ID   GLDA_PSEPU              Reviewed;         365 AA.
AC   P50173;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Glycerol dehydrogenase;
DE            Short=GDH;
DE            Short=GLDH;
DE            EC=1.1.1.6;
GN   Name=gldA; Synonyms=bedD;
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OG   Plasmid pHMT112.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ML2;
RX   PubMed=8824602; DOI=10.1128/jb.178.19.5592-5601.1996;
RA   Fong K.P.Y., Goh C.B.H., Tan H.M.;
RT   "Characterization and expression of the plasmid-borne bedD gene from
RT   Pseudomonas putida ML2, which codes for a NAD+-dependent cis-benzene
RT   dihydrodiol dehydrogenase.";
RL   J. Bacteriol. 178:5592-5601(1996).
CC   -!- FUNCTION: Catalyzes the NAD-dependent oxidation of glycerol to
CC       dihydroxyacetone (glycerone). Allows microorganisms to utilize glycerol
CC       as a source of carbon under anaerobic conditions (By similarity).
CC       {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- PATHWAY: Polyol metabolism; glycerol fermentation; glycerone phosphate
CC       from glycerol (oxidative route): step 1/2.
CC   -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase
CC       family. {ECO:0000305}.
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DR   EMBL; AF148496; AAC44426.1; -; Genomic_DNA.
DR   AlphaFoldDB; P50173; -.
DR   SMR; P50173; -.
DR   UniPathway; UPA00617; UER00668.
DR   GO; GO:0008888; F:glycerol dehydrogenase [NAD+] activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019588; P:anaerobic glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR001670; ADH_Fe/GldA.
DR   InterPro; IPR018211; ADH_Fe_CS.
DR   InterPro; IPR016205; Glycerol_DH.
DR   PANTHER; PTHR43616; PTHR43616; 1.
DR   Pfam; PF00465; Fe-ADH; 1.
DR   PIRSF; PIRSF000112; Glycerol_dehydrogenase; 1.
DR   PROSITE; PS00913; ADH_IRON_1; 1.
DR   PROSITE; PS00060; ADH_IRON_2; 1.
PE   3: Inferred from homology;
KW   Glycerol metabolism; Metal-binding; NAD; Oxidoreductase; Plasmid; Zinc.
FT   CHAIN           1..365
FT                   /note="Glycerol dehydrogenase"
FT                   /id="PRO_0000087830"
FT   BINDING         37
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         94..98
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         116..119
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         121
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         125
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         127
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         131
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         171
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         171
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         254
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         254
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         271
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         271
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   365 AA;  38316 MW;  D6AEAA16D52A8D47 CRC64;
     MDRAIQSPGK YVQGADALQR LGDYLKPLAD SWLVIADKFV LGFAEDTIRQ SLSKAGLAMD
     IVAFNGECSQ GEVDRLCQLA TQNGRSAIVG IGGGKTLDTA KAVAFFQKVP VAVAPTIAST
     DAPCSALSVL YTDEGEFDRY LMLPTNPALV VVDTAIVARA PARLLAAGIG DALATWFEAR
     AASRSSAATM AGGPATQTAL NLARFCYDTL LEEGEKAMLA VQAQVVTPAL ERIVEANTYL
     SGVGFESGGV AAAHAVHNGL TAVAETHHFY HGEKVAFGVL VQLALENASN AEMQEVMSLC
     HAVGLPITLA QLDITEDIPT KMRAVAELAC APGETIHNMP GGVTVEQVYG ALLVADQLGQ
     HFLEF