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Database: UniProt
Entry: F5TDW6_9FIRM
LinkDB: F5TDW6_9FIRM
Original site: F5TDW6_9FIRM 
ID   F5TDW6_9FIRM            Unreviewed;       319 AA.
AC   F5TDW6;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   24-JAN-2024, entry version 62.
DE   SubName: Full=Putative glycerol-3-phosphate dehydrogenase [NAD(P)+] {ECO:0000313|EMBL:EGL35774.1};
DE            EC=1.1.1.- {ECO:0000313|EMBL:EGL35774.1};
GN   ORFNames=HMPREF9126_1534 {ECO:0000313|EMBL:EGL35774.1};
OS   Parvimonas sp. oral taxon 110 str. F0139.
OC   Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC   Parvimonas.
OX   NCBI_TaxID=767100 {ECO:0000313|EMBL:EGL35774.1, ECO:0000313|Proteomes:UP000003475};
RN   [1] {ECO:0000313|EMBL:EGL35774.1, ECO:0000313|Proteomes:UP000003475}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0139 {ECO:0000313|EMBL:EGL35774.1,
RC   ECO:0000313|Proteomes:UP000003475};
RA   Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Nelson K.E.;
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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:EGL35774.1}.
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DR   EMBL; AFII01000002; EGL35774.1; -; Genomic_DNA.
DR   AlphaFoldDB; F5TDW6; -.
DR   STRING; 767100.HMPREF9126_1534; -.
DR   OrthoDB; 9812273at2; -.
DR   UniPathway; UPA00940; -.
DR   Proteomes; UP000003475; 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:0006650; P:glycerophospholipid metabolic process; IEA:UniProtKB-UniPathway.
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   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   ECO:0000313|EMBL:EGL35774.1};
KW   Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW   Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264}.
FT   DOMAIN          2..154
FT                   /note="Glycerol-3-phosphate dehydrogenase NAD-dependent N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01210"
FT   DOMAIN          176..307
FT                   /note="Glycerol-3-phosphate dehydrogenase NAD-dependent C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07479"
FT   ACT_SITE        186
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000114-1"
FT   BINDING         7..12
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
FT   BINDING         265
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
SQ   SEQUENCE   319 AA;  35818 MW;  FBAFF5D39B1B9DC5 CRC64;
     MKIAVIGCGR WGSFIAWYLD KIGNEVTLYG RETSEKMKNF LENRKNNFLE LPKSISLTTN
     INDVFDKDLI IISVGTQGLR DLLNENKSLF KEKNIPIILC MKGIEIKTGF TPTKIVKDIL
     GENYSCGAWI GPGHVQDFTN GIPNCMVIDS DDRELVKKLV DSFSSNLIRF YYGTNLLGNE
     IGAASKNVIG IAAGMLDGFN LSSLKGALMS RGTREIARLI EKMGGDKSCA YGLCHLGDYE
     ATVFSEFSNN RKFGEKFVKG ESFEKLAEGY YTTKALMDLS EKYDVELPIT NAVYEIIYNK
     KDPKEILDNL FKRSIKMEF
//
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