ID A0A1G7UD55_9LACT Unreviewed; 366 AA.
AC A0A1G7UD55;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Uncharacterized oxidoreductase {ECO:0000313|EMBL:SDG45397.1};
GN ORFNames=SAMN05421791_10952 {ECO:0000313|EMBL:SDG45397.1};
OS Facklamia miroungae.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Facklamia.
OX NCBI_TaxID=120956 {ECO:0000313|EMBL:SDG45397.1, ECO:0000313|Proteomes:UP000199708};
RN [1] {ECO:0000313|EMBL:SDG45397.1, ECO:0000313|Proteomes:UP000199708}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-466 {ECO:0000313|EMBL:SDG45397.1,
RC ECO:0000313|Proteomes:UP000199708};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FNCK01000009; SDG45397.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7UD55; -.
DR STRING; 120956.SAMN05421791_10952; -.
DR OrthoDB; 5198708at2; -.
DR Proteomes; UP000199708; 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:UP000199708};
KW Zinc {ECO:0000256|PIRSR:PIRSR000112-1}.
FT DOMAIN 11..352
FT /note="Alcohol dehydrogenase iron-type/glycerol
FT dehydrogenase GldA"
FT /evidence="ECO:0000259|Pfam:PF00465"
FT BINDING 97..101
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT BINDING 119..122
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 130
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT BINDING 134
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT BINDING 175
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
FT BINDING 260
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
FT BINDING 278
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
SQ SEQUENCE 366 AA; 41204 MW; DA9376203FF929E1 CRC64;
MFNNLTVKVG PQVYRYNVNA IDTVPEVLTE YSAERVLIVH GTISWQKAKA KINFLDDERF
EFYYHQYTGV CSYVGAQTIA DKVEKEGISF IIGVGGGSLA DLVGYSAHLA NVPFGIIPTL
ASNCAPWTPL SVMYKETGES EGKTEHYLRQ AAFLITDPEL VIDAPVKYFI AGLADTIAKW
YECESILKQE HLQNDPFLKL GGYTAKLSSE VIIEHSAQAI KDMENQEVTH SFKYLSEIIF
GVAGLVGGLG DKFARNAAAH AMHDALGKYI PASQKFLHGE KVAYGIFYQM ALEQRWEEID
KLMPFYKELK LPVSLHQMGL YPENEDTLNK MVEFIDSLEK VHLIPVQITK DRLFKAIIDL
EDYIQK
//