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Database: UniProt
Entry: E8TDV2_MESCW
LinkDB: E8TDV2_MESCW
Original site: E8TDV2_MESCW 
ID   E8TDV2_MESCW            Unreviewed;       390 AA.
AC   E8TDV2;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=Iron-containing alcohol dehydrogenase {ECO:0000313|EMBL:ADV10995.1};
GN   OrderedLocusNames=Mesci_1841 {ECO:0000313|EMBL:ADV10995.1};
OS   Mesorhizobium ciceri biovar biserrulae (strain HAMBI 2942 / LMG 23838 /
OS   WSM1271).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=765698 {ECO:0000313|EMBL:ADV10995.1, ECO:0000313|Proteomes:UP000007471};
RN   [1] {ECO:0000313|Proteomes:UP000007471}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAMBI 2942 / LMG 23838 / WSM1271
RC   {ECO:0000313|Proteomes:UP000007471};
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Nandasena K., Reeve W.G., Howieson J.G., O'Hara G.,
RA   Tiwari R.P., Woyke T.;
RT   "Complete sequence of chromosome of Mesorhizobium ciceri bv. biserrulae
RT   WSM1271.";
RL   Submitted (JAN-2011) 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}.
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DR   EMBL; CP002447; ADV10995.1; -; Genomic_DNA.
DR   RefSeq; WP_013529684.1; NC_014923.1.
DR   RefSeq; YP_004141045.1; NC_014923.1.
DR   AlphaFoldDB; E8TDV2; -.
DR   STRING; 765698.Mesci_1841; -.
DR   KEGG; mci:Mesci_1841; -.
DR   PATRIC; fig|765698.3.peg.2295; -.
DR   eggNOG; COG1454; Bacteria.
DR   HOGENOM; CLU_007207_0_0_5; -.
DR   OrthoDB; 9815791at2; -.
DR   Proteomes; UP000007471; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd14861; Fe-ADH-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; 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          11..376
FT                   /note="Alcohol dehydrogenase iron-type/glycerol
FT                   dehydrogenase GldA"
FT                   /evidence="ECO:0000259|Pfam:PF00465"
SQ   SEQUENCE   390 AA;  41231 MW;  777ED1CB43667FE5 CRC64;
     MSKLISKWNY PTTVRFGAGR IKELPEVLAA TGIKRPLFVT DPGLAKLPVV ASTLKILDDA
     KVPYGVFSEV RPNPVESNLT AGIAVFKKGK HDGVIAFGGG SALDLGKLIA FQAGQVRPVW
     DFEDVDDWWT RANSDAIAPI IAVPTTAGTG SEVGRAGVIT NEATHTKKVI FHPKLLPAIV
     IADPELSVGM PGFITAGTGM DALAHCLEAY CAPGYHPMAD GIAVEGVRLV FENLPKAYAN
     GRDLVARAHM MSAAAMGATA FQKGLGAIHS LSHPVGALYD THHGMTNAVF MPYVLAFNRD
     SIEERIGRLA AYCGIKGGFD GFAKAIIKLR KELKVPHALP GLIKGLDMDK KRKALIADMA
     VVDPTAGGNP VKLTKKAALT LLENAIAGTV
//
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