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Database: UniProt
Entry: A0A411WKN0_9GAMM
LinkDB: A0A411WKN0_9GAMM
Original site: A0A411WKN0_9GAMM 
ID   A0A411WKN0_9GAMM        Unreviewed;       366 AA.
AC   A0A411WKN0;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Glycerol dehydrogenase {ECO:0000256|ARBA:ARBA00040132};
DE            EC=1.1.1.6 {ECO:0000256|ARBA:ARBA00039147};
GN   ORFNames=EKN56_10135 {ECO:0000313|EMBL:QBH96732.1};
OS   Limnobaculum zhutongyuii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Budviciaceae; Limnobaculum.
OX   NCBI_TaxID=2498113 {ECO:0000313|EMBL:QBH96732.1, ECO:0000313|Proteomes:UP000293154};
RN   [1] {ECO:0000313|EMBL:QBH96732.1, ECO:0000313|Proteomes:UP000293154}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF-458 {ECO:0000313|EMBL:QBH96732.1,
RC   ECO:0000313|Proteomes:UP000293154};
RA   Ge Y.;
RT   "Pragia sp. nov. isolated from the gut tract of Carduelis flavirostris.";
RL   Submitted (MAR-2019) 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}.
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DR   EMBL; CP034752; QBH96732.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A411WKN0; -.
DR   KEGG; prag:EKN56_10135; -.
DR   OrthoDB; 5198708at2; -.
DR   Proteomes; UP000293154; Chromosome.
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.
DR   PROSITE; PS00060; ADH_IRON_2; 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   Zinc {ECO:0000256|PIRSR:PIRSR000112-1}.
FT   DOMAIN          8..348
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         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         121
FT                   /ligand="glycerol"
FT                   /ligand_id="ChEBI:CHEBI:17754"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000112-2"
FT   BINDING         125
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT   BINDING         127
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         171
FT                   /ligand="glycerol"
FT                   /ligand_id="ChEBI:CHEBI:17754"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
FT   BINDING         254
FT                   /ligand="glycerol"
FT                   /ligand_id="ChEBI:CHEBI:17754"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
FT   BINDING         271
FT                   /ligand="glycerol"
FT                   /ligand_id="ChEBI:CHEBI:17754"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
SQ   SEQUENCE   366 AA;  39276 MW;  4127913CA3CAE1AC CRC64;
     MITTAIFPGR YVQGSGAVEK CLGDELSRLG QKALILQDPV VHQKLGNDIV KALEGKIACQ
     VEVFNSECSD EEIDRISALA QNYGAEVIVG IGGGKTLDTA KATGAFLKLP IAIVPTLAST
     DAPCSSLVVI YTQEGKFKRY MMIPRNPDVV LVDSKIIAQA PVRFLVSGIG DALATWFEAE
     DCRIKMAGNM TGRPGPMSAY GLARLCYDTL LQYGVLAKSA CEQQQVTPAL EHVIEANTLL
     SGLGFESGGL AAAHAIHNGL TVLPQTHSYW HGEKVAFGTL AMLMLTDREP EVIDTVYNFC
     RDVGLPTTLE DIGLKQVSDD DLMKVAEASC SQGETIHNEP HEISAENVLA ALRAADAEGQ
     RRKLFA
//
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