Q4X1Q4 (ADE_ASPFU) 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
ORF Names:	AFUA_2G09150

Organism

Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)

Taxonomic identifier

330879 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	354 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 Reference 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 – 354	354	Adenine deaminase		PRO_0000256230
Sites
	Active site	214	1	Proton donor By similarity
	Metal binding	19	1	Zinc; catalytic By similarity
	Metal binding	21	1	Zinc; catalytic By similarity
	Metal binding	211	1	Zinc; catalytic By similarity
	Metal binding	291	1	Zinc; catalytic By similarity
	Binding site	292	1	Substrate By similarity
	Site	234	1	Important for catalytic activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q4X1Q4 [UniParc]. Last modified July 5, 2005. Version 1. Checksum: 591204D6B19AB461	FASTA	354	39,864
	10 20 30 40 50 60 MCQSPLHDFL HGLPKCEHHV HLEGCVTPEL IFQLAEKNNI QLPNPATHPA YASVEALRAR 70 80 90 100 110 120 YAEFTSLNDF LDFYFHGMSV LHHQSDFEEL AWAYFQKAHA DGVHHAEVFF DPQVHQARGI 130 140 150 160 170 180 DYETVVSGFT AGCKRAEREL GLSTRLILCF VRHLPVDSAT KLYELALASN HFESRVVHGL 190 200 210 220 230 240 GWSSSEVGPP KDMFREIYAS ASGKGIRLTA HAGEEGDPTY ISTALELGAR RIDHGIRLVE 250 260 270 280 290 300 DPELMERVAR EGIMLTVCPL SNVRLRCVQS VEQVPIRKFL DAGVKFSINS DDPAYFGGYI 310 320 330 340 350 LDNYCAVQEA FQLSILEWRV IAENSVNESW IDEARKAELL KRIDDHVQKH TVVA

References

[1]

"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus." Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W. Nature 438:1151-1156(2005) [PubMed: 16372009] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAHF01000001 Genomic DNA. Translation: EAL93211.1.
RefSeq	XP_755249.1. XM_750156.1.
3D structure databases
HSSP	HSSP built from PDB template 2AMX based on UniProtKB Q7RMV2.
ProteinModelPortal	Q4X1Q4.
ModBase	Search...
Protein-protein interaction databases
STRING	Q4X1Q4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADAFUAT00004029; CADAFUAP00004029; CADAFUAG00004029.
GeneID	3513729.
GenomeReviews	Gene locus aah1 in contig CM000170_GR.
KEGG	afm:AFUA_2G09150.
Phylogenomic databases
eggNOG	fuNOG04795.
GeneTree	EFGT00050000005551.
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_ASPFU

Accession

Primary (citable) accession number: Q4X1Q4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	July 5, 2005
Last modified:	December 14, 2011
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program