GLDA_ECOL6
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 03-AUG-2022, entry version 88.
DE RecName: Full=Glycerol dehydrogenase;
DE Short=GDH;
DE Short=GLDH;
DE EC=1.1.1.6;
GN Name=gldA; OrderedLocusNames=c4904;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT 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 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN83332.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE014075; AAN83332.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000374004.1; NC_004431.1.
DR AlphaFoldDB; P0A9S6; -.
DR SMR; P0A9S6; -.
DR STRING; 199310.c4904; -.
DR EnsemblBacteria; AAN83332; AAN83332; c4904.
DR GeneID; 66672144; -.
DR KEGG; ecc:c4904; -.
DR eggNOG; COG0371; Bacteria.
DR HOGENOM; CLU_044754_1_0_6; -.
DR OMA; ALHGEQC; -.
DR UniPathway; UPA00617; UER00668.
DR Proteomes; UP000001410; Chromosome.
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; Zinc.
FT CHAIN 1..367
FT /note="Glycerol dehydrogenase"
FT /id="PRO_0000087829"
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 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
