ID Q8A5W3_BACTN Unreviewed; 345 AA.
AC Q8A5W3;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 24-JAN-2024, entry version 156.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU000439};
DE EC=1.1.1.94 {ECO:0000256|RuleBase:RU000439};
GN OrderedLocusNames=BT_2123 {ECO:0000313|EMBL:AAO77230.1};
OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=226186 {ECO:0000313|EMBL:AAO77230.1, ECO:0000313|Proteomes:UP000001414};
RN [1] {ECO:0000313|EMBL:AAO77230.1, ECO:0000313|Proteomes:UP000001414}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50 {ECO:0000313|Proteomes:UP000001414};
RX PubMed=12663928; DOI=10.1126/science.1080029;
RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA Hooper L.V., Gordon J.I.;
RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL Science 299:2074-2076(2003).
RN [2] {ECO:0000313|EMBL:AAO77230.1, ECO:0000313|Proteomes:UP000001414}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50 {ECO:0000313|Proteomes:UP000001414};
RX PubMed=19321416; DOI=10.1073/pnas.0901529106;
RA Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S.,
RA Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L.,
RA Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C.,
RA Hettich R.L., Gordon J.I.;
RT "Characterizing a model human gut microbiota composed of members of its two
RT dominant bacterial phyla.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009).
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;
CC Evidence={ECO:0000256|RuleBase:RU000439};
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; AE015928; AAO77230.1; -; Genomic_DNA.
DR RefSeq; NP_811036.1; NC_004663.1.
DR AlphaFoldDB; Q8A5W3; -.
DR STRING; 226186.BT_2123; -.
DR PaxDb; 226186-BT_2123; -.
DR DNASU; 1074249; -.
DR EnsemblBacteria; AAO77230; AAO77230; BT_2123.
DR KEGG; bth:BT_2123; -.
DR PATRIC; fig|226186.12.peg.2185; -.
DR eggNOG; COG0240; Bacteria.
DR HOGENOM; CLU_033449_0_0_10; -.
DR InParanoid; Q8A5W3; -.
DR OMA; NRMFGNM; -.
DR OrthoDB; 9812273at2; -.
DR Proteomes; UP000001414; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0047952; F:glycerol-3-phosphate dehydrogenase [NAD(P)+] activity; IBA:GO_Central.
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:0006072; P:glycerol-3-phosphate metabolic process; IBA:GO_Central.
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; 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 Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW NAD {ECO:0000256|PIRSR:PIRSR000114-3, ECO:0000256|RuleBase:RU000437};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000437};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW Reference proteome {ECO:0000313|Proteomes:UP000001414}.
FT DOMAIN 20..176
FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF01210"
FT DOMAIN 197..334
FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF07479"
FT ACT_SITE 208
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-1"
FT BINDING 123
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-2"
FT BINDING 157
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
FT BINDING 272..273
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-2"
FT BINDING 272
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
SQ SEQUENCE 345 AA; 38659 MW; F22A52797A8268ED CRC64;
MTNSQLSTFN FQLNMKLPGK IAIMGGGSWA TAIAKMCLAQ EDSINWYMRR DDRIADFKRL
GHNPAYLTGV KFDTKRITFS SNINDVVKES DTLIFVTPSP YLKAHLKKLK TKIKDKFIIT
AIKGIVPDDN VIVSEYFTKE YGVPPENIAV LAGPCHAEEV ALERLSYLTI ACPDKDKARI
FARRLGSSFI KTSVSDDVAG IEYSSVLKNV YAIAAGICSG LKYGDNFQAV LISNAIQEMN
RFLNTVHPLN RNVDDSVYLG DLLVTGYSNF SRNRTFGSMI GKGYSVKSAQ IEMEMIAEGY
YGTKCIKEIN KHHHVNMPIL DAVYNILYER ISPMIEIKLL TDSFR
//