ID A0A0Q9QMJ3_9MICC Unreviewed; 347 AA.
AC A0A0Q9QMJ3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00013190};
DE EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
GN ORFNames=ASH00_15415 {ECO:0000313|EMBL:KRF04039.1};
OS Arthrobacter sp. Soil782.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1736410 {ECO:0000313|EMBL:KRF04039.1, ECO:0000313|Proteomes:UP000053496};
RN [1] {ECO:0000313|EMBL:KRF04039.1, ECO:0000313|Proteomes:UP000053496}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil782 {ECO:0000313|EMBL:KRF04039.1,
RC ECO:0000313|Proteomes:UP000053496};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRF04039.1, ECO:0000313|Proteomes:UP000053496}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil782 {ECO:0000313|EMBL:KRF04039.1,
RC ECO:0000313|Proteomes:UP000053496};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KRF04039.1}.
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DR EMBL; LMSO01000012; KRF04039.1; -; Genomic_DNA.
DR RefSeq; WP_056550295.1; NZ_LMSO01000012.1.
DR AlphaFoldDB; A0A0Q9QMJ3; -.
DR STRING; 1736410.ASH00_15415; -.
DR OrthoDB; 3567264at2; -.
DR Proteomes; UP000053496; 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; cd05284; arabinose_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; 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..341
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 347 AA; 36567 MW; 13E48E59A0ACF501 CRC64;
MKAVRVHRYR EDPHLDDVDE PTVIGPWDVI VEVGAAGLCR TDLHVIEGQW DHIQHPSLPY
ILGHENAGWV REVGSAVSNV SAGDTVIMHP LVTCGLCMAC REGQDSHCDN ATFPGLNVDG
GMAEYMRTNA RSVVKLDSSL QPADIAALAD AGLTAYHAVR KAVPQLPPGS HAVVIGSGGL
GHIGIQSLKA LTAATVTVVD RSPDALELAV SLGADHTVTA SSDGNGDAGR LLDITDGGAH
VVFDFVGEHG TESLGVTALR NRGSYYSIGY GGAVNIDTIE IISREINVVG NLVGTYTDLV
ELMTLTAQGK VTLHTQKYDL EDAVQAMHDL DSGALVGRGI LVPKLNH
//