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Alcohol dehydrogenase 4, mitochondrial (EC 1.1.1.1) (Alcohol dehydrogenase IV)

 ADH4_KLULA              Reviewed;         375 AA.
P49385; Q6CK50;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
31-AUG-2004, sequence version 2.
22-NOV-2017, entry version 116.
RecName: Full=Alcohol dehydrogenase 4, mitochondrial;
EC=1.1.1.1;
AltName: Full=Alcohol dehydrogenase IV;
Flags: Precursor;
Name=ADH4; OrderedLocusNames=KLLA0F13530g;
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC
1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
NCBI_TaxID=284590;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1872030; DOI=10.1002/yea.320070409;
Saliola M., Gonnella R., Mazzoni C., Falcone C.;
"Two genes encoding putative mitochondrial alcohol dehydrogenases are
present in the yeast Kluyveromyces lactis.";
Yeast 7:391-400(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 /
WM37;
PubMed=15229592; DOI=10.1038/nature02579;
Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
Wincker P., Souciet J.-L.;
"Genome evolution in yeasts.";
Nature 430:35-44(2004).
-!- CATALYTIC ACTIVITY: A primary alcohol + NAD(+) = an aldehyde +
NADH.
-!- CATALYTIC ACTIVITY: A secondary alcohol + NAD(+) = a ketone +
NADH.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
-!- SUBUNIT: Homotetramer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Mitochondrion matrix.
-!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
family. {ECO:0000305}.
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EMBL; X62767; CAA44614.1; -; Genomic_DNA.
EMBL; CR382126; CAG98397.1; -; Genomic_DNA.
PIR; S17253; S17253.
RefSeq; XP_455689.1; XM_455689.1.
ProteinModelPortal; P49385; -.
SMR; P49385; -.
STRING; 284590.XP_455689.1; -.
PRIDE; P49385; -.
EnsemblFungi; CAG98397; CAG98397; KLLA0_F13530g.
GeneID; 2894943; -.
KEGG; kla:KLLA0F13530g; -.
eggNOG; KOG0023; Eukaryota.
eggNOG; COG1064; LUCA.
HOGENOM; HOG000294685; -.
InParanoid; P49385; -.
KO; K13953; -.
OMA; RKGAFPH; -.
OrthoDB; EOG092C2Q8E; -.
Proteomes; UP000000598; Chromosome F.
GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
GO; GO:0004022; F:alcohol dehydrogenase (NAD) activity; IEA:UniProtKB-EC.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
InterPro; IPR013149; ADH_C.
InterPro; IPR013154; ADH_N.
InterPro; IPR002328; ADH_Zn_CS.
InterPro; IPR011032; GroES-like_sf.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR020843; PKS_ER.
Pfam; PF08240; ADH_N; 1.
Pfam; PF00107; ADH_zinc_N; 1.
SMART; SM00829; PKS_ER; 1.
SUPFAM; SSF50129; SSF50129; 1.
SUPFAM; SSF51735; SSF51735; 1.
PROSITE; PS00059; ADH_ZINC; 1.
3: Inferred from homology;
Complete proteome; Metal-binding; Mitochondrion; NAD; Oxidoreductase;
Reference proteome; Transit peptide; Zinc.
TRANSIT 1 27 Mitochondrion. {ECO:0000255}.
CHAIN 28 375 Alcohol dehydrogenase 4, mitochondrial.
/FTId=PRO_0000000878.
NP_BIND 205 211 NAD. {ECO:0000250}.
NP_BIND 296 298 NAD. {ECO:0000250}.
METAL 71 71 Zinc 1; catalytic. {ECO:0000250}.
METAL 94 94 Zinc 1; catalytic. {ECO:0000250}.
METAL 125 125 Zinc 2. {ECO:0000250}.
METAL 128 128 Zinc 2. {ECO:0000250}.
METAL 131 131 Zinc 2. {ECO:0000250}.
METAL 139 139 Zinc 2. {ECO:0000250}.
METAL 181 181 Zinc 1; catalytic. {ECO:0000250}.
BINDING 229 229 NAD. {ECO:0000250}.
BINDING 234 234 NAD. {ECO:0000250}.
BINDING 368 368 NAD. {ECO:0000250}.
CONFLICT 157 157 A -> R (in Ref. 1; CAA44614).
{ECO:0000305}.
CONFLICT 218 218 A -> R (in Ref. 1; CAA44614).
{ECO:0000305}.
CONFLICT 280 280 I -> V (in Ref. 1; CAA44614).
{ECO:0000305}.
CONFLICT 287 287 V -> L (in Ref. 1; CAA44614).
{ECO:0000305}.
CONFLICT 292 292 V -> L (in Ref. 1; CAA44614).
{ECO:0000305}.
CONFLICT 335 335 F -> L (in Ref. 1; CAA44614).
{ECO:0000305}.
CONFLICT 358 358 E -> A (in Ref. 1; CAA44614).
{ECO:0000305}.
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


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