ID   GLDA_ECOL6              Reviewed;         367 AA.
AC   P0A9S6; P32665; P78132;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   16-JUN-2009, entry version 30.
DE   RecName: Full=Glycerol dehydrogenase;
DE            Short=GLDH;
DE            Short=GDH;
DE            EC=1.1.1.6;
GN   Name=gldA; OrderedLocusNames=c4904;
OS   Escherichia coli O6.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=217992;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O6:H1 / CFT073 / ATCC 700928 / UPEC;
RX   MEDLINE=22388234; PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P.,
RA   Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D.,
RA   Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T.,
RA   Mobley H.L.T., Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence
RT   of uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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; AE014075; AAN83332.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_756758.2; -.
DR   HSSP; Q9WYQ4; 1KQ3.
DR   GeneID; 1040105; -.
DR   GenomeReviews; AE014075_GR; c4904.
DR   KEGG; ecc:c4904; -.
DR   HOGENOM; P0A9S6; -.
DR   OMA; P0A9S6; KYIRFYQ.
DR   BRENDA; 1.1.1.6; 292881.
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; ADH_Fe.
DR   InterPro; IPR018211; ADH_Fe_CS.
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   Complete proteome; Glycerol metabolism; Metal-binding; NAD;
KW   Oxidoreductase; Zinc.
FT   CHAIN         1    367       Glycerol dehydrogenase.
FT                                /FTId=PRO_0000087829.
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   367 AA;  38712 MW;  F6F3F275B4091F28 CRC64;
     MDRIIQSPGK YIQGADVINR LGEYLKPLAE RWLVVGDKFV LGFAQSTVEK SFKDAGLVVE
     IAPFGGECSQ NEIDRLRGIA ETAQCGAILG IGGGKTLDTA KALAHFMGVP VAIAPTIAST
     DAPCSALSVI YTDEGEFDRY LLLPNNPNMV IVDTKIVAGA PARLLAAGIG DALATWFEAR
     ACSRSGATTM AGGKCTQAAL ALAELCYNTL LEEGEKAMLA AEQHVVTPAL ERVIEANTYL
     SGVGFESGGL AAAHAVHNGL TAIPDAHHYY HGEKVAFGTL TQLVLENAPV EEIETVAALS
     HAVGLPITLA QLDIKEDVPA KMRIVAEAAC AEGETIHNMP GGATPDQVYA ALLVADQYGQ
     RFLQEWE
//