ADH4_KLULA
ID ADH4_KLULA Reviewed; 375 AA.
AC P49385; Q6CK50;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Alcohol dehydrogenase 4, mitochondrial;
DE EC=1.1.1.1;
DE AltName: Full=Alcohol dehydrogenase IV;
DE Flags: Precursor;
GN Name=ADH4; OrderedLocusNames=KLLA0F13530g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1872030; DOI=10.1002/yea.320070409;
RA Saliola M., Gonnella R., Mazzoni C., Falcone C.;
RT "Two genes encoding putative mitochondrial alcohol dehydrogenases are
RT present in the yeast Kluyveromyces lactis.";
RL Yeast 7:391-400(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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 -!- 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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; X62767; CAA44614.1; -; Genomic_DNA.
DR EMBL; CR382126; CAG98397.1; -; Genomic_DNA.
DR PIR; S17253; S17253.
DR RefSeq; XP_455689.1; XM_455689.1.
DR AlphaFoldDB; P49385; -.
DR SMR; P49385; -.
DR STRING; 28985.XP_455689.1; -.
DR EnsemblFungi; CAG98397; CAG98397; KLLA0_F13530g.
DR GeneID; 2894943; -.
DR KEGG; kla:KLLA0_F13530g; -.
DR eggNOG; KOG0023; Eukaryota.
DR HOGENOM; CLU_026673_20_1_1; -.
DR InParanoid; P49385; -.
DR OMA; GLKMTDT; -.
DR Proteomes; UP000000598; Chromosome F.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000947; P:amino acid catabolic process to alcohol via Ehrlich pathway; IEA:EnsemblFungi.
DR GO; GO:0006116; P:NADH oxidation; IEA:EnsemblFungi.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_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 Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 3: Inferred from homology;
KW Metal-binding; Mitochondrion; NAD; Oxidoreductase; Reference proteome;
KW Transit peptide; Zinc.
FT TRANSIT 1..27
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 28..375
FT /note="Alcohol dehydrogenase 4, mitochondrial"
FT /id="PRO_0000000878"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 205..211
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 234
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 296..298
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 368
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT CONFLICT 157
FT /note="A -> R (in Ref. 1; CAA44614)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="A -> R (in Ref. 1; CAA44614)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="I -> V (in Ref. 1; CAA44614)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="V -> L (in Ref. 1; CAA44614)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="V -> L (in Ref. 1; CAA44614)"
FT /evidence="ECO:0000305"
FT CONFLICT 335
FT /note="F -> L (in Ref. 1; CAA44614)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="E -> A (in Ref. 1; CAA44614)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 375 AA; 40163 MW; 14E66B615564F756 CRC64;
MFRLARAQTA LANKASVSRS FLRLNSSFAI PETQKGVIFY ENGGKLEYKD LPVPKPKANE
ILINVKYSGV CHTDLHAWKG DWPLPVKLPL VGGHEGAGIV VAKGENVKNF EIGDYAGIKW
LNGSCMSCEL CEQGYESNCL QADLSGYTHD GSFQQYATAD AVQAAQIPKG TDLAEIAPIL
CAGVTVYKAL KTADLKPGQW VAISGAAGGL GSLAVQYAKA MGLRVLGIDG GDGKEELFKQ
CGGEVFIDFR KSKDMVADIQ EATNGGPHGV INVSVSEAAI SMSTEYVRPT GVVVLVGLPA
DAYVKSEVFS HVVKSISIKG SYVGNRADTR EATDFFTRGL VKSPIKIIGL SELPEAYELM
EQGKILGRFV VDTYK
