Reviewed, UniProtKB/Swiss-Prot P49383 (ADH2_KLULA)

Names and origin

Protein names

Recommended name:
    Alcohol dehydrogenase 2
    EC=1.1.1.1
Alternative name(s):
    Alcohol dehydrogenase II

Gene names

Name:	ADH2
Ordered Locus Names:	KLLA0F18260g

Organism

Kluyveromyces lactis (Yeast) (Candida sphaerica) [Complete proteome]

Taxonomic identifier

28985 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Kluyveromyces

Protein attributes

Sequence length	348 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	An alcohol + NAD+ = an aldehyde or ketone + NADH.
Cofactor	Binds 2 zinc ions per subunit By similarity.
Subunit structure	Homotetramer By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the zinc-containing alcohol dehydrogenase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Metal-binding NAD Zinc
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	alcohol dehydrogenase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 348	348	Alcohol dehydrogenase 2		PRO_0000160723
Regions
	Nucleotide binding	178 – 184	7	NAD By similarity
	Nucleotide binding	269 – 271	3	NAD By similarity
Sites
	Metal binding	44	1	Zinc 1; catalytic By similarity
	Metal binding	67	1	Zinc 1; catalytic By similarity
	Metal binding	98	1	Zinc 2 By similarity
	Metal binding	101	1	Zinc 2 By similarity
	Metal binding	104	1	Zinc 2 By similarity
	Metal binding	112	1	Zinc 2 By similarity
	Metal binding	154	1	Zinc 1; catalytic By similarity
	Binding site	202	1	NAD By similarity
	Binding site	207	1	NAD By similarity
	Binding site	341	1	NAD By similarity
Experimental info
	Sequence conflict	84	1	N → I in CAA45739. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P49383-1 [UniParc]. Last modified August 31, 2004. Version 2. Checksum: F21D3DE1F6FB389C	FASTA	348	37,098
	10 20 30 40 50 60 MSIPETQKGV IFYENGGELQ YKDIPVPKPK ANELLINVKY SGVCHTDLHA WKGDWPLPTK 70 80 90 100 110 120 LPLVGGHEGA GVVVAMGENV KGWNIGDFAG IKWLNGSCMS CEYCELSNES NCPDADLSGY 130 140 150 160 170 180 THDGSFQQYA TADAVQAARI PKGTDLAEVA PILCAGVTVY KALKSADLKA GDWVAISGAC 190 200 210 220 230 240 GGLGSLAIQY AKAMGYRVLG IDTGAEKAKL FKELGGEYFV DYAVSKDLIK EIVDATNGGA 250 260 270 280 290 300 HGVINVSVSE FAIEQSTNYV RSNGTVVLVG LPRDAKCKSD VFTQVVKSVS IVGSYVGNRA 310 320 330 340 DTREALDFFA RGLVHAPIKI VGLSELADVY DKMVKGEIVG RYVVDTSK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Evolution of the alcohol dehydrogenase (ADH) genes in yeast: characterization of a fourth ADH in Kluyveromyces lactis." Shain D.H., Salvadore C., Denis C.L. Mol. Gen. Genet. 232:479-488(1992) [PubMed: 1588917] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NRRL Y-1140 / WM37.
[2]	"Genome evolution in yeasts." 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. Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NRRL Y-1140 / WM37.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X64397 Genomic DNA. Translation: CAA45739.1. CR382126 Genomic DNA. Translation: CAG98607.1.
PIR	S20911.
RefSeq	XP_455899.1.
3D structure databases
HSSP	HSSP built from PDB template 1JVB based on UniProtKB P39462.
SMR	P49383. Positions 2-348.
ModBase	Search...
Genome annotation databases
GeneID	2894942.
KEGG	kla:KLLA0F18260g.
Phylogenomic databases
HOGENOM	P49383.
OMA	P49383. HPLIGGH.
Enzyme and pathway databases
BRENDA	1.1.1.1. 74088.
Family and domain databases
InterPro	IPR013154. ADH_GroES-like. IPR002085. ADH_SF_Zn. IPR013149. ADH_Zn-bd. IPR002328. ADH_Zn_CS. [Graphical view]
PANTHER	PTHR11695. ADH_Sf_Zn. 1 hit.
Pfam	PF08240. ADH_N. 1 hit. PF00107. ADH_zinc_N. 1 hit. [Graphical view]
PROSITE	PS00059. ADH_ZINC. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ADH2_KLULA

Accession

Primary (citable) accession number: P49383
Secondary accession number(s): Q6CJJ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	August 31, 2004
Last modified:	June 16, 2009
This is version 60 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)