ID Q9CEN0_LACLA Unreviewed; 340 AA.
AC Q9CEN0;
DT 01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2001, sequence version 1.
DT 27-MAR-2024, entry version 128.
DE RecName: Full=Alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00016352};
DE EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
GN Name=adhA {ECO:0000313|EMBL:AAK05905.1};
GN ORFNames=L55758 {ECO:0000313|EMBL:AAK05905.1};
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623 {ECO:0000313|EMBL:AAK05905.1, ECO:0000313|Proteomes:UP000002196};
RN [1] {ECO:0000313|EMBL:AAK05905.1, ECO:0000313|Proteomes:UP000002196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403 {ECO:0000313|EMBL:AAK05905.1,
RC ECO:0000313|Proteomes:UP000002196};
RX PubMed=11337471; DOI=10.1101/gr.GR-1697R;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH;
CC Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001146};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a secondary alcohol + NAD(+) = a ketone + H(+) + NADH;
CC Xref=Rhea:RHEA:10740, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087,
CC ChEBI:CHEBI:35681, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000781};
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; AE005176; AAK05905.1; -; Genomic_DNA.
DR PIR; G86850; G86850.
DR RefSeq; NP_267964.1; NC_002662.1.
DR RefSeq; WP_003130326.1; NC_002662.1.
DR AlphaFoldDB; Q9CEN0; -.
DR PaxDb; 272623-L55758; -.
DR EnsemblBacteria; AAK05905; AAK05905; L55758.
DR KEGG; lla:L55758; -.
DR PATRIC; fig|272623.7.peg.1937; -.
DR eggNOG; COG1064; Bacteria.
DR HOGENOM; CLU_026673_20_1_9; -.
DR OrthoDB; 9806940at2; -.
DR BRENDA; 1.1.1.1; 2864.
DR Proteomes; UP000002196; Chromosome.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08297; CAD3; 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; PTHR42940; ALCOHOL DEHYDROGENASE 1-RELATED; 1.
DR PANTHER; PTHR42940:SF8; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 11; 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 ECO:0000313|EMBL:AAK05905.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002196};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 14..336
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 340 AA; 35778 MW; 9235A285FACAB624 CRC64;
MKAAVVRHNP DGYADLVEKE LRAIKPNEAL LDMEYCGVCH TDLHVAAGDY GNKAGTVLGH
EGIGIVKEIG TDVSSLQVGD RVSVAWFFEG CGHCEYCVSG NETFCREVKN AGYSVDGGMA
EEAIVVADYA VKVPDGLDPI EASSITCAGV TTYKAIKVSG VKPGDWQVIF GAGGLGNLAI
QYAKNVFGAK VIAVDINQDK LNLAKKIGAD VIINSGDVNP VDEIKKITGG LGAQSAIVCA
VARIAFEQAV ASLKPMGKMV AVALPNTEMT LSVPTVVFDG VEVAGSLVGT RLDLAEAFQF
GAEGKVKPIV ATRKLEEIND IIDEMKAGKI EGRMVIDFTK
//
