Reviewed, UniProtKB/Swiss-Prot P20369 (ADH1_KLULA)

Names and origin

Protein names

Recommended name:
    Alcohol dehydrogenase 1
    EC=1.1.1.1
Alternative name(s):
    Alcohol dehydrogenase I

Gene names

Name:	ADH1
Ordered Locus Names:	KLLA0F21010g

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	350 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.
Subunit structure	Homotetramer.
Subcellular location	Cytoplasm.
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 – 350	350	Alcohol dehydrogenase 1		PRO_0000160722
Regions
	Nucleotide binding	180 – 186	7	NAD By similarity
	Nucleotide binding	271 – 273	3	NAD By similarity
Sites
	Metal binding	46	1	Zinc 1; catalytic
	Metal binding	69	1	Zinc 1; catalytic
	Metal binding	100	1	Zinc 2
	Metal binding	103	1	Zinc 2
	Metal binding	106	1	Zinc 2
	Metal binding	114	1	Zinc 2
	Metal binding	156	1	Zinc 1; catalytic
	Binding site	204	1	NAD By similarity
	Binding site	209	1	NAD By similarity
	Binding site	343	1	NAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	P20369-1 [UniParc]. Last modified February 1, 1991. Version 1. Checksum: 3D71BE2D5CC86119	FASTA	350	37,261
	10 20 30 40 50 60 MAASIPETQK GVIFYENGGE LQYKDIPVPK PKANELLINV KYSGVCHTDL HAWKGDWPLP 70 80 90 100 110 120 TKLPLVGGHE GAGVVVAMGE NVKGWKIGDF AGIKWLNGSC MSCEYCELSN ESNCPEADLS 130 140 150 160 170 180 GYTHDGSFQQ YATADAVQAA KIPVGTDLAE VAPVLCAGVT VYKALKSANL KAGDWVAISG 190 200 210 220 230 240 AAGGLGSLAV QYAKAMGYRV LGIDAGEEKA KLFKDLGGEY FIDFTKSKNI PEEVIEATKG 250 260 270 280 290 300 GAHGVINVSV SEFAIEQSTN YVRSNGTVVL VGLPRDAKCK SDVFNQVVKS ISIVGSYVGN 310 320 330 340 350 RADTREAIDF FSRGLVKAPI HVVGLSELPS IYEKMEKGAI VGRYVVDTSK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The alcohol dehydrogenase system in the yeast, Kluyveromyces lactis." Saliola M., Shuster J.R., Falcone C. Yeast 6:193-204(1990) [PubMed: 2190430] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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	CR382126 Genomic DNA. Translation: CAG98731.1.
PIR	S09475.
RefSeq	XP_456023.1.
3D structure databases
HSSP	HSSP built from PDB template 1JVB based on UniProtKB P39462.
SMR	P20369. Positions 4-350.
ModBase	Search...
Genome annotation databases
GeneID	2895056.
KEGG	kla:KLLA0F21010g.
Phylogenomic databases
HOGENOM	P20369.
OMA	P20369. ATDGGPH.
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

ADH1_KLULA

Accession

Primary (citable) accession number: P20369

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 1, 1991
Last modified:	June 16, 2009
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)