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Database: UniProt
Entry: R2S8J5_9ENTE
LinkDB: R2S8J5_9ENTE
Original site: R2S8J5_9ENTE 
ID   R2S8J5_9ENTE            Unreviewed;       364 AA.
AC   R2S8J5;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   RecName: Full=Alcohol dehydrogenase iron-type/glycerol dehydrogenase GldA domain-containing protein {ECO:0000259|Pfam:PF00465};
GN   ORFNames=UAU_03162 {ECO:0000313|EMBL:EOH91860.1};
OS   Enterococcus pallens ATCC BAA-351.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=1158607 {ECO:0000313|EMBL:EOH91860.1, ECO:0000313|Proteomes:UP000013782};
RN   [1] {ECO:0000313|EMBL:EOH91860.1, ECO:0000313|Proteomes:UP000013782}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-351 {ECO:0000313|EMBL:EOH91860.1,
RC   ECO:0000313|Proteomes:UP000013782};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A.M., Gilmore M.S., Lebreton F., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Enterococcus pallens BAA-351.";
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
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   -!- 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:EOH91860.1}.
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DR   EMBL; AJAQ01000033; EOH91860.1; -; Genomic_DNA.
DR   RefSeq; WP_010758144.1; NZ_KB946309.1.
DR   AlphaFoldDB; R2S8J5; -.
DR   STRING; 160454.RV10_GL004980; -.
DR   PATRIC; fig|1158607.3.peg.3150; -.
DR   eggNOG; COG0371; Bacteria.
DR   HOGENOM; CLU_044754_2_0_9; -.
DR   OrthoDB; 5198708at2; -.
DR   Proteomes; UP000013782; 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   CDD; cd08172; 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; IPR018211; ADH_Fe_CS.
DR   InterPro; IPR016205; Glycerol_DH.
DR   PANTHER; PTHR43616; GLYCEROL DEHYDROGENASE; 1.
DR   PANTHER; PTHR43616:SF3; HYDROXYCARBOXYLATE DEHYDROGENASE A; 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   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000112-1}; NAD {ECO:0000256|PIRSR:PIRSR000112-3};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013782};
KW   Zinc {ECO:0000256|PIRSR:PIRSR000112-1}.
FT   DOMAIN          11..346
FT                   /note="Alcohol dehydrogenase iron-type/glycerol
FT                   dehydrogenase GldA"
FT                   /evidence="ECO:0000259|Pfam:PF00465"
FT   BINDING         95..99
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
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         256
FT                   /ligand="glycerol"
FT                   /ligand_id="ChEBI:CHEBI:17754"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
FT   BINDING         273
FT                   /ligand="glycerol"
FT                   /ligand_id="ChEBI:CHEBI:17754"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
SQ   SEQUENCE   364 AA;  40514 MW;  13A720B05BD377E7 CRC64;
     MATNLIVRGA PQEYELKTDA WQALPEHLAR RNLSKVMILH GETSWQAVKS YFPSLPNCET
     FFYYYGKKCT DEAAEHFVQI ARENQAEVLI AVGGGKVADL TKLTAYHLNL PVIILPTLAA
     TCAAYTPLSV VYNDEGVMLR YDIFPKATDL VLIDPQVLLE SPYELMVAGI GDTLAKWYES
     DAIISQLTIK PIEIQVAEFA AKKCRDILLA ESSAALQAMR AQQLNQAFID IVETNILLAG
     MVGGFGDEYG RTSGAHSIHD ALTVLPDSHK QLHGNKVAYG ILVQLMIEQK VAEIRQLLPF
     YQKLDLPINL QAMNLSLTED DYQQVAKRAS APDEMIHFMK ETITPEVIIQ AMKDLEILTT
     DAWS
//
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