ID A0A3N6ITG8_9ACTN Unreviewed; 353 AA.
AC A0A3N6ITG8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Glycerol-1-phosphate dehydrogenase [NAD(P)+] {ECO:0000313|EMBL:RPK84389.1};
DE EC=1.1.1.261 {ECO:0000313|EMBL:RPK84389.1};
GN Name=egsA {ECO:0000313|EMBL:RPK84389.1};
GN ORFNames=EES45_03855 {ECO:0000313|EMBL:RPK84389.1};
OS Streptomyces sp. ADI97-07.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1522762 {ECO:0000313|EMBL:RPK84389.1, ECO:0000313|Proteomes:UP000281409};
RN [1] {ECO:0000313|EMBL:RPK84389.1, ECO:0000313|Proteomes:UP000281409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ADI97-07 {ECO:0000313|EMBL:RPK84389.1,
RC ECO:0000313|Proteomes:UP000281409};
RA Guerrero-Garzon J.F., Zehl M., Urban E., Schneider O., Ruckert C.,
RA Busche T., Kalinowski J., Zotchev S.B.;
RT "Streptomyces spp. from the marine sponge Antho dichothoma: analyses of
RT secondary metabolite biosynthesis gene clusters and some of their
RT products.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR000112-1};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000112-1};
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:RPK84389.1}.
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DR EMBL; RPGY01000021; RPK84389.1; -; Genomic_DNA.
DR RefSeq; WP_056792466.1; NZ_ML123098.1.
DR AlphaFoldDB; A0A3N6ITG8; -.
DR Proteomes; UP000281409; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0050492; F:glycerol-1-phosphate dehydrogenase [NAD(P)+] activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd08174; G1PDH-like; 1.
DR Gene3D; 3.40.50.1970; -; 1.
DR Gene3D; 1.20.1090.10; Dehydroquinate synthase-like - alpha domain; 1.
DR InterPro; IPR032837; G1PDH.
DR InterPro; IPR016205; Glycerol_DH.
DR PANTHER; PTHR43616; GLYCEROL DEHYDROGENASE; 1.
DR PANTHER; PTHR43616:SF5; GLYCEROL DEHYDROGENASE 1; 1.
DR Pfam; PF13685; Fe-ADH_2; 1.
DR PIRSF; PIRSF000112; Glycerol_dehydrogenase; 1.
DR SUPFAM; SSF56796; Dehydroquinate synthase-like; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000112-1};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000112-3};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:RPK84389.1};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW Reference proteome {ECO:0000313|Proteomes:UP000281409};
KW Zinc {ECO:0000256|PIRSR:PIRSR000112-1}.
FT BINDING 96..100
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT BINDING 118..121
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT BINDING 123
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-2"
FT BINDING 127
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT BINDING 170
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
FT BINDING 248
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
FT BINDING 265
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
SQ SEQUENCE 353 AA; 37000 MW; F8DBD76A12465334 CRC64;
MPVLTRLIPS PVVVDIRRGA MDDLAGLLAD QRISASGKLA IAISGGSGLA LRERLAPVLP
GADWYPVGDG TIDSAVRLAD GIKGNRYDAL VGLGGGKIID VAKYAAARVG MPMVAVATNL
SHDGLCSPVA TLDNDNGRGS YGVPTPIAVV IDLDVIREAP ARYVRSGIGD AVSNISCVAD
WELAHEIQGE EIDGLAAAMA RQAGEAVLRH PGGVGDDAFL KVLAEGLVLT GISMSVAGDS
RPASGGCHEI NHAFDLLYPK RAASHGEQVG LGACFAMHLR GAREESLHMA SVLRRHGLPV
LPGEIGFTPD EFVRAVEYAP QTRPGRFTIL EHLNLSTDQI RDAYADYAKA IHS
//