ID W8UUE1_KLEPN Unreviewed; 362 AA.
AC W8UUE1;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00013190};
DE EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
GN ORFNames=KPNJ2_02483 {ECO:0000313|EMBL:AHM79263.1};
OS Klebsiella pneumoniae 30684/NJST258_2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=1420013 {ECO:0000313|EMBL:AHM79263.1, ECO:0000313|Proteomes:UP000019586};
RN [1] {ECO:0000313|EMBL:AHM79263.1, ECO:0000313|Proteomes:UP000019586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=30684/NJST258_2 {ECO:0000313|EMBL:AHM79263.1};
RX PubMed=24639510; DOI=10.1073/pnas.1321364111;
RA Deleo F.R., Chen L., Porcella S.F., Martens C.A., Kobayashi S.D.,
RA Porter A.R., Chavda K.D., Jacobs M.R., Mathema B., Olsen R.J., Bonomo R.A.,
RA Musser J.M., Kreiswirth B.N.;
RT "Molecular dissection of the evolution of carbapenem-resistant multilocus
RT sequence type 258 Klebsiella pneumoniae.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:4988-4993(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH;
CC Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001146};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a secondary alcohol + NAD(+) = a ketone + H(+) + NADH;
CC Xref=Rhea:RHEA:10740, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087,
CC ChEBI:CHEBI:35681, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000781};
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}.
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DR EMBL; CP006918; AHM79263.1; -; Genomic_DNA.
DR RefSeq; WP_002907491.1; NZ_CP006918.1.
DR AlphaFoldDB; W8UUE1; -.
DR SMR; W8UUE1; -.
DR KEGG; kps:KPNJ2_02483; -.
DR PATRIC; fig|1420013.3.peg.2336; -.
DR HOGENOM; CLU_026673_14_1_6; -.
DR Proteomes; UP000019586; Chromosome.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:RHEA.
DR GO; GO:0018456; F:aryl-alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08278; benzyl_alcohol_DH; 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; 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; 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 ECO:0000313|EMBL:AHM79263.1}; Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 10..361
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 362 AA; 37623 MW; BEA94C0BB0D4449A CRC64;
MQVKAAVTLG YQQPFVIKDV EVAPPGKDEI LVKIVATGVC HTDAVMRDNP GVVPMPAILG
HEGAGIVASV GEAVSGIRVG DHVVLSYAAC HHCENCLSNH PSACEDFNTL NFGGRREDGT
TPYRLGDQDL SLFFGQSSFS QYVVTRASNA VVVDPEVDLT LLGPLGCGIQ TGSGTVLNRL
KPVVGESLVV FGCGAVGLSA IMAAKLTGCS QIIAVDIHAS RLALAGELGA THQINGKEQD
AVAVIKQITG KGAHYAVETT GVSAIVLQAV HAVKPLGTVA IVGFTGDITL NVQNDLMAEG
KSLVGVIEGD AVPALFIPLL VQLYKQGKFP IDKLIARYPL ADINQAFADS ASGKVIKPVV
VM
//
