ID T0CX93_ALIAG Unreviewed; 344 AA.
AC T0CX93; A0A9E6ZMV4;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Zinc-type alcohol dehydrogenase-like protein {ECO:0000256|RuleBase:RU364000};
GN ORFNames=K1I37_09580 {ECO:0000313|EMBL:UNO50656.1};
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:UNO50656.1, 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 -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Quinone oxidoreductase subfamily.
CC {ECO:0000256|RuleBase:RU364000}.
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; UNO50656.1; -; Genomic_DNA.
DR RefSeq; WP_021298374.1; NZ_AURB01000187.1.
DR STRING; 1356854.N007_16090; -.
DR KEGG; aaco:K1I37_09580; -.
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; cd08252; AL_MDR; 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; IPR013154; ADH-like_N.
DR InterPro; IPR014182; ADH_Zn_typ-1.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR NCBIfam; TIGR02817; adh_fam_1; 1.
DR PANTHER; PTHR44154; QUINONE OXIDOREDUCTASE; 1.
DR PANTHER; PTHR44154:SF1; QUINONE OXIDOREDUCTASE; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|RuleBase:RU364000};
KW Oxidoreductase {ECO:0000256|RuleBase:RU364000};
KW Reference proteome {ECO:0000313|Proteomes:UP000829401};
KW Zinc {ECO:0000256|RuleBase:RU364000}.
SQ SEQUENCE 344 AA; 37630 MW; 3AD1113EFECAFB44 CRC64;
MTSTTMKAVG LYKYLPIDHP ESLIDVEIEK PTPTGRDLLV RVKAISVNPV DVKVRAPKDR
TETKPRVIGW DVAGVVEETG PDCTLFKPGD EVYYAGSLVR AGGNSEFHLV DERIVGFKPA
TLDFAQAAAL PLTSLTAWEG LFDRLGISSE PGSNPGRTIL IIGAAGGVGS IAIQLAKYAG
LTVIGTASRP ESAEWVKGLG ADHVINHFED FVPQLKALGL ESVDYIFCLN STEKHWRNMA
EAIAPQGKIC SIVETDELLD LTLLKNKSVT FVWEFMFTRS MYETADMIEQ HKLLNELAGL
VDQGIVRTTV NEKLEPINAE NLRKAHAMLE SGSMVGKVVL EHFR
//
