
FT BINDING 67
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-2"
FT BINDING 97
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
FT BINDING 205..206
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-2"
FT BINDING 205
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
SQ SEQUENCE 276 AA; 30089 MW; 6E5DBDFB2D362648 CRC64;
MKIAVLGNGI FGSAMASYLS KKRHEVVFDM IDNSEIIFVC STSNLVLSSL LKLQKEMTNQ
KIIICSKGFA EEGKLISEVL KGNFKNEIFF LYGPTLAEEL EKGVPSSMVL AGGNGKEEIK
KQIESKNLRV ELSDDVIGVE ISATLKNVMA LFIGIAQGAG YGQNTAAFVF TKAVQEVKNI
GLALGGKVET FLGLTCVGDL FLSSRNRLFG IELGKGRKLD EISSETGHTP AGIFDLKNAQ
RMVKKLDIKA PIIESLYKIV FENCPVRDTI KEIISN
//
