ID A0A0W7W745_9MICO Unreviewed; 367 AA.
AC A0A0W7W745;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:KUF06373.1};
GN ORFNames=AUL38_13165 {ECO:0000313|EMBL:KUF06373.1};
OS Leucobacter sp. G161.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leucobacter.
OX NCBI_TaxID=663704 {ECO:0000313|EMBL:KUF06373.1, ECO:0000313|Proteomes:UP000053012};
RN [1] {ECO:0000313|EMBL:KUF06373.1, ECO:0000313|Proteomes:UP000053012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G161 {ECO:0000313|EMBL:KUF06373.1,
RC ECO:0000313|Proteomes:UP000053012};
RA Ge S., Dong X.;
RT "High quality draft genome sequence of Leucobacter sp. G161, a distinct and
RT effective chromium reducer.";
RL Submitted (DEC-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|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:KUF06373.1}.
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DR EMBL; LOHP01000069; KUF06373.1; -; Genomic_DNA.
DR RefSeq; WP_059062457.1; NZ_LOHP01000069.1.
DR AlphaFoldDB; A0A0W7W745; -.
DR STRING; 663704.AUL38_13165; -.
DR OrthoDB; 334894at2; -.
DR Proteomes; UP000053012; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; PTHR43350; NAD-DEPENDENT ALCOHOL DEHYDROGENASE; 1.
DR PANTHER; PTHR43350:SF19; RIBULOSE-5-PHOSPHATE REDUCTASE; 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; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000053012};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 19..365
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 367 AA; 37967 MW; 541A8E9571B01953 CRC64;
MTHIRGAVLT ASGSPQPWAQ SQPIEVRELE LRDPGAGELL VRIEAASVCH SDLSVVNGSR
PRPLPMLLGH EAAGRVEAVG SDSDAILIGR RVVMTFLPRC GTCASCLTDG LLPCEPGSAA
NAAGTLMSEE TRIFQGSEPI RHHLGVSGFA THAVVDARSV VPVDDDVPPD IAALLGCAVL
TGGGAVVNAG KPAEGDTVAV IGLGGVGMAA LLVAHAEGHR VVGIDANEHK FAAALAAGAA
ECVTPQQALE RSMRFPVVVE CAGHARAFET AYQVTAPGGR TVTVGLPAPD QRSEISPLTL
TAEARTVIGS YLGSAVPSRD IPRYAQLWRD GKLGLEALIS ATIELDDINA AMDALETGDA
LRQIIRF
//
