Q6FP78 (ADE_CANGA) 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:	CAGL0J05984g

Organism

Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata) [Complete proteome]

Taxonomic identifier

284593 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Nakaseomyces › mitosporic Nakaseomyces

Protein attributes

Sequence length	347 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 – 347	347	Adenine deaminase		PRO_0000256233
Sites
	Active site	207	1	Proton donor By similarity
	Metal binding	16	1	Zinc; catalytic By similarity
	Metal binding	18	1	Zinc; catalytic By similarity
	Metal binding	204	1	Zinc; catalytic By similarity
	Metal binding	285	1	Zinc; catalytic By similarity
	Binding site	286	1	Substrate By similarity
	Site	228	1	Important for catalytic activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6FP78 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: F48170A9E08B8C9F	FASTA	347	39,697
	10 20 30 40 50 60 MVPESFLLEL PKCEHHLHLE GTLEPDLLFP LAKRNNIQLP DHFPQTPEEL AVRYTQFKDL 70 80 90 100 110 120 QDFLDYYYIG TNVLLKEEDF FDLAWAYFTK VSKQGLVHAE LFYDPQSHTT RGVSLETVTR 130 140 150 160 170 180 GFERACKKAH EELGITSKLI MCLLRHLPPQ DCLQTIEEAE QLIKSGVIHG LGLDSAEKPF 190 200 210 220 230 240 PPSLFVECYE RAAKINPELR LTAHAGEEGT HQFVSDALDL LNVTRIDHGV NSKQSEELMA 250 260 270 280 290 300 RLAEQQTLLT VCPLSNVKLQ VVQSVKEIPL QLFLDKNIAF SLNSDDPAYF GGYILDNYYQ 310 320 330 340 VNKDFPDWDF KVWERIAKNG INGSWCEQKR KEELLAKVDA VVAKYTN

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 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR380956 Genomic DNA. Translation: CAG60917.1.
RefSeq	XP_447966.1. XM_447966.1.
3D structure databases
HSSP	HSSP built from PDB template 2AMX based on UniProtKB Q7RMV2.
ProteinModelPortal	Q6FP78.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2889775.
GenomeReviews	Gene locus CAGL0J05984g in contig CR380956_GR.
KEGG	cgr:CAGL0J05984g.
Phylogenomic databases
eggNOG	fuNOG04795.
HOGENOM	HBG630382.
OMA	CLLRHLP.
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_CANGA

Accession

Primary (citable) accession number: Q6FP78

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	July 19, 2004
Last modified:	December 14, 2011
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program