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Database: UniProt
Entry: B7CC58_9FIRM
LinkDB: B7CC58_9FIRM
Original site: B7CC58_9FIRM 
ID   B7CC58_9FIRM            Unreviewed;       360 AA.
AC   B7CC58;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=Glycerol dehydrogenase {ECO:0000256|ARBA:ARBA00040132};
DE            EC=1.1.1.6 {ECO:0000256|ARBA:ARBA00039147};
GN   ORFNames=EUBIFOR_01807 {ECO:0000313|EMBL:EEC89629.1};
OS   Holdemanella biformis DSM 3989.
OC   Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC   Erysipelotrichaceae; Holdemanella.
OX   NCBI_TaxID=518637 {ECO:0000313|EMBL:EEC89629.1, ECO:0000313|Proteomes:UP000004315};
RN   [1] {ECO:0000313|EMBL:EEC89629.1, ECO:0000313|Proteomes:UP000004315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 3989 {ECO:0000313|EMBL:EEC89629.1,
RC   ECO:0000313|Proteomes:UP000004315};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EEC89629.1, ECO:0000313|Proteomes:UP000004315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 3989 {ECO:0000313|EMBL:EEC89629.1,
RC   ECO:0000313|Proteomes:UP000004315};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Eubacterium biforme (DSM 3989).";
RL   Submitted (NOV-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:EEC89629.1}.
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DR   EMBL; ABYT01000096; EEC89629.1; -; Genomic_DNA.
DR   RefSeq; WP_003865594.1; NZ_DS996844.1.
DR   AlphaFoldDB; B7CC58; -.
DR   STRING; 518637.EUBIFOR_01807; -.
DR   eggNOG; COG0371; Bacteria.
DR   HOGENOM; CLU_044754_3_1_9; -.
DR   OrthoDB; 5198708at2; -.
DR   Proteomes; UP000004315; Unassembled WGS sequence.
DR   GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0008888; F:glycerol dehydrogenase [NAD+] activity; IEA:RHEA.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   ECO:0000313|EMBL:EEC89629.1}; 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         117..120
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         132
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT   BINDING         171
FT                   /ligand="glycerol"
FT                   /ligand_id="ChEBI:CHEBI:17754"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
FT   BINDING         257
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   360 AA;  39132 MW;  862E5BA597D16DB8 CRC64;
     MKTIEMSNYS VGESCYNEIP SVCEKYNVKK VVLIGGKRAL AAAEPRIREA IKETDIIITD
     SIVYGVDSTM TNVHKLTSNP NVQEADVIFA IGGGKAIDTC KTASIEMDDK MVFSFPTICS
     NCSAATAIAV VYDDNGALDH YSYPHCPAHI FINPDVIAKA PSEYFWAGIG DALSKQCEVE
     FATQGKTLDH TATMGLALAK TCTEPLLKYG KQGMEDCKND TNSAAIEAIA LDIVVSTGYV
     SNLTNQPEYY YNSSIAHAFY NGSCSIARNG HHLHGEVVSF GVLVLYAYAK DEENLMKMAK
     FNKSIGLPVT LADMDLNESY LEALTQAATK TNEWKNAPFP FTKEEFIAAI KKADAVGQSL
//
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