ID B0SQW1_LEPBP Unreviewed; 346 AA.
AC B0SQW1;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE SubName: Full=Putative zinc-binding alcohol dehydrogenase {ECO:0000313|EMBL:ABZ99358.1};
DE EC=1.1.1.- {ECO:0000313|EMBL:ABZ99358.1};
GN OrderedLocusNames=LEPBI_I3293 {ECO:0000313|EMBL:ABZ99358.1};
OS Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris).
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=456481 {ECO:0000313|EMBL:ABZ99358.1, ECO:0000313|Proteomes:UP000001847};
RN [1] {ECO:0000313|EMBL:ABZ99358.1, ECO:0000313|Proteomes:UP000001847}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Patoc 1 / ATCC 23582 / Paris
RC {ECO:0000313|Proteomes:UP000001847};
RX PubMed=18270594; DOI=10.1371/journal.pone.0001607;
RA Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N.,
RA Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A.,
RA Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L.,
RA Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.;
RT "Genome sequence of the saprophyte Leptospira biflexa provides insights
RT into the evolution of Leptospira and the pathogenesis of leptospirosis.";
RL PLoS ONE 3:E1607-E1607(2008).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={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; CP000786; ABZ99358.1; -; Genomic_DNA.
DR RefSeq; WP_012390214.1; NC_010602.1.
DR AlphaFoldDB; B0SQW1; -.
DR STRING; 456481.LEPBI_I3293; -.
DR KEGG; lbi:LEPBI_I3293; -.
DR HOGENOM; CLU_026673_11_2_12; -.
DR OrthoDB; 9769198at2; -.
DR BioCyc; LBIF456481:LEPBI_RS16130-MONOMER; -.
DR Proteomes; UP000001847; Chromosome I.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR CDD; cd08254; hydroxyacyl_CoA_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; PTHR43401; L-THREONINE 3-DEHYDROGENASE; 1.
DR PANTHER; PTHR43401:SF2; L-THREONINE 3-DEHYDROGENASE; 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|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ABZ99358.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001847};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 9..329
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 346 AA; 37406 MW; 65976CDF0D5BE200 CRC64;
MKAAVLPSGS RSLEIQELDL PPLPPNQVKV KVKACGICGS DIHFILHGKM KATYSPCVPG
HETSGVVAEI GDQVTKFKLG DRVVVSAGTS CGKCKHCLAG RENLCENIGV IGFNQRGGFA
EFIQTEERYL HLLPEEIPFA EGAILADAVS TPYHAIKYQG ELKAGESVAI IGCGGLGIHA
VAIAKALGAA KIYAIDIDSG SLENAKAYGA DELILVEKNM QVGKVLKEKS GGIDLLCDFT
GYMPNIESSV RAMNRGGRIV LVGIGRNKLE IPMPFFLIER QIRITGSYGS DRRAIPELIQ
LYQEKKLNLT KSISGIHKLE DTNEFLHALE EKKGNPIRFI INPELS
//
