ID D3HPV5_LEGLN Unreviewed; 348 AA.
AC D3HPV5;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Putative oxidoreductase, Zn-dependent and NAD(P)-binding {ECO:0000313|EMBL:CBJ10919.1};
GN Name=yahK {ECO:0000313|EMBL:CBJ10919.1};
GN OrderedLocusNames=LLO_0585 {ECO:0000313|EMBL:CBJ10919.1};
OS Legionella longbeachae serogroup 1 (strain NSW150).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=661367 {ECO:0000313|EMBL:CBJ10919.1, ECO:0000313|Proteomes:UP000001060};
RN [1] {ECO:0000313|EMBL:CBJ10919.1, ECO:0000313|Proteomes:UP000001060}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NSW150 {ECO:0000313|EMBL:CBJ10919.1,
RC ECO:0000313|Proteomes:UP000001060};
RX PubMed=20174605; DOI=10.1371/journal.pgen.1000851;
RA Cazalet C., Gomez-Valero L., Rusniok C., Lomma M., Dervins-Ravault D.,
RA Newton H., Sansom F., Jarraud S., Zidane N., Ma L., Bouchier C.,
RA Etienne J., Hartland E., Buchrieser C.;
RT "Analysis of the Legionella longbeachae genome and transcriptome uncovers
RT unique strategies to cause Legionnaires' disease.";
RL PLoS Genet. 6:E1000851-E1000851(2010).
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; FN650140; CBJ10919.1; -; Genomic_DNA.
DR RefSeq; WP_003632934.1; NC_013861.1.
DR AlphaFoldDB; D3HPV5; -.
DR STRING; 661367.LLO_0585; -.
DR KEGG; llo:LLO_0585; -.
DR eggNOG; COG1064; Bacteria.
DR HOGENOM; CLU_026673_20_2_6; -.
DR OrthoDB; 9771084at2; -.
DR Proteomes; UP000001060; Chromosome.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
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; 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.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001060};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 8..342
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 348 AA; 38213 MW; 6C1934D68A8B131D CRC64;
MIPVKGYAAQ SAKAPLTPYS FNRREVGEHD VLIDIHYCGI CHSDIHLVRG EWGGSIFPMV
PGHEIIGLVS QTGSAVTQFK IGDRVGVGCF VDSCRQCDNC HEGFEQFCDK GMTLTYNSTE
PNGKNTTKGG YSTKIVVDEN YVLKIPSNLP LDAAAPLLCA GITLYSPLKH WQTGPGKRVG
ILGLGGLGHM GVKLAHAMGA EVSVLSHSLN KEADGIRMGA DHFFATSNPK TFEQLTNYFD
LIICTVSAKI DWNEYLKLLK RDGTMVVVGI PEEPALINSF SLIERRRNLA GSLIGGIKET
QEMLDFCGKH HIVSEIELIP MHQVNEAYER VLKSDVRYRF VIDMASLS
//
