ID A0A372LWW0_9ACTN Unreviewed; 355 AA.
AC A0A372LWW0;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Iron-containing alcohol dehydrogenase {ECO:0000313|EMBL:RFU83162.1};
GN ORFNames=DY218_29215 {ECO:0000313|EMBL:RFU83162.1};
OS Streptomyces triticagri.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2293568 {ECO:0000313|EMBL:RFU83162.1, ECO:0000313|Proteomes:UP000263094};
RN [1] {ECO:0000313|EMBL:RFU83162.1, ECO:0000313|Proteomes:UP000263094}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEAU-YY421 {ECO:0000313|EMBL:RFU83162.1,
RC ECO:0000313|Proteomes:UP000263094};
RA Han C.;
RT "Isolation, diversity and antifungal activity of Actinobacteria from
RT wheat.";
RL Submitted (AUG-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:RFU83162.1}.
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DR EMBL; QUAK01000218; RFU83162.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A372LWW0; -.
DR OrthoDB; 5198708at2; -.
DR Proteomes; UP000263094; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
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 Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW Zinc {ECO:0000256|PIRSR:PIRSR000112-1}.
FT BINDING 98..102
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT BINDING 125
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-2"
FT BINDING 129
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT BINDING 172
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
FT BINDING 250
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
FT BINDING 267
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
SQ SEQUENCE 355 AA; 37387 MW; AFE1E526D9060ADC CRC64;
MPVLTRLMPS PVVVDIRAGA LDDLATILTD QRIAPTGKLA FAISNGGSGK MLQERFAPAF
PGADWFDDAD GTIDGAVKLA DSIKKSGRYD AVVSLGGGKV VDCAKYAAAR VGLPLVAVAT
NLAHDGLCSP VATLDNDAGR GSYGVPNPIG VVIDLDVIRD APSRFVRAGI GDVICKISAV
ADWELSHRVN GEQVDGLAAA MARQAAHAVL RHPGGIGDDA FLSVLAESLV MCGLAMSVAG
DSRPASGACH EICHAFDLRF PKRNAQHGEQ CGFGGAFATF LRGDLDTAKE MVDTLRRHGL
PVLAEEMGYS DQDLVEAVLF APQTRPGRYT ILEHLDYNAD QIKDAYADYV KTIGS
//
