ID A0A377KNP2_9ENTE Unreviewed; 324 AA.
AC A0A377KNP2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Putative glycerol dehydrogenase {ECO:0000313|EMBL:STP30820.1};
DE EC=1.1.1.6 {ECO:0000313|EMBL:STP30820.1};
GN Name=gldA {ECO:0000313|EMBL:STP30820.1};
GN ORFNames=NCTC8129_03075 {ECO:0000313|EMBL:STP30820.1};
OS Enterococcus durans.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=53345 {ECO:0000313|EMBL:STP30820.1, ECO:0000313|Proteomes:UP000254070};
RN [1] {ECO:0000313|EMBL:STP30820.1, ECO:0000313|Proteomes:UP000254070}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC8129 {ECO:0000313|EMBL:STP30820.1,
RC ECO:0000313|Proteomes:UP000254070};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-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 -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00007358}.
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DR EMBL; UGIF01000002; STP30820.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A377KNP2; -.
DR Proteomes; UP000254070; Unassembled WGS sequence.
DR GO; GO:0008888; F:glycerol dehydrogenase [NAD+] activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd08172; GlyDH-like; 1.
DR Gene3D; 3.40.50.1970; -; 1.
DR Gene3D; 1.20.1090.10; Dehydroquinate synthase-like - alpha domain; 1.
DR InterPro; IPR001670; ADH_Fe/GldA.
DR InterPro; IPR018211; ADH_Fe_CS.
DR InterPro; IPR016205; Glycerol_DH.
DR PANTHER; PTHR43616; GLYCEROL DEHYDROGENASE; 1.
DR PANTHER; PTHR43616:SF3; HYDROXYCARBOXYLATE DEHYDROGENASE A; 1.
DR Pfam; PF00465; Fe-ADH; 1.
DR PIRSF; PIRSF000112; Glycerol_dehydrogenase; 1.
DR SUPFAM; SSF56796; Dehydroquinate synthase-like; 1.
DR PROSITE; PS00913; ADH_IRON_1; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000112-1}; NAD {ECO:0000256|PIRSR:PIRSR000112-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:STP30820.1}; Zinc {ECO:0000256|PIRSR:PIRSR000112-1}.
FT DOMAIN 19..308
FT /note="Alcohol dehydrogenase iron-type/glycerol
FT dehydrogenase GldA"
FT /evidence="ECO:0000259|Pfam:PF00465"
FT BINDING 58..62
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT BINDING 89
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT BINDING 91
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT BINDING 95
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT BINDING 135
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
FT BINDING 219
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
FT BINDING 236
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
SQ SEQUENCE 324 AA; 35825 MW; DEB0C7E9A9E2B8D2 CRC64;
MILHGKTSWK AVKDDFPELS ITKIFEYYGG ECTDPLADSF VSLCKKKKVN GIIAVGGGKV
ADLGKLIAYK TNLPIIILPT LAATCAAYTP LSVVYNEEGV MLRYDMFTKA NDLVLIDPKI
ILHSPREMMI AGIGDTLAKW YESHAIISQL TIKPIEVQVA EFAALRCREI LLEKSAEAME
AMDQQKINQA FIDVVETNIL LAGMVGGFGD DYGRTAGAHS IHDAMTLLPD SHQQLHGNKV
AYGILVQLMI ENKLAEIEHL LPFYHHLNLP TSLADMGLHL TESDYQAVAE RACLPDEMIH
FMKETITPAL VVQKMKELEQ VTQG
//