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Database: UniProt
Entry: A0A0J1J1V0_9FIRM
LinkDB: A0A0J1J1V0_9FIRM
Original site: A0A0J1J1V0_9FIRM 
ID   A0A0J1J1V0_9FIRM        Unreviewed;       387 AA.
AC   A0A0J1J1V0;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Alcohol dehydrogenase iron-type/glycerol dehydrogenase GldA domain-containing protein {ECO:0000259|Pfam:PF00465};
GN   ORFNames=RHS_3160 {ECO:0000313|EMBL:KLU71051.1};
OS   Robinsoniella sp. RHS.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Robinsoniella.
OX   NCBI_TaxID=1504536 {ECO:0000313|EMBL:KLU71051.1, ECO:0000313|Proteomes:UP000036477};
RN   [1] {ECO:0000313|EMBL:KLU71051.1, ECO:0000313|Proteomes:UP000036477}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHS {ECO:0000313|EMBL:KLU71051.1};
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   -!- 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:KLU71051.1}.
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DR   EMBL; JNGB01000030; KLU71051.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J1J1V0; -.
DR   PATRIC; fig|1504536.3.peg.4052; -.
DR   Proteomes; UP000036477; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd08188; PDDH; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036477}.
FT   DOMAIN          9..370
FT                   /note="Alcohol dehydrogenase iron-type/glycerol
FT                   dehydrogenase GldA"
FT                   /evidence="ECO:0000259|Pfam:PF00465"
SQ   SEQUENCE   387 AA;  41784 MW;  1E881F0D8003D63A CRC64;
     MNYRELYQPA HTLIGKGCIC EIPRHIDLIS GKKAFIVTDK PLVDIGTVKK VTDVLDSAGK
     DYTIYDGVKP NPTVSIVNEA KSLFDREHCD YMIGIGGGSS LDVSKAVSIL ANNGGDIAAY
     NGLNKSKNPG IPLIAINTTA GTGSEVTRAY VVTDEINKVK MLMVDANCLS YLAINDPMLM
     LDMPAFLTAS TGMDALTHAI EAYTAKSHFP FTDGIALEAI HLIGMSLEKA VFEGRNIEAR
     TDMCWAEYMA GLAFSNSGLG MVHAMAHQLG GFYNTPHGVA NAILLPYVMK YNTSVCKERY
     SRIGQALGID TSRMTADQGA AAAICHIREL SQRIGIPKLN TTSFRPSDVV TLSLHALEDT
     GMPENPKEAA LVDVQKVYMD AYYDSAP
//
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