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Database: UniProt
Entry: A0A377KNP2_9ENTE
LinkDB: A0A377KNP2_9ENTE
Original site: A0A377KNP2_9ENTE 
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
//
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