ID A0A1E8VWI7_9ACTN Unreviewed; 364 AA.
AC A0A1E8VWI7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Glycerol dehydrogenase {ECO:0000256|ARBA:ARBA00040132};
DE EC=1.1.1.6 {ECO:0000256|ARBA:ARBA00039147};
GN ORFNames=HMPREF2826_04185 {ECO:0000313|EMBL:OFK23703.1};
OS Olsenella sp. HMSC062G07.
OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales; Atopobiaceae;
OC Olsenella.
OX NCBI_TaxID=1739330 {ECO:0000313|EMBL:OFK23703.1, ECO:0000313|Proteomes:UP000176754};
RN [1] {ECO:0000313|Proteomes:UP000176754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMSC062G07 {ECO:0000313|Proteomes:UP000176754};
RA Mitreva M., Pepin K.H., Mihindukulasuriya K.A., Fulton R., Fronick C.,
RA O'Laughlin M., Miner T., Herter B., Rosa B.A., Cordes M., Tomlinson C.,
RA Wollam A., Palsikar V.B., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2016) 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:OFK23703.1}.
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DR EMBL; LTFF01000026; OFK23703.1; -; Genomic_DNA.
DR RefSeq; WP_070639466.1; NZ_KV806951.1.
DR AlphaFoldDB; A0A1E8VWI7; -.
DR STRING; 1739330.HMPREF2826_04185; -.
DR OrthoDB; 323926at2; -.
DR Proteomes; UP000176754; 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; cd08550; 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:UP000176754};
KW Zinc {ECO:0000256|PIRSR:PIRSR000112-1}.
FT DOMAIN 17..345
FT /note="Alcohol dehydrogenase iron-type/glycerol
FT dehydrogenase GldA"
FT /evidence="ECO:0000259|Pfam:PF00465"
FT BINDING 101..105
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT BINDING 123..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 138
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT BINDING 178
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
FT BINDING 264
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
FT BINDING 283
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
SQ SEQUENCE 364 AA; 39540 MW; B02AF1374CF9751C CRC64;
MADTSKLDTA IKFGAGRYRQ ERGLIGSCGE EVARFGTRPL VVTGPNSWAA VGEPLLEDFA
AAGLAPKVEV FDGWCSFEAA EDLAKAARAH GADEIVGVGG GKIMDLAKAV GETAGLGTVN
IPTSASSCAP FTCMSVMYTA EGGKKLSWRF DHEIDACLMD MDVIAACPIR FNAAGIIDAM
AKRIEMLNGK PALSLDDTPV DVFTAYSVAE YTYRVLKDVA LRAIEDNRRH EATKALNDMA
FMNVPVTGVI ANTTKSFRQS ELAHVIYDGV RTIFTEEGQD AIHGEVVGVG LFCQLYFNGQ
QGQEQELRDL MRAMDMPLTF PDLGIKATDK NLDAIEEYIV NSRHYNSTDP ADRRRLHEAV
HEMA
//