ID B1MWN0_LEUCK Unreviewed; 900 AA.
AC B1MWN0;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=Aldehyde-alcohol dehydrogenase {ECO:0000256|PIRNR:PIRNR000111};
GN Name=adhE {ECO:0000313|EMBL:ACA81952.1};
GN OrderedLocusNames=LCK_00119 {ECO:0000313|EMBL:ACA81952.1};
OS Leuconostoc citreum (strain KM20).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Leuconostoc.
OX NCBI_TaxID=349519 {ECO:0000313|EMBL:ACA81952.1, ECO:0000313|Proteomes:UP000002166};
RN [1] {ECO:0000313|EMBL:ACA81952.1, ECO:0000313|Proteomes:UP000002166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KM20 {ECO:0000313|EMBL:ACA81952.1,
RC ECO:0000313|Proteomes:UP000002166};
RX PubMed=18281406; DOI=10.1128/JB.01862-07;
RA Kim J.F., Jeong H., Lee J.-S., Choi S.-H., Ha M., Hur C.-G., Kim J.-S.,
RA Lee S., Park H.-S., Park Y.-H., Oh T.K.;
RT "Complete genome sequence of Leuconostoc citreum KM20.";
RL J. Bacteriol. 190:3093-3094(2008).
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
CC -!- SIMILARITY: In the C-terminal section; belongs to the iron-containing
CC alcohol dehydrogenase family. {ECO:0000256|ARBA:ARBA00035645,
CC ECO:0000256|PIRNR:PIRNR000111}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the aldehyde
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00035641,
CC ECO:0000256|PIRNR:PIRNR000111}.
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DR EMBL; DQ489736; ACA81952.1; -; Genomic_DNA.
DR RefSeq; WP_004908583.1; NC_010471.1.
DR AlphaFoldDB; B1MWN0; -.
DR STRING; 349519.LCK_00119; -.
DR KEGG; lci:LCK_00119; -.
DR eggNOG; COG1012; Bacteria.
DR eggNOG; COG1454; Bacteria.
DR HOGENOM; CLU_007207_1_0_9; -.
DR OrthoDB; 9815791at2; -.
DR Proteomes; UP000002166; Chromosome.
DR GO; GO:0008774; F:acetaldehyde dehydrogenase (acetylating) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006066; P:alcohol metabolic process; IEA:InterPro.
DR GO; GO:0015976; P:carbon utilization; IEA:InterPro.
DR CDD; cd08178; AAD_C; 1.
DR CDD; cd07122; ALDH_F20_ACDH; 1.
DR Gene3D; 3.40.50.1970; -; 1.
DR Gene3D; 1.20.1090.10; Dehydroquinate synthase-like - alpha domain; 1.
DR InterPro; IPR034789; AAD_C.
DR InterPro; IPR001670; ADH_Fe/GldA.
DR InterPro; IPR018211; ADH_Fe_CS.
DR InterPro; IPR039697; Alcohol_dehydrogenase_Fe.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR012079; Bifunc_Ald-ADH.
DR PANTHER; PTHR11496; ALCOHOL DEHYDROGENASE; 1.
DR PANTHER; PTHR11496:SF83; HYDROXYACID-OXOACID TRANSHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF00171; Aldedh; 1.
DR Pfam; PF00465; Fe-ADH; 1.
DR PIRSF; PIRSF000111; ALDH_ADH; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR SUPFAM; SSF56796; Dehydroquinate synthase-like; 1.
DR PROSITE; PS00913; ADH_IRON_1; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000111}.
FT DOMAIN 18..290
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT DOMAIN 481..892
FT /note="Alcohol dehydrogenase iron-type/glycerol
FT dehydrogenase GldA"
FT /evidence="ECO:0000259|Pfam:PF00465"
SQ SEQUENCE 900 AA; 98015 MW; 82AA3CC7797A5D77 CRC64;
MVEATTKKPV KKVLTPEEKA VLQTQAEKMT AELVEKSQKA LAEFSTFTQE QVDKIVAAMA
LAGSENSLLL AHEAHDETGR GVVEDKDTKN RFASESVYNA IKYDKTVGVI NEDKIQGKVE
LAAPLGVLAG IVPTTNPTST TIFKSMLTAK TRNTIIFAFH PQAQKSSSHA AQIVYEAALK
AGAPENFIQW IEKPSIYGTS ALIQNTGIAS ILATGGPSMV NAALKSGNPS MGVGAGNGAV
YIDGTVDTDR AVSDLLLSKR FDNGMICATE NSAVIQASVY DDVLQKLQDQ GAYLVPKKDY
KKIADYVFKP NAEGFGVAGP VAGMSGRWIA EQAGVKIPEG KDVLLFELDQ KNIGEALSSE
KLSPLLSIYK VTERQEAIDT VQALLNYQGA GHNAAIQIGS QDDPFIKSYA DAIGASRILV
NQPDSIGGVG DIYTDAMRPS LTLGTGSWGK NSLSHNLSTY DLLNIKTVAR RRNRPQWIRL
PKEVYYEANA ITYLQDLPSV KRAFIVADPG MVEFGFVGKV LSQLELRQEQ VETNIYGSVK
PDPTLSQAVD IARQMADFKP DTVILLGGGS ALDAGKIGRF LYEYSTRHEG ILSDEEGIKE
LFMELQQKFM DIRKRIVKFY HARLTQMVAI PTTSGTGSEV TPFAVITDDH THVKYPLADY
ELTPEVAIVD PEFVMTVPKR TVAFSGLDAL SHAFESYVSV MASEFTRPWA LQAIKLIFEN
LTTSYKYDPK QPTKEGQNAR TKMHYASTLA GMSFANAFLG INHSLAHKTG GEFGLPHGLA
IAIAMPHVIK FNAVTGNVKR TPYPRYETYT AQKDYADIAR YLGLQGTTDA ELVDALIVAI
KALAKSVEVD QTLSGNGVKK ADLEKNIDQL TDLVYNDQCT PGNPRQPSLA EIKQLLMDQL
//
