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Database: UniProt
Entry: A0A0J1GDK3_9FIRM
LinkDB: A0A0J1GDK3_9FIRM
Original site: A0A0J1GDK3_9FIRM 
ID   A0A0J1GDK3_9FIRM        Unreviewed;       430 AA.
AC   A0A0J1GDK3;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Glycerol dehydrogenase {ECO:0000256|ARBA:ARBA00040132};
DE            EC=1.1.1.6 {ECO:0000256|ARBA:ARBA00039147};
GN   ORFNames=RHS_0445 {ECO:0000313|EMBL:KLU73589.1};
OS   Robinsoniella sp. RHS.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Robinsoniella.
OX   NCBI_TaxID=1504536 {ECO:0000313|EMBL:KLU73589.1, ECO:0000313|Proteomes:UP000036477};
RN   [1] {ECO:0000313|EMBL:KLU73589.1, ECO:0000313|Proteomes:UP000036477}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHS {ECO:0000313|EMBL:KLU73589.1};
RX   PubMed=25284151; DOI=10.1016/j.cell.2014.09.008;
RA   Seedorf H., Griffin N.W., Ridaura V.K., Reyes A., Cheng J., Rey F.E.,
RA   Smith M.I., Simon G.M., Scheffrahn R.H., Woebken D., Spormann A.M.,
RA   Van Treuren W., Ursell L.K., Pirrung M., Robbins-Pianka A., Cantarel B.L.,
RA   Lombard V., Henrissat B., Knight R., Gordon J.I.;
RT   "Bacteria from diverse habitats colonize and compete in the mouse gut.";
RL   Cell 159:253-266(2014).
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   -!- 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:KLU73589.1}.
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DR   EMBL; JNGB01000003; KLU73589.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J1GDK3; -.
DR   PATRIC; fig|1504536.3.peg.3748; -.
DR   Proteomes; UP000036477; 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   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   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036477}.
FT   DOMAIN          58..407
FT                   /note="Alcohol dehydrogenase iron-type/glycerol
FT                   dehydrogenase GldA"
FT                   /evidence="ECO:0000259|Pfam:PF00465"
SQ   SEQUENCE   430 AA;  45965 MW;  B22CD3EFBE73340F CRC64;
     MLLALHEITI PESDDKKLRY RIIISGHHSS LYPLCIPAKI KPSNTAGGIK MRKAFICPTK
     YVQGEDEIRN LGYFVKTFGS SALLIAHPDD VGRVKEKLLI TAKEYQISFV ESGFKGECSR
     QEVARLQELA KEKGCHCTIG LGGGKAIDTA KCVAAGEALI IVPTIAATDA PTSHSAVLYT
     PDGAFDDYAY FKQSPSVILI DTTVIAQAPS RFLVSGMGDA LSTYFEARAT AASCSNVNAG
     LPCGFREGCC GPAKGTNTAM ALASLCYQTL MEDGEKAKTA CDCNQVTPAL ENIIETNILL
     SGLGFESAGL GGAHAIHDGL TIFEGTHKYF HGEKVAFGTL AQLVLENAPS KEIEEVLDFC
     LKIGLPVCLE DIGVDQFTTE ELMEAANKAC IPEESIHAMP FPVTPQSVAA AIITADRIGK
     NFKEESRCGK
//
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