ID A0A1L4BWY0_9LACT Unreviewed; 379 AA.
AC A0A1L4BWY0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Glycerol dehydrogenase {ECO:0000256|ARBA:ARBA00040132};
DE EC=1.1.1.6 {ECO:0000256|ARBA:ARBA00039147};
GN Name=gldA {ECO:0000313|EMBL:API88361.1};
GN ORFNames=BKP56_03170 {ECO:0000313|EMBL:API88361.1};
OS Marinilactibacillus sp. 15R.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Marinilactibacillus.
OX NCBI_TaxID=1911586 {ECO:0000313|EMBL:API88361.1, ECO:0000313|Proteomes:UP000184433};
RN [1] {ECO:0000313|EMBL:API88361.1, ECO:0000313|Proteomes:UP000184433}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=15R {ECO:0000313|EMBL:API88361.1,
RC ECO:0000313|Proteomes:UP000184433};
RA Wei Y., Cao J., Fang J.;
RT "Genome sequence of Marinilactibacillus sp. 15R.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycerol + NAD(+) = dihydroxyacetone + H(+) + NADH;
CC Xref=Rhea:RHEA:13769, ChEBI:CHEBI:15378, ChEBI:CHEBI:16016,
CC ChEBI:CHEBI:17754, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.6;
CC Evidence={ECO:0000256|ARBA:ARBA00036918};
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 -!- PATHWAY: Polyol metabolism; glycerol fermentation; glycerone phosphate
CC from glycerol (oxidative route): step 1/2.
CC {ECO:0000256|ARBA:ARBA00037918}.
CC -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00007358}.
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DR EMBL; CP017761; API88361.1; -; Genomic_DNA.
DR RefSeq; WP_072693680.1; NZ_CP017761.1.
DR AlphaFoldDB; A0A1L4BWY0; -.
DR STRING; 1911586.BKP56_03170; -.
DR KEGG; marr:BKP56_03170; -.
DR Proteomes; UP000184433; Chromosome.
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:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR CDD; cd08170; GlyDH; 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:SF5; GLYCEROL DEHYDROGENASE 1; 1.
DR Pfam; PF00465; Fe-ADH; 1.
DR PIRSF; PIRSF000112; Glycerol_dehydrogenase; 1.
DR SUPFAM; SSF56796; Dehydroquinate synthase-like; 1.
DR PROSITE; PS00060; ADH_IRON_2; 1.
PE 3: Inferred from homology;
KW Glycerol metabolism {ECO:0000256|ARBA:ARBA00022798};
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000184433};
KW Zinc {ECO:0000256|PIRSR:PIRSR000112-1}.
FT DOMAIN 8..358
FT /note="Alcohol dehydrogenase iron-type/glycerol
FT dehydrogenase GldA"
FT /evidence="ECO:0000259|Pfam:PF00465"
FT BINDING 94..98
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT BINDING 119
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-2"
FT BINDING 123
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT BINDING 129
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT BINDING 169
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
FT BINDING 264
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
FT BINDING 281
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
SQ SEQUENCE 379 AA; 40709 MW; CC97834950EAED57 CRC64;
MRKAFISPTK YVQGENELLN LGFYVKSFGE SALVIGNPGD IERVQDKLDK TAEHFGITLH
LADFGGEATR EEVNRLKKLA KEKGTDIIVG LGGGKAIDTS KTVANGHNLI VCPTIAATDA
PTSHSAVLYT KDHHFDEYAY FIQSPSVVLM DTTVIAQAPA RFLISGMGDS LATYYEARAT
RRSNSNVNAG LPNGYHTGDT APAKGTIASI TLARACYETV MENGYNAKIA CDNNVVTPAL
ENIIEANTLL SGLGFESGGL AAAHAIYNGL TVLDGPHNYF HGEQVAFTTF VQLILEDAPN
DEVEALLDFS LSVGLPVSLA DLDVAEVKYE EILKVAEKAC IPEESIHAMP FEVTPESVAQ
AIIAADVIGR DYKKRKSVK
//
