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   03-AUG-2022, entry version 79.
DE   RecName: Full=Glycerol dehydrogenase;
DE            Short=GDH;
DE            Short=GLDH;
DE            EC=1.1.1.6;
GN   Name=dhaD;
OS   Citrobacter freundii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter; Citrobacter freundii complex.
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; DOI=10.1128/jb.177.15.4392-4401.1995;
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 glycerol
CC       as a source of carbon under anaerobic conditions. Exhibits a rather
CC       broad substrate specificity since it can also oxidize 1,2-propanediol
CC       and 2,3-butanediol and reduce dihydroxyacetone. Cannot use NADP(+) as
CC       an electron acceptor for the oxidation of glycerol.
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=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC   -!- ACTIVITY 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 phosphate
CC       from glycerol (oxidative route): step 1/2.
CC   -!- SUBUNIT: Homohexamer.
CC   -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase
CC       family. {ECO:0000305}.
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DR   EMBL; U09771; AAB48844.1; -; Genomic_DNA.
DR   AlphaFoldDB; P45511; -.
DR   SMR; P45511; -.
DR   STRING; 1333848.CFNIH1_02640; -.
DR   BioCyc; MetaCyc:MON-4503; -.
DR   SABIO-RK; P45511; -.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Glycerol metabolism; Manganese; Metal-binding;
KW   NAD; Oxidoreductase.
FT   CHAIN           1..365
FT                   /note="Glycerol dehydrogenase"
FT                   /id="PRO_0000087827"
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="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         171
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         254
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         254
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         271
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         271
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
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