ID A7KGA3_KLEPN Unreviewed; 305 AA.
AC A7KGA3;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE RecName: Full=Zinc-type alcohol dehydrogenase-like protein {ECO:0000256|RuleBase:RU364000};
OS Klebsiella pneumoniae.
OG Plasmid pK29 {ECO:0000313|EMBL:ABQ02970.1}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=573 {ECO:0000313|EMBL:ABQ02970.1};
RN [1] {ECO:0000313|EMBL:ABQ02970.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NK29 {ECO:0000313|EMBL:ABQ02970.1};
RC PLASMID=pK29 {ECO:0000313|EMBL:ABQ02970.1};
RX PubMed=17526756; DOI=10.1128/AAC.00167-07;
RA Chen Y.T., Lauderdale T.L., Liao T.L., Shiau Y.R., Shu H.Y., Wu K.M.,
RA Yan J.J., Su I.J., Tsai S.F.;
RT "Sequencing and comparative genomic analysis of pK29, a 269-kilobase
RT conjugative plasmid encoding CMY-8 and CTX-M-3 beta-lactamases in
RT Klebsiella pneumoniae.";
RL Antimicrob. Agents Chemother. 51:3004-3007(2007).
RN [2] {ECO:0000313|EMBL:ABQ02970.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NK29 {ECO:0000313|EMBL:ABQ02970.1};
RC PLASMID=pK29 {ECO:0000313|EMBL:ABQ02970.1};
RA Chen Y.-T., Wu K.-M., Liao T.-L., Shiau Y.-R., Yan J.-J., Su I.-J.,
RA Lauderdale T.-L., Tsai S.-F.;
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Quinone oxidoreductase subfamily.
CC {ECO:0000256|RuleBase:RU364000}.
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DR EMBL; EF382672; ABQ02970.1; -; Genomic_DNA.
DR RefSeq; YP_001965913.1; NC_010870.1.
DR AlphaFoldDB; A7KGA3; -.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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; IPR013149; ADH-like_C.
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; 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.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:ABQ02970.1};
KW Metal-binding {ECO:0000256|RuleBase:RU364000};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU364000}; Plasmid {ECO:0000313|EMBL:ABQ02970.1};
KW Zinc {ECO:0000256|RuleBase:RU364000}.
FT DOMAIN 2..304
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 305 AA; 33000 MW; 6870D650D238477E CRC64;
MSLPHPSMPK GRDLLIRVRA VAVNPRDLKS RRNISPSAGN PVVMGYDASG VVEATGPEMT
LFRPGDHVFY AGVLDRQGAN AEFQLVDERI TGIKPAALSF EAAASVPLTG LTAWEMLFDR
LQLSVNGDAD QTLLMLGGAG GVPCMAIQLA RTLSRVNIIG TASRQESVRA VRGFGAHYVL
DHSCALAPQV ASLAGLPPIT RIFSTYTTPS AWENMAEIIA PQGRIGLIDD PEPLDLRLIK
FKSVSVHWEA MFTRPMHATA DMSKQHDILN KLSCMLDSGK LKPPLLAEYG RLNAKALRRA
HEGLC
//