ID A0A1B1SDI1_9BACT Unreviewed; 322 AA.
AC A0A1B1SDI1; A0A1Z2XKU9;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 2.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU000439};
DE EC=1.1.1.94 {ECO:0000256|RuleBase:RU000439};
GN ORFNames=A4V02_12045 {ECO:0000313|EMBL:ANU64867.2};
OS Muribaculum intestinale.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae;
OC Muribaculum.
OX NCBI_TaxID=1796646 {ECO:0000313|EMBL:ANU64867.2, ECO:0000313|Proteomes:UP000186351};
RN [1] {ECO:0000313|Proteomes:UP000186351}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YL27 {ECO:0000313|Proteomes:UP000186351};
RA Uchimura Y., Wyss M., Brugiroux S., Limenitakis J.P., Stecher B.,
RA McCoy K.D., Macpherson A.J.;
RT "Complete Genome Sequences of Twelve Strains of a Stable Defined Moderately
RT Diverse Mouse Microbiota 2 (sDMDMm2).";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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; CP015402; ANU64867.2; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B1SDI1; -.
DR STRING; 1796646.A4V02_12045; -.
DR KEGG; pary:A4V02_12045; -.
DR OrthoDB; 9812273at2; -.
DR Proteomes; UP000186351; 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-EC.
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; 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:UP000186351}.
FT DOMAIN 1..154
FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF01210"
FT DOMAIN 174..314
FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF07479"
FT ACT_SITE 185
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-1"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-2"
FT BINDING 134
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
FT BINDING 249..250
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-2"
FT BINDING 249
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
SQ SEQUENCE 322 AA; 35781 MW; EFB6B296F0466A75 CRC64;
MGGGSWATAL AKLIIRNEER IIWYMRRDDR IEEFRRIGHN PAYLSDVEFP IDRIDFTSDI
NAAARDADTL LMAMPSPYFK SHLAKLDTNI SDKNIVIATK GIIPDENQLV TDYLEERYNI
DPSRMIVVSG PCHAEEVALG RLSYLTVGSE SKDAAEAFAR CLNGPAMRTL ISGDVRGIEY
GGVLKNVYAI ASGIVHGMKA GDNFQAILVA NAAKEMERFI DKAVGGERCI CHSVYLGDLL
VTAYSKFSRN HNFGSMIGRG CAVRRAMMEM EMVTEGYYAA KCMHEINLVI GADMPILEGV
YDILYRSLPA AKIMERISHH LT
//
