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Database: UniProt
Entry: A0A1A0FID1_9GAMM
LinkDB: A0A1A0FID1_9GAMM
Original site: A0A1A0FID1_9GAMM 
ID   A0A1A0FID1_9GAMM        Unreviewed;       399 AA.
AC   A0A1A0FID1;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:OAZ99253.1};
GN   ORFNames=ADS46_02275 {ECO:0000313|EMBL:OAZ99253.1};
OS   Halomonas sp. G11.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=1684425 {ECO:0000313|EMBL:OAZ99253.1, ECO:0000313|Proteomes:UP000092250};
RN   [1] {ECO:0000313|EMBL:OAZ99253.1, ECO:0000313|Proteomes:UP000092250}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G11 {ECO:0000313|EMBL:OAZ99253.1,
RC   ECO:0000313|Proteomes:UP000092250};
RA   Naifar M., Chouchane H., Najjari A., El Hidri D., Mahjoubi M., Ghedira K.,
RA   Soufi L., Salah A., Raddadi N., Sghaier H., Ouzari H.I.,
RA   Eddine Masmoudi A.S., Cherif A.;
RT   "Genomic basis for crude oil degradation, heavy metal resistance and high
RT   salt tolerance of Halomonas hydrocarbonoclasticus G11 isolated from
RT   Tunisian Chott El-Djerid salt lake.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|ARBA:ARBA00001962};
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:OAZ99253.1}.
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DR   EMBL; LYXG01000012; OAZ99253.1; -; Genomic_DNA.
DR   RefSeq; WP_066318157.1; NZ_LYXG01000012.1.
DR   AlphaFoldDB; A0A1A0FID1; -.
DR   OrthoDB; 9815791at2; -.
DR   Proteomes; UP000092250; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; IPR039697; Alcohol_dehydrogenase_Fe.
DR   PANTHER; PTHR11496; ALCOHOL DEHYDROGENASE; 1.
DR   PANTHER; PTHR11496:SF102; ALCOHOL DEHYDROGENASE 4; 1.
DR   Pfam; PF00465; Fe-ADH; 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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          13..366
FT                   /note="Alcohol dehydrogenase iron-type/glycerol
FT                   dehydrogenase GldA"
FT                   /evidence="ECO:0000259|Pfam:PF00465"
SQ   SEQUENCE   399 AA;  41847 MW;  175609700C117EDB CRC64;
     MPLNHFHTGR QTPIIAGPGS LEQLPELRRR LGASRYMVIS DQGLAATGLV DALIDDLTAD
     AEVDTFLAPT GEPSVATADA AAVAVRALPG RPLVIGLGGG TALDIAKLVA ALAESQGDME
     NYLLARTPWA GRVPAVMVPT TSGTGSEVTR TSILTDAGGR KLWAWGDELL PDAVLLDPVL
     TRGLPALLTA TTGLDAFVHA LEATTGQGRH AFIEAPALQA IRQVGQALPT AVTTPNDLVA
     RQRMQEAACL AGQAIDNGGT GIAHNIGHAL GSCYHLPHGV AVTLALEASL AWSVADNEAC
     FAPAAHALKA GSKAQELPRL FRELADQTHF NQALAPFTTQ TLDAETLAST MQKDENAPMA
     RNAARRPTGE DWQWLAEATV SVFDRRVAEL ATQNREISA
//
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