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Database: UniProt
Entry: A0A3N6ITG8_9ACTN
LinkDB: A0A3N6ITG8_9ACTN
Original site: A0A3N6ITG8_9ACTN 
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
//
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