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Database: UniProt
Entry: A0A1H8F285_9MICO
LinkDB: A0A1H8F285_9MICO
Original site: A0A1H8F285_9MICO 
ID   A0A1H8F285_9MICO        Unreviewed;       367 AA.
AC   A0A1H8F285;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(P)+] {ECO:0000256|HAMAP-Rule:MF_00394};
DE            EC=1.1.1.94 {ECO:0000256|HAMAP-Rule:MF_00394};
DE   AltName: Full=NAD(P)H-dependent glycerol-3-phosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00394};
GN   Name=gpsA {ECO:0000256|HAMAP-Rule:MF_00394};
GN   ORFNames=E3O10_15150 {ECO:0000313|EMBL:TFB85470.1};
OS   Cryobacterium luteum.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Cryobacterium.
OX   NCBI_TaxID=1424661 {ECO:0000313|EMBL:TFB85470.1, ECO:0000313|Proteomes:UP000297654};
RN   [1] {ECO:0000313|EMBL:TFB85470.1, ECO:0000313|Proteomes:UP000297654}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hh15 {ECO:0000313|EMBL:TFB85470.1,
RC   ECO:0000313|Proteomes:UP000297654};
RA   Liu Q., Xin Y.-H.;
RT   "Genomics of glacier-inhabiting Cryobacterium strains.";
RL   Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate
CC         + H(+) + NADH; Xref=Rhea:RHEA:11092, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57597, ChEBI:CHEBI:57642,
CC         ChEBI:CHEBI:57945; EC=1.1.1.94; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00394};
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; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00394, ECO:0000256|RuleBase:RU000439};
CC   -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism.
CC       {ECO:0000256|HAMAP-Rule:MF_00394}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00394}.
CC   -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00011009,
CC       ECO:0000256|HAMAP-Rule:MF_00394, ECO:0000256|RuleBase:RU000437}.
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:TFB85470.1}.
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DR   EMBL; SOFF01000041; TFB85470.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H8F285; -.
DR   STRING; 1424661.SAMN05216281_105141; -.
DR   OrthoDB; 9812273at2; -.
DR   UniPathway; UPA00940; -.
DR   Proteomes; UP000297654; 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-UniRule.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0046167; P:glycerol-3-phosphate biosynthetic process; IEA:UniProtKB-UniRule.
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-UniRule.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   HAMAP; MF_00394; NAD_Glyc3P_dehydrog; 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   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00394};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW   Rule:MF_00394};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW   Rule:MF_00394};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_00394, ECO:0000256|RuleBase:RU000437};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_00394};
KW   Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209,
KW   ECO:0000256|HAMAP-Rule:MF_00394};
KW   Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264, ECO:0000256|HAMAP-
KW   Rule:MF_00394}.
FT   DOMAIN          1..156
FT                   /note="Glycerol-3-phosphate dehydrogenase NAD-dependent N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01210"
FT   DOMAIN          177..316
FT                   /note="Glycerol-3-phosphate dehydrogenase NAD-dependent C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07479"
FT   ACT_SITE        188
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00394"
FT   BINDING         5..10
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00394"
FT   BINDING         103
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00394"
FT   BINDING         103
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00394"
FT   BINDING         137
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00394"
FT   BINDING         252..253
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00394"
FT   BINDING         252
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00394"
FT   BINDING         278
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00394"
SQ   SEQUENCE   367 AA;  38851 MW;  DA6AA5BEF842D93D CRC64;
     MAVLGAGSWG TTFAKILTDG GADVVLWARR PELAREISEA RRNSDYLPGV NLPIGLRATS
     RLDLALAGAE MVFVSVPSQS LRENLKHVEP YLAENAILIS LMKGVERSTG MRMSSVIEEV
     LRIDPARIAA ISGPNLALEI AKEQPTGAVV SSSSLETAQA VAKLATNRYF RSYINTDVIG
     TEFGGVLKNL IAVAIGIVDG VGYGENTKAS IITRGLVEMT DFAVAYGAQA ETLAGLAGLG
     DLIATCQSPL SRNNTAGRLL GQGYSINDVV KQMQQTTEGL ASVKPVLELA RAKGVEMPIV
     EQVRQVLDGT LNPRDIAPHL TTDSGEPQGE RTLDDAQAHG GASLWGAFQR TLDQLRHGGR
     SAGSPRP
//
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