ID A0A0Q6Z1L4_9BRAD Unreviewed; 361 AA.
AC A0A0Q6Z1L4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Glycerol dehydrogenase {ECO:0000256|ARBA:ARBA00040132};
DE EC=1.1.1.6 {ECO:0000256|ARBA:ARBA00039147};
GN ORFNames=ASC80_01105 {ECO:0000313|EMBL:KQW22031.1};
OS Afipia sp. Root123D2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Afipia.
OX NCBI_TaxID=1736436 {ECO:0000313|EMBL:KQW22031.1, ECO:0000313|Proteomes:UP000051348};
RN [1] {ECO:0000313|EMBL:KQW22031.1, ECO:0000313|Proteomes:UP000051348}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root123D2 {ECO:0000313|EMBL:KQW22031.1,
RC ECO:0000313|Proteomes:UP000051348};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW22031.1, ECO:0000313|Proteomes:UP000051348}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root123D2 {ECO:0000313|EMBL:KQW22031.1,
RC ECO:0000313|Proteomes:UP000051348};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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 -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00007358}.
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:KQW22031.1}.
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DR EMBL; LMDP01000001; KQW22031.1; -; Genomic_DNA.
DR RefSeq; WP_056292043.1; NZ_LMDP01000001.1.
DR AlphaFoldDB; A0A0Q6Z1L4; -.
DR STRING; 1736436.ASC80_01105; -.
DR OrthoDB; 5198708at2; -.
DR Proteomes; UP000051348; 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; 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.
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:UP000051348};
KW Zinc {ECO:0000256|PIRSR:PIRSR000112-1}.
FT DOMAIN 9..337
FT /note="Alcohol dehydrogenase iron-type/glycerol
FT dehydrogenase GldA"
FT /evidence="ECO:0000259|Pfam:PF00465"
FT BINDING 38
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT BINDING 95..99
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 122
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-2"
FT BINDING 126
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT BINDING 128
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 172
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
FT BINDING 255
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
FT BINDING 272
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
SQ SEQUENCE 361 AA; 38329 MW; C265B367337B7CD9 CRC64;
MTIRAFGGPH RYVQGPGALS ELATLVPMYG RRPLIVADVA VLGSLRPQLE ALLKPCVDGW
VFAEFSGECS ASQIDLMASK ADATKSDVVV AIGGGKAIDT AKGVRILRGG GIIVVPTVAS
NDAPTSRLAI VYTDDHVLKE VRMMATNPDA VVVDTSVIAR APRRFFVAGI GDALTKKFEA
EQCYNSGGLN FYKARPAALA VFIADQCYQV IRRDAIASLA AVDRKEPDPA FENVVEATIL
LSGLGFESGG LSIAHSLTRG FSAIPSLNSS LHGEQVAFGL LTQLCLEKRP AKFLTDMVAF
YREVGLPTSL KDLGFSGNVQ EGIRTIAERS IAEAPYLKQF VGAVTVQNLI AALEDADRCA
A
//
