ID K0IE04_NITGG Unreviewed; 350 AA.
AC K0IE04;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE SubName: Full=NAD-dependent alcohol dehydrogenase {ECO:0000313|EMBL:AFU59601.1};
DE EC=1.1.1.1 {ECO:0000313|EMBL:AFU59601.1};
GN Name=adh4 {ECO:0000313|EMBL:AFU59601.1};
GN OrderedLocusNames=Ngar_c26800 {ECO:0000313|EMBL:AFU59601.1};
OS Nitrososphaera gargensis (strain Ga9.2).
OC Archaea; Nitrososphaerota; Nitrososphaeria; Nitrososphaerales;
OC Nitrososphaeraceae; Nitrososphaera.
OX NCBI_TaxID=1237085 {ECO:0000313|EMBL:AFU59601.1, ECO:0000313|Proteomes:UP000008037};
RN [1] {ECO:0000313|EMBL:AFU59601.1, ECO:0000313|Proteomes:UP000008037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ga9.2 {ECO:0000313|Proteomes:UP000008037};
RX PubMed=23057602; DOI=10.1111/j.1462-2920.2012.02893.x;
RA Spang A., Poehlein A., Offre P., Zumbragel S., Haider S., Rychlik N.,
RA Nowka B., Schmeisser C., Lebedeva E.V., Rattei T., Bohm C., Schmid M.,
RA Galushko A., Hatzenpichler R., Weinmaier T., Daniel R., Schleper C.,
RA Spieck E., Streit W., Wagner M.;
RT "The genome of the ammonia-oxidizing Candidatus Nitrososphaera gargensis:
RT insights into metabolic versatility and environmental adaptations.";
RL Environ. Microbiol. 14:3122-45(2012).
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|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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DR EMBL; CP002408; AFU59601.1; -; Genomic_DNA.
DR AlphaFoldDB; K0IE04; -.
DR STRING; 1237085.Ngar_c26800; -.
DR KEGG; nga:Ngar_c26800; -.
DR PATRIC; fig|1237085.11.peg.2655; -.
DR HOGENOM; CLU_026673_11_2_2; -.
DR InParanoid; K0IE04; -.
DR OMA; CERQTQP; -.
DR OrthoDB; 73567at2157; -.
DR Proteomes; UP000008037; Chromosome.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08240; 6_hydroxyhexanoate_dh_like; 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; PTHR43401:SF4; ALCOHOL DEHYDROGENASE GROES DOMAIN PROTEIN; 1.
DR PANTHER; PTHR43401; 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 ECO:0000313|EMBL:AFU59601.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008037};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 8..348
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 350 AA; 37108 MW; DC72E19607A41354 CRC64;
MKAARIIKTK EPLEIKDVGV PKPKNDQVLV RVESAGVCHS DLHLWEGGYA GPQGVFMKVE
DRGVKFPLTP GHEIAGTIEE MGESVTGFSK GEKVLVYPWI GEGTCPACRV GEENVCDAPR
SLGIYQDGGY SEMVLVPSHK YLVKLQGLDP NSAASLACSG LTAYTAVKKA GAQPGDTLVI
VGAGGLGLMA VQIAKSITNA RIAIVDIDDK KLAEAKRLGA HEVINSGASD SVKGVKDITN
NFGAEAVIDF VNNAKTAPNS LNMLRKRGRL VMVGLFGGSL ELNLPLIPLR AFTLTGAYTG
KFADLVELVA LARMDKIQSV VSRKFTLDQA NSALEELKSG KIIGRAVINP
//