ID   Q5ZXW9_LEGPH            Unreviewed;       348 AA.
AC   Q5ZXW9;
DT   23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT   23-NOV-2004, sequence version 1.
DT   27-MAR-2024, entry version 117.
DE   SubName: Full=Alcohol dehydrogenase (NADP-dependent, zinc-type) {ECO:0000313|EMBL:AAU26701.1};
DE            EC=1.1.1.2 {ECO:0000313|EMBL:AAU26701.1};
GN   OrderedLocusNames=lpg0612 {ECO:0000313|EMBL:AAU26701.1};
OS   Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS   33152 / DSM 7513).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=272624 {ECO:0000313|EMBL:AAU26701.1, ECO:0000313|Proteomes:UP000000609};
RN   [1] {ECO:0000313|EMBL:AAU26701.1, ECO:0000313|Proteomes:UP000000609}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513
RC   {ECO:0000313|Proteomes:UP000000609};
RX   PubMed=15448271; DOI=10.1126/science.1099776;
RA   Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA   Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA   Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA   Chou I.C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA   Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA   Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA   Russo J.J.;
RT   "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL   Science 305:1966-1968(2004).
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}.
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DR   EMBL; AE017354; AAU26701.1; -; Genomic_DNA.
DR   RefSeq; WP_010946349.1; NC_002942.5.
DR   RefSeq; YP_094648.1; NC_002942.5.
DR   AlphaFoldDB; Q5ZXW9; -.
DR   STRING; 272624.lpg0612; -.
DR   PaxDb; 272624-lpg0612; -.
DR   GeneID; 66489801; -.
DR   KEGG; lpn:lpg0612; -.
DR   PATRIC; fig|272624.6.peg.629; -.
DR   eggNOG; COG1064; Bacteria.
DR   HOGENOM; CLU_026673_20_2_6; -.
DR   OrthoDB; 9771084at2; -.
DR   Proteomes; UP000000609; Chromosome.
DR   GO; GO:0008106; F:alcohol dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd05283; CAD1; 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; IPR047109; CAD-like.
DR   InterPro; IPR029752; D-isomer_DH_CS1.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   PANTHER; PTHR42683; ALDEHYDE REDUCTASE; 1.
DR   PANTHER; PTHR42683:SF85; CINNAMYL ALCOHOL DEHYDROGENASE 6-RELATED; 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.
DR   PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:AAU26701.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000609};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          13..342
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   348 AA;  37930 MW;  E45A6F3E604A256E CRC64;
     MSETIGYAAH KAGAPLKPFT FERRPVGAHD VAIDILFCGI CHSDLHQVNN DWAGAFYPMV
     PGHEIIGRVK EVGHQVRRFK AGDLVGVGCM VDSCRQCTYC HQHEEQYCKS GATFTYNSQD
     NHLGGVTYGG YSKHIVVTED FVLKIDESLD PAAAAPLLCA GITTYSPLKR AKVGKMSKVG
     IVGLGGLGHM AVKLARAMGA YVTVFTTSIN KIKAGKDLGA HDVVLSTDNN VMQTLANQYD
     FILDTVSAKH DLGQYLNLLK VDGQLTQVGL PSDPLEVTMF PVILKRLSIN GSLIGGIKET
     QEVLDFCARH GITADIELIK MHEVNSAYER LLKGDVKYRF VIDMSTLD
//