ID   A9QPK5_METI4            Unreviewed;       337 AA.
AC   A9QPK5;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   24-JAN-2024, entry version 74.
DE   RecName: Full=alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00013190};
DE            EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
GN   Name=adhP {ECO:0000313|EMBL:ABX56663.1};
OS   Methylacidiphilum infernorum (isolate V4) (Methylokorus infernorum (strain
OS   V4)).
OC   Bacteria; Verrucomicrobiota; Methylacidiphilae; Methylacidiphilales;
OC   Methylacidiphilaceae; Methylacidiphilum (ex Ratnadevi et al. 2023).
OX   NCBI_TaxID=481448 {ECO:0000313|EMBL:ABX56663.1};
RN   [1] {ECO:0000313|EMBL:ABX56663.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=V4 {ECO:0000313|EMBL:ABX56663.1};
RX   PubMed=18004300; DOI=10.1038/nature06411;
RA   Dunfield P.F., Yuryev A., Senin P., Smirnova A.V., Stott M.B., Hou S.,
RA   Ly B., Saw J.H., Zhou Z., Ren Y., Wang J., Mountain B.W., Crowe M.A.,
RA   Weatherby T.M., Bodelier P.L.E., Liesack W., Feng L., Wang L., Alam M.;
RT   "Methane oxidation by an extremely acidophilic bacterium of the phylum
RT   Verrucomicrobia.";
RL   Nature 450:879-882(2007).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|RuleBase:RU361277};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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DR   EMBL; EU223921; ABX56663.1; -; Genomic_DNA.
DR   RefSeq; WP_048810015.1; NC_010794.1.
DR   AlphaFoldDB; A9QPK5; -.
DR   OrthoDB; 9806940at2; -.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd08298; CAD2; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR014187; ADH_Zn_typ-2.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   PANTHER; PTHR42940; ALCOHOL DEHYDROGENASE 1-RELATED; 1.
DR   PANTHER; PTHR42940:SF8; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 11; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          14..335
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   337 AA;  36676 MW;  4A2DD2BA169D2FEB CRC64;
     MKALLLTTPS AIEKQPLRLE QVDIPYPKED EVLVKIEACG VCRSNLHMIE GEWLQRGIPA
     KLPIIPGHEI VGRVEDVGDR VRHFKKGDRV GLQPLWLSCG HCSYCWTGRE ELCPEKEITG
     ETVDGGYAEY VLGKEDHLYP VPETLSAMEA APLFCPGITA YHALKRVGNV MGKRVAIFGI
     GGVGHMALQF ARVAGATTIA ISRNPIHLQV AKELGAEECI HGEDRSALEK LKREGAVDCA
     IVFAPSSAVA QLAISLVNAG GKVVLGVNVE LGSFSFVEEK TVLGTVIGSR EEMREVLRLA
     EERKVKPISQ GFSLEDAPEA LMKLKKGEII MRAVLVL
//