ID A0A1G0XHE4_9BACT Unreviewed; 317 AA.
AC A0A1G0XHE4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0000259|SMART:SM00829};
GN ORFNames=A2523_12120 {ECO:0000313|EMBL:OGV33092.1};
OS Ignavibacteria bacterium RIFOXYD12_FULL_36_8.
OC Bacteria; Ignavibacteriota; Ignavibacteria.
OX NCBI_TaxID=1798454 {ECO:0000313|EMBL:OGV33092.1, ECO:0000313|Proteomes:UP000177243};
RN [1] {ECO:0000313|EMBL:OGV33092.1, ECO:0000313|Proteomes:UP000177243}
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|RuleBase:RU361277};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {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:OGV33092.1}.
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DR EMBL; MHBA01000029; OGV33092.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G0XHE4; -.
DR STRING; 1798454.A2523_12120; -.
DR Proteomes; UP000177243; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 2.
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; PTHR43401; L-THREONINE 3-DEHYDROGENASE; 1.
DR PANTHER; PTHR43401:SF2; L-THREONINE 3-DEHYDROGENASE; 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|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 8..314
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 317 AA; 35508 MW; E6A71B26AF6CA4F5 CRC64;
MKAAVLYGAH DWKIEDRRTP LFGDNECLIK IKACGVCHSE IHQWETRVEG LEYPRYIGHE
VAGEILKVGS HVKQFKVGDR VAAWADGRGY AEEIAVSTEF LSLISDEIPY EHALSEPIAC
TTNAVLRTNV QLGDTIALVG MGFMGLIMLQ ELRLIGAKKI IAVDVRKEML ELSAKLGADI
QLNPDEHDID LEIKKLTGEK GVDISFEIGG NQSTLDLASQ ICRMEGKLVI FGYHPGSRII
KDLGYWNWMA FDIINAHFRD MKTILNGMKR GMDLFNAGKI KMDKLITHKF RLDKIEDAFT
SAKNKPIGFV KSVIVFD
//
