ID C5CEI1_KOSOT Unreviewed; 364 AA.
AC C5CEI1;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Glycerol dehydrogenase {ECO:0000256|ARBA:ARBA00040132};
DE EC=1.1.1.6 {ECO:0000256|ARBA:ARBA00039147};
GN OrderedLocusNames=Kole_0505 {ECO:0000313|EMBL:ACR79227.1};
OS Kosmotoga olearia (strain ATCC BAA-1733 / DSM 21960 / TBF 19.5.1).
OC Bacteria; Thermotogota; Thermotogae; Kosmotogales; Kosmotogaceae;
OC Kosmotoga.
OX NCBI_TaxID=521045 {ECO:0000313|EMBL:ACR79227.1, ECO:0000313|Proteomes:UP000002382};
RN [1] {ECO:0000313|EMBL:ACR79227.1, ECO:0000313|Proteomes:UP000002382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1733 / DSM 21960 / TBF 19.5.1
RC {ECO:0000313|Proteomes:UP000002382};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA Noll K.;
RT "Complete sequence of Thermotogales bacterium TBF 19.5.1.";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACR79227.1, ECO:0000313|Proteomes:UP000002382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1733 / DSM 21960 / TBF 19.5.1
RC {ECO:0000313|Proteomes:UP000002382};
RX PubMed=21914881; DOI=10.1128/JB.05828-11;
RA Swithers K.S., Dipippo J.L., Bruce D.C., Detter C., Tapia R., Han S.,
RA Goodwin L.A., Han J., Woyke T., Pitluck S., Pennacchio L., Nolan M.,
RA Mikhailova N., Land M.L., Nesbo C.L., Gogarten J.P., Noll K.M.;
RT "Genome Sequence of Kosmotoga olearia Strain TBF 19.5.1, a Thermophilic
RT Bacterium with a Wide Growth Temperature Range, Isolated from the Troll B
RT Oil Platform in the North Sea.";
RL J. Bacteriol. 193:5566-5567(2011).
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 Evidence={ECO:0000256|ARBA:ARBA00036918};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR000112-1};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000112-1};
CC -!- PATHWAY: Polyol metabolism; glycerol fermentation; glycerone phosphate
CC from glycerol (oxidative route): step 1/2.
CC {ECO:0000256|ARBA:ARBA00037918}.
CC -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00007358}.
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DR EMBL; CP001634; ACR79227.1; -; Genomic_DNA.
DR RefSeq; WP_012745012.1; NC_012785.1.
DR AlphaFoldDB; C5CEI1; -.
DR STRING; 521045.Kole_0505; -.
DR KEGG; kol:Kole_0505; -.
DR eggNOG; COG0371; Bacteria.
DR HOGENOM; CLU_044754_1_0_0; -.
DR OrthoDB; 5198708at2; -.
DR Proteomes; UP000002382; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR CDD; cd08170; GlyDH; 1.
DR Gene3D; 3.40.50.1970; -; 1.
DR Gene3D; 1.20.1090.10; Dehydroquinate synthase-like - alpha domain; 1.
DR InterPro; IPR001670; ADH_Fe/GldA.
DR InterPro; IPR018211; ADH_Fe_CS.
DR InterPro; IPR016205; Glycerol_DH.
DR PANTHER; PTHR43616; GLYCEROL DEHYDROGENASE; 1.
DR PANTHER; PTHR43616:SF5; GLYCEROL DEHYDROGENASE 1; 1.
DR Pfam; PF00465; Fe-ADH; 1.
DR PIRSF; PIRSF000112; Glycerol_dehydrogenase; 1.
DR SUPFAM; SSF56796; Dehydroquinate synthase-like; 1.
DR PROSITE; PS00913; ADH_IRON_1; 1.
DR PROSITE; PS00060; ADH_IRON_2; 1.
PE 3: Inferred from homology;
KW Glycerol metabolism {ECO:0000256|ARBA:ARBA00022798};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000112-1};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000112-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000002382};
KW Zinc {ECO:0000256|PIRSR:PIRSR000112-1}.
FT DOMAIN 8..347
FT /note="Alcohol dehydrogenase iron-type/glycerol
FT dehydrogenase GldA"
FT /evidence="ECO:0000259|Pfam:PF00465"
FT BINDING 37
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT BINDING 93..97
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT BINDING 115..118
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT BINDING 120
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-2"
FT BINDING 124
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT BINDING 126
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT BINDING 130
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT BINDING 170
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
FT BINDING 253
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
FT BINDING 270
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
SQ SEQUENCE 364 AA; 38864 MW; A3EAF7277980B335 CRC64;
MISTTIFPGR YVQGSGALER LGSEMVRFGK KGFVICDSFV LENLLPDFRQ SMEQSLEVVV
EKFGGECSDE EISRLADLAK GAGCELIVGI GGGKTLDTAK AVAYELKLPV VIVPTLASTD
APCSALSVIY TPNGEFKRYL ILPKNPDLVL VDTKIIAQAP ARFLVSGMGD ALATWFEAES
CMKKYAKNMT GNVGSMTAYA LAKLCYETLL EYGVAAKSSC EANAVTPALE HIVEANTLLS
GLGFESGGLA AAHAIHNGLT VLEQTHKYYH GEKVAFGTLT SLFLTDKPRE IIDEVYSFCE
SVGLPTTLAD IGLDGVSDEE LMKVAEAACA EGETIHNEPI PVTPEAVYSA IKTADAEGKR
RKAV
//
