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Entry: A0A1H5LPW7_9MICO
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Original site: A0A1H5LPW7_9MICO 
ID   A0A1H5LPW7_9MICO        Unreviewed;       340 AA.
AC   A0A1H5LPW7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU000439};
DE            EC=1.1.1.94 {ECO:0000256|RuleBase:RU000439};
GN   ORFNames=SAMN04488554_2920 {ECO:0000313|EMBL:SEE79113.1};
OS   Ruania alba.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Ruaniaceae; Ruania.
OX   NCBI_TaxID=648782 {ECO:0000313|EMBL:SEE79113.1, ECO:0000313|Proteomes:UP000199220};
RN   [1] {ECO:0000313|Proteomes:UP000199220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21368 {ECO:0000313|Proteomes:UP000199220};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-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; FNTX01000002; SEE79113.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H5LPW7; -.
DR   STRING; 648782.SAMN04488554_2920; -.
DR   OrthoDB; 9812273at2; -.
DR   Proteomes; UP000199220; 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: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:SF33; GLYCEROL-3-PHOSPHATE DEHYDROGENASE [NAD(+)] 3, CYTOSOLIC-RELATED; 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.
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:UP000199220}.
FT   DOMAIN          4..162
FT                   /note="Glycerol-3-phosphate dehydrogenase NAD-dependent N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01210"
FT   DOMAIN          186..336
FT                   /note="Glycerol-3-phosphate dehydrogenase NAD-dependent C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07479"
FT   ACT_SITE        197
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000114-1"
FT   BINDING         8..13
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
FT   BINDING         34
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
FT   BINDING         108
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000114-2"
FT   BINDING         145
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
FT   BINDING         264..265
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000114-2"
FT   BINDING         264
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
SQ   SEQUENCE   340 AA;  34663 MW;  4A0EEF0FF988063B CRC64;
     MARVTILGAG AMGSALATPL RANGHQVALW GTWFDDHFLA ELADGGPHPG TKVALAEGTE
     VFTSDRIADA LAGSDAVIVA VASGGVLEVS RLAAAHLAHR PTLGLVSKGF HQRADGSIAL
     MPEAVREAIE DSGAVVVAIG GPCKANEVAA GRFTATAFAS TDGGQAAGRL ADVMRTPDYR
     PNVSDDEAGL EVCAPLKNVY AIALGFADGL EQSTGEPWHN LKSAIFAKAS QEMGLVAEAL
     GGRVETAFGL PGVGDLEVTG LSGRNKVYGA RIGAGESAPE ALERMREAGQ TVEGVAASGL
     AETLVTTQLQ SIADRLTLLA AIRAVLDGAA DPLTVIRQAL
//
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