ID A0A1F8JQF7_9BACT Unreviewed; 338 AA.
AC A0A1F8JQF7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00013190};
DE EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
GN ORFNames=A3E26_02725 {ECO:0000313|EMBL:OGN63556.1};
OS Chlamydiae bacterium RIFCSPHIGHO2_12_FULL_49_32.
OC Bacteria; Chlamydiota.
OX NCBI_TaxID=1797604 {ECO:0000313|EMBL:OGN63556.1, ECO:0000313|Proteomes:UP000176567};
RN [1] {ECO:0000313|EMBL:OGN63556.1, ECO:0000313|Proteomes:UP000176567}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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}.
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:OGN63556.1}.
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DR EMBL; MGLX01000037; OGN63556.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8JQF7; -.
DR Proteomes; UP000176567; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08297; CAD3; 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; 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 8..334
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 338 AA; 36094 MW; AD96C94156009955 CRC64;
MKAAVVHAFD KPLVVEDVAK PTPGPGEVIV KMETSGICHT DIHAAHGDWP VKPKLPFIPG
HEGIGIVESI GSQVTEVKEG DRVALPWLGY ACGSCEYCVS GWETLCLKQL NTGYAINGSY
GEYAKAFAKY VGKVPKGIDP KEAAPLTCAG VTTYKAVKMS GARSSDLVAI FGVGGLGHLA
LQYAKIAGAT VAAVDLFDDK LKMAKELGAD LTINASKQDP VKELQKLGGA DAVVCTAVSP
KSFEQGFYSL RRGGTLVFVG LPKENLIQIP IFQTVLGGIH IVGSIVGNRL DLAEVFELHA
AGRTKVYLEC RKLETINECF HEVETGKIPA RLVIDYRK
//
