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Database: UniProt
Entry: B6GCK0_9ACTN
LinkDB: B6GCK0_9ACTN
Original site: B6GCK0_9ACTN 
ID   B6GCK0_9ACTN            Unreviewed;       362 AA.
AC   B6GCK0;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=Glycerol dehydrogenase {ECO:0000256|ARBA:ARBA00040132};
DE            EC=1.1.1.6 {ECO:0000256|ARBA:ARBA00039147};
GN   ORFNames=COLSTE_01823 {ECO:0000313|EMBL:EEA90031.1};
OS   Collinsella stercoris DSM 13279.
OC   Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales;
OC   Coriobacteriaceae; Collinsella.
OX   NCBI_TaxID=445975 {ECO:0000313|EMBL:EEA90031.1, ECO:0000313|Proteomes:UP000003560};
RN   [1] {ECO:0000313|EMBL:EEA90031.1, ECO:0000313|Proteomes:UP000003560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13279 {ECO:0000313|EMBL:EEA90031.1,
RC   ECO:0000313|Proteomes:UP000003560};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Collinsella stercoris (DSM 13279).";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EEA90031.1, ECO:0000313|Proteomes:UP000003560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13279 {ECO:0000313|EMBL:EEA90031.1,
RC   ECO:0000313|Proteomes:UP000003560};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EEA90031.1}.
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DR   EMBL; ABXJ01000105; EEA90031.1; -; Genomic_DNA.
DR   RefSeq; WP_006721457.1; NZ_DS995476.1.
DR   AlphaFoldDB; B6GCK0; -.
DR   STRING; 445975.COLSTE_01823; -.
DR   eggNOG; COG0371; Bacteria.
DR   HOGENOM; CLU_044754_3_1_11; -.
DR   OrthoDB; 323926at2; -.
DR   Proteomes; UP000003560; Unassembled WGS sequence.
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; cd08171; GlyDH-like; 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; 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.
PE   4: Predicted;
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:UP000003560};
KW   Zinc {ECO:0000256|PIRSR:PIRSR000112-1}.
FT   DOMAIN          9..345
FT                   /note="Alcohol dehydrogenase iron-type/glycerol
FT                   dehydrogenase GldA"
FT                   /evidence="ECO:0000259|Pfam:PF00465"
FT   BINDING         94..98
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT   BINDING         116..119
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT   BINDING         125
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT   BINDING         131
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         256
FT                   /ligand="glycerol"
FT                   /ligand_id="ChEBI:CHEBI:17754"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
FT   BINDING         274
FT                   /ligand="glycerol"
FT                   /ligand_id="ChEBI:CHEBI:17754"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
SQ   SEQUENCE   362 AA;  38677 MW;  247BAE8E5D5D68E9 CRC64;
     MRTIQMSSYT VGEDCFEAIA HVLAPHHAQS IVLVGGARAL AAAAPEIRKA LADTSVEILD
     EIVYGTDSTQ SAIDALVRND AFRAADVAFA IGGGKAIDTV KTAAKELDKT VFSVPTICSN
     CSSATAIAVV YNDDHSLKGY AYPDAPAHIF INPAIIAEAP AEYFWAGIGD ALSKQPEVEY
     ATSRADLTHT GTLGLTLAHT CTAPLMTYGE QGLADVRADR SSEAVRQIAL DIVVNTGYVS
     NLTNQPDFYY NSSLAHAFYN ATCGVPRAGR THLHGEVVSF GVLVLFAYMG NTAELERYAA
     FNKNIGLPTT LAELDLDESH LDRIATLAQN TNEWKQGNPE PFSPEAFVEA IRVADAYGRS
     LA
//
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