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Database: UniProt
Entry: L8TMR8_9MICC
LinkDB: L8TMR8_9MICC
Original site: L8TMR8_9MICC 
ID   L8TMR8_9MICC            Unreviewed;       372 AA.
AC   L8TMR8;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:ELT42936.1};
GN   ORFNames=G205_21484 {ECO:0000313|EMBL:ELT42936.1};
OS   Arthrobacter nitrophenolicus.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=683150 {ECO:0000313|EMBL:ELT42936.1, ECO:0000313|Proteomes:UP000011189};
RN   [1] {ECO:0000313|Proteomes:UP000011189}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SJCon {ECO:0000313|Proteomes:UP000011189};
RX   PubMed=23516196; DOI=10.1128/genomeA.00058-13;
RA   Vikram S., Kumar S., Vaidya B., Pinnaka A.K., Raghava G.P.;
RT   "Draft Genome Sequence of the 2-Chloro-4-Nitrophenol-Degrading Bacterium
RT   Arthrobacter sp. Strain SJCon.";
RL   Genome Announc. 1:e0005813-e0005813(2013).
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:ELT42936.1}.
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DR   EMBL; AOFD01000073; ELT42936.1; -; Genomic_DNA.
DR   RefSeq; WP_009359379.1; NZ_AOFD01000073.1.
DR   AlphaFoldDB; L8TMR8; -.
DR   PATRIC; fig|683150.5.peg.4206; -.
DR   Proteomes; UP000011189; 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; PTHR43880; ALCOHOL DEHYDROGENASE; 1.
DR   PANTHER; PTHR43880:SF12; ALCOHOL DEHYDROGENASE CLASS-3; 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   Reference proteome {ECO:0000313|Proteomes:UP000011189};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          13..366
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   372 AA;  38256 MW;  BD4898EB5581CFF4 CRC64;
     MRAAVLYNTV PAGTSYSEAR PLTVEELERP EPRAGELGIS ITYSSLCHSD LSVVDGSRVR
     PLPMALGHEA VGRVVSVGDG VTDVSPGDHV VLVFVPSCGD CRACRAGRPA LCHRAADVNG
     SGDLLHGEAL LRTRSGERIN HHLGVSAFAD YAVVARESVV VVDDDIPDTV AAMFGCAVLT
     GMGAVFNTAQ VDGGQSVAVF GLGAVGLSAV MAARIARAAS IIAIDPNPGK HQLALDCGAS
     AAGTPEEAAG LIAGAAGDGV DVAVEAVGSA RVIASCLELV ARGGAVVSVG LPHPSAELVV
     PALQFAGAGK RLLGSYMGDA VPDRDIPRYL EYWRDGRLPV ELLHSDTRPL AEINEGLDAL
     AAGKVVRRLF RP
//
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