ID   GLDA_CITFR              Reviewed;         365 AA.
AC   P45511;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   04-NOV-2008, entry version 44.
DE   RecName: Full=Glycerol dehydrogenase;
DE            Short=GLDH;
DE            Short=GDH;
DE            EC=1.1.1.6;
GN   Name=dhaD;
OS   Citrobacter freundii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=546;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-30, AND
RP   CHARACTERIZATION.
RC   STRAIN=ATCC 6750 / DSM 30040 / NCIB 8173 / M8BK;
RX   PubMed=7635824;
RA   Daniel R., Stuertz K., Gottschalk G.;
RT   "Biochemical and molecular characterization of the oxidative branch of
RT   glycerol utilization by Citrobacter freundii.";
RL   J. Bacteriol. 177:4392-4401(1995).
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.
CC       Exhibits a rather broad substrate specificity since it can also
CC       oxidize 1,2-propanediol and 2,3-butanediol and reduce
CC       dihydroxyacetone. Can not use NADP(+) as an electron acceptor for
CC       the oxidation of glycerol.
CC   -!- CATALYTIC ACTIVITY: Glycerol + NAD(+) = glycerone + NADH.
CC   -!- COFACTOR: Manganese.
CC   -!- ENZYME REGULATION: Inhibited by zinc.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.27 mM for glycerol;
CC         KM=57 uM for NAD(+);
CC   -!- PATHWAY: Polyol metabolism; glycerol fermentation; glycerone
CC       phosphate from glycerol (oxidative route): step 1/2.
CC   -!- SUBUNIT: Homohexamer.
CC   -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase
CC       family.
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DR   EMBL; U09771; AAB48844.1; -; Genomic_DNA.
DR   HSSP; P32816; 1JPU.
DR   BioCyc; MetaCyc:MON-4503; -.
DR   GO; GO:0008888; F:glycerol dehydrogenase activity; IEA:EC.
DR   GO; GO:0030145; F:manganese 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   1: Evidence at protein level;
KW   Direct protein sequencing; Glycerol metabolism; Manganese;
KW   Metal-binding; NAD; Oxidoreductase.
FT   CHAIN         1    365       Glycerol dehydrogenase.
FT                                /FTId=PRO_0000087827.
FT   NP_BIND      94     98       NAD (By similarity).
FT   NP_BIND     116    119       NAD (By similarity).
FT   METAL       171    171       Manganese; catalytic (By similarity).
FT   METAL       254    254       Manganese; catalytic (By similarity).
FT   METAL       271    271       Manganese; 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;  39019 MW;  CB20076C0EE9DD8B CRC64;
     MLKVIQSPAK YLQGPDASTL FGQYAKNLAD SFFVIADDFV MKLAGEKVLN GLHSHDISCH
     AERFNGECSH IEINRLIAIL KQHGCRGVVG IGGGKTLDTA KAIGYYQKLP VVVIPTIAST
     DAPTSALSVI YTEAGEFEEY LIYPKNPDMV VMDTAIIAKA PVRLLVAGMG DALSTWFEAK
     ACYDARATSM AGGQSTVAAL SLARLCYDTL LAEGEKARFA AQAGVVTDAL ERIVEANTYL
     SGIGFESSGL AGAHAIHNGF TILEECHHLY HGEKVAFGTL AQLVLQNSPM EEIETVLNFC
     QKVGLPVTLA EMGVKDDIDG KIMAVAKATC AEGETIHNMP FSVTPESVHA AILTADLLGQ
     QWLAR
//