ID   V6HVM4_9LEPT            Unreviewed;       352 AA.
AC   V6HVM4;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Alcohol dehydrogenase, catalytic domain, GroES-like family {ECO:0000313|EMBL:EQA36909.1};
GN   ORFNames=LEP1GSC047_2814 {ECO:0000313|EMBL:EQA36909.1};
OS   Leptospira inadai serovar Lyme str. 10.
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=1049790 {ECO:0000313|EMBL:EQA36909.1, ECO:0000313|Proteomes:UP000018719};
RN   [1] {ECO:0000313|EMBL:EQA36909.1, ECO:0000313|Proteomes:UP000018719}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=10 {ECO:0000313|EMBL:EQA36909.1,
RC   ECO:0000313|Proteomes:UP000018719};
RA   Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA   Sanka R., DePew J., Purushe J., Hartskeerl R.A., Ahmed A.,
RA   van der Linden H., Goris M.G.A., Vinetz J.M., Sutton G.G., Nierman W.C.,
RA   Fouts D.E.;
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EQA36909.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AHMM02000017; EQA36909.1; -; Genomic_DNA.
DR   RefSeq; WP_010418109.1; NZ_AHMM02000017.1.
DR   AlphaFoldDB; V6HVM4; -.
DR   STRING; 1049790.LEP1GSC047_2814; -.
DR   Proteomes; UP000018719; Unassembled WGS sequence.
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; cd08240; 6_hydroxyhexanoate_dh_like; 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   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          10..348
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   352 AA;  37446 MW;  A86110DF6BC8755F CRC64;
     MKRVQLIDFG KPLVLNIAPD PIPEDNEVLL EVLACGVCHS DLHIREGYYE LGSGKKMWVK
     DRGVSLPLTP GHEVVGRILK IGSKVAGVFV GELFLVYPWI GCDVCSECQA DLPHLCASPK
     SLGVYQDGGY SDRILVPDKK WLIPIGNLKP EVACSYACAG LTAFSALKKA LPLSEKETLV
     IIGAGGLGFF AAQIVRCLTN ANIIFLDVDS DRLKKIGEFD SSFHTILSSA GEAEIRKSIG
     ASGAKSIVDF VNNSETAALA FSLLSKNGKQ ICVGLFGGEV TLQTPIIALK NLKIQGSYTG
     SPSELTELLS LVSNNRLLPV PIHLASLNDA NSILDSMAGG KGVGRTVLIP TS
//