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Database: UniProt
Entry: R6AFV1_9FIRM
LinkDB: R6AFV1_9FIRM
Original site: R6AFV1_9FIRM 
ID   R6AFV1_9FIRM            Unreviewed;       352 AA.
AC   R6AFV1;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Glycerol dehydrogenase {ECO:0000256|ARBA:ARBA00040132};
DE            EC=1.1.1.6 {ECO:0000256|ARBA:ARBA00039147};
GN   ORFNames=BN678_00998 {ECO:0000313|EMBL:CDA47654.1};
OS   Dialister sp. CAG:486.
OC   Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC   Dialister; environmental samples.
OX   NCBI_TaxID=1262870 {ECO:0000313|EMBL:CDA47654.1, ECO:0000313|Proteomes:UP000017985};
RN   [1] {ECO:0000313|EMBL:CDA47654.1, ECO:0000313|Proteomes:UP000017985}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:486 {ECO:0000313|Proteomes:UP000017985};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CDA47654.1}.
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DR   EMBL; CBBY010000074; CDA47654.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6AFV1; -.
DR   STRING; 1262870.BN678_00998; -.
DR   Proteomes; UP000017985; 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:UP000017985};
KW   Zinc {ECO:0000256|PIRSR:PIRSR000112-1}.
FT   DOMAIN          10..339
FT                   /note="Alcohol dehydrogenase iron-type/glycerol
FT                   dehydrogenase GldA"
FT                   /evidence="ECO:0000259|Pfam:PF00465"
FT   BINDING         92..96
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT   BINDING         114..117
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT   BINDING         123
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT   BINDING         129
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT   BINDING         169
FT                   /ligand="glycerol"
FT                   /ligand_id="ChEBI:CHEBI:17754"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
FT   BINDING         252
FT                   /ligand="glycerol"
FT                   /ligand_id="ChEBI:CHEBI:17754"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
FT   BINDING         269
FT                   /ligand="glycerol"
FT                   /ligand_id="ChEBI:CHEBI:17754"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
SQ   SEQUENCE   352 AA;  38823 MW;  F1D64755D9E0058B CRC64;
     MKSTFFPHFT IGVDAYDAIP DICLDYGKTA VIVGGEKSRA AAEPLIRKAI EGKIELLGSF
     QYGDDATFEN AEALTRIPEI RKADMVFAVG GGRATDTAKW ATHLLKKPLF TFPTLASNCA
     SVTAVCIMYH PDHSFKGSIY RDRNAYHTFI NTEVIAHSPR EYFWAGLGDA LAKQYEVPFS
     ARGMDLTWVQ ETGVRNAQNV APGILKYGKA ALEAVDKGIV TDALEPAILS IIVAPGMASV
     CIEDDLDSSL AHAIYNSHTR TPHKGNHLHG AVVNYGLQVM LTMDGQIEER DKIYRFAKSI
     GLPHCLSDIG IDPAHPDELV ENCLHTKDMR VKPYDITFDM VYKAMMELEK LK
//
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