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   04-NOV-2008, entry version 41.
DE   RecName: Full=Glycerol dehydrogenase;
DE            Short=GLDH;
DE            Short=GDH;
DE            EC=1.1.1.6;
GN   Name=gldA; Synonyms=bedD;
OS   Pseudomonas putida.
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   MEDLINE=96421985; PubMed=8824602;
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
CC       glycerol as a source of carbon under anaerobic conditions (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Glycerol + NAD(+) = glycerone + NADH.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- PATHWAY: Polyol metabolism; glycerol fermentation; glycerone
CC       phosphate from glycerol (oxidative route): step 1/2.
CC   -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase
CC       family.
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DR   EMBL; AF148496; AAC44426.1; -; Genomic_DNA.
DR   HSSP; Q9WYQ4; 1KQ3.
DR   GO; GO:0008888; F:glycerol dehydrogenase activity; IEA:EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR001670; Fe_AlcDHase.
DR   InterPro; IPR016205; Glycerol_DH.
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;
KW   Zinc.
FT   CHAIN         1    365       Glycerol dehydrogenase.
FT                                /FTId=PRO_0000087830.
FT   NP_BIND      94     98       NAD (By similarity).
FT   NP_BIND     116    119       NAD (By similarity).
FT   METAL       171    171       Zinc; catalytic (By similarity).
FT   METAL       254    254       Zinc; catalytic (By similarity).
FT   METAL       271    271       Zinc; catalytic (By similarity).
FT   BINDING      37     37       NAD (By similarity).
FT   BINDING     121    121       Substrate (By similarity).
FT   BINDING     125    125       NAD (By similarity).
FT   BINDING     127    127       NAD; via carbonyl oxygen (By similarity).
FT   BINDING     131    131       NAD (By similarity).
FT   BINDING     171    171       Substrate (By similarity).
FT   BINDING     254    254       Substrate (By similarity).
FT   BINDING     271    271       Substrate (By similarity).
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
//