Q6CM42 (ADE_KLULA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Adenine deaminase
Short name=ADE
EC=3.5.4.2

Alternative name(s):
Adenine aminohydrolase
Short name=AAH

Gene names

Name:	AAH1
Ordered Locus Names:	KLLA0E23254g

Organism

Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica) [Complete proteome]

Taxonomic identifier

284590 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	355 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the hydrolytic deamination of adenine to hypoxanthine. Plays an important role in the purine salvage pathway and in nitrogen catabolism By similarity.
Catalytic activity	Adenine + H2O = hypoxanthine + NH3.
Cofactor	Binds 1 zinc ion per subunit By similarity.
Subcellular location	Cytoplasm By similarity. Nucleus By similarity.
Sequence similarities	Belongs to the adenosine and AMP deaminases family. Adenine deaminase type 2 subfamily.

Ontologies

Keywords
Biological process	Nucleotide metabolism
Cellular component	Cytoplasm Nucleus
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	purine ribonucleoside monophosphate biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	adenine deaminase activity Inferred from electronic annotation. Source: EC metal 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 – 355	355	Adenine deaminase		PRO_0000256236
Sites
	Active site	214	1	Proton donor By similarity
	Metal binding	23	1	Zinc; catalytic By similarity
	Metal binding	25	1	Zinc; catalytic By similarity
	Metal binding	211	1	Zinc; catalytic By similarity
	Metal binding	292	1	Zinc; catalytic By similarity
	Binding site	293	1	Substrate By similarity
	Site	235	1	Important for catalytic activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6CM42 [UniParc]. Last modified August 16, 2004. Version 1. Checksum: C7AB5F79AE851F42	FASTA	355	40,428
	10 20 30 40 50 60 MAKFECTDEV TNFLTELPKC EHHLHLEGTL EPELLFQLVE RNGVQLPGTF PKTVNELHVI 70 80 90 100 110 120 YNNFADLQDF LNYYYIGCNV LLSEDDFFEL AWSYFKRVST QGLRHAEVFY DPQSHTSRGI 130 140 150 160 170 180 SLEVVTKGFE RACAKAQEEF NISTKLIMCL LRHCPVEECM DTVKSAKSLI ESGVIDGLGL 190 200 210 220 230 240 DSSERPFPPE LFVECYQLAK SYNKELQLTA HAGEEGDPSF VTNTLDLLET TRIDHGVRSI 250 260 270 280 290 300 EDAELIKRLA AQKVMLTLCP LSNVKLQVVK DVSELPLQEF LDNDVPFSIN SDDPAYFGGY 310 320 330 340 350 ILQNYLEVYS RFGWSKAVWA KIARQSIEGS WCDPKRKQEL LSEVSEVVNK YVNLP

References

[1]

"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 / NBRC 1267 / NRRL Y-1140 / WM37.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR382125 Genomic DNA. Translation: CAH00084.1.
RefSeq	XP_454997.1. XM_454997.1.
3D structure databases
ProteinModelPortal	Q6CM42.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6CM42.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2894386.
GenomeReviews	Gene locus KLLA0E23254g in contig CR382125_GR.
KEGG	kla:KLLA0E23167g.
Phylogenomic databases
eggNOG	fuNOG04795.
HOGENOM	HBG630382.
OMA	EGIMLTV.
OrthoDB	EOG4P5PJR.
Family and domain databases
InterPro	IPR006650. A/AMP_deam_AS. IPR001365. A/AMP_deaminase_dom. IPR006330. A_deaminase. [Graphical view]
KO	K01488.
PANTHER	PTHR11409:SF21. PTHR11409:SF21. 1 hit.
Pfam	PF00962. A_deaminase. 1 hit. [Graphical view]
TIGRFAMs	TIGR01430. Aden_deam. 1 hit.
PROSITE	PS00485. A_DEAMINASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ADE_KLULA

Accession

Primary (citable) accession number: Q6CM42

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	August 16, 2004
Last modified:	December 14, 2011
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program