ID T0DK19_ALIAG Unreviewed; 345 AA.
AC T0DK19; A0A9E6ZFY5;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Zinc-dependent alcohol dehydrogenase family protein {ECO:0000313|EMBL:UNO49617.1};
GN ORFNames=K1I37_03485 {ECO:0000313|EMBL:UNO49617.1};
OS Alicyclobacillus acidoterrestris (strain ATCC 49025 / DSM 3922 / CIP 106132
OS / NCIMB 13137 / GD3B).
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC Alicyclobacillus.
OX NCBI_TaxID=1356854 {ECO:0000313|EMBL:UNO49617.1, ECO:0000313|Proteomes:UP000829401};
RN [1] {ECO:0000313|Proteomes:UP000829401}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3922 {ECO:0000313|Proteomes:UP000829401};
RX PubMed=36240455; DOI=10.1093/g3journal/jkac225;
RA Leonardo I.C., Barreto Crespo M.T., Gaspar F.B.;
RT "Unveiling the complete genome sequence of Alicyclobacillus acidoterrestris
RT DSM 3922T, a taint-producing strain.";
RL G3 (Bethesda) 12:0-0(2022).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP080467; UNO49617.1; -; Genomic_DNA.
DR RefSeq; WP_021295360.1; NZ_AURB01000062.1.
DR STRING; 1356854.N007_20685; -.
DR KEGG; aaco:K1I37_03485; -.
DR Proteomes; UP000829401; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08286; FDH_like_ADH2; 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; PTHR42813:SF4; NADP-DEPENDENT ISOPROPANOL DEHYDROGENASE; 1.
DR PANTHER; PTHR42813; ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE; 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:UP000829401};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
SQ SEQUENCE 345 AA; 36448 MW; AB90770CFA56FA4E CRC64;
MKALVYRGPG KKEWVDSPMP TIEAPTDAVV RITKTTICGT DLHILKGDVP AVVEGRTLGH
EGVGVIEEVG SGVHNFKVGD RVLISCVTSC AKCDSCKKGM YSHCEDGGWI LGHLIDGTQA
EYVRIPYADT SLYPLPDGVD EEALVMLSDI LPTGFEVGVL NGKVQPGDTV AIVGAGPVGL
AALLTAQFYS PAEIIAVDLD DNRLEVARKF GATKTVNSSK GNPVEAVLEL TGGKGVDVAI
EAVGIPATFD ICQGIVGAGG RIANVGVHGK SVNLHLEKLW IQNITLTTGL VDTNSTPMLL
KTVAAGKIEP KLLITHRFPL SEILQAYDVF GNAARENALK VILYQ
//
