Q4IMJ1 (ADE_GIBZE) 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:	FG01567

Organism

Gibberella zeae (strain PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084) (Wheat head blight fungus) (Fusarium graminearum)

Taxonomic identifier

229533 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Hypocreomycetidae › Hypocreales › Nectriaceae › Gibberella

Protein attributes

Sequence length	353 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
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 – 353	353	Adenine deaminase		PRO_0000256235
Sites
	Active site	211	1	Proton donor By similarity
	Metal binding	19	1	Zinc; catalytic By similarity
	Metal binding	21	1	Zinc; catalytic By similarity
	Metal binding	208	1	Zinc; catalytic By similarity
	Metal binding	289	1	Zinc; catalytic By similarity
	Binding site	290	1	Substrate By similarity
	Site	232	1	Important for catalytic activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q4IMJ1 [UniParc]. Last modified August 16, 2005. Version 1. Checksum: 6F9DE1537E7814F5	FASTA	353	39,774
	10 20 30 40 50 60 MCKSRVHSFL QALPKVEQHL HIEGTLEPEL LFTLAEKNGI ELPNDPVYES ADKLRERYGR 70 80 90 100 110 120 FTSLDDFLHY YYLGMSVLIT ENDFETLAYQ YFQRAAGENV RHAEIFFDPQ AHIARGVSYD 130 140 150 160 170 180 TVVAGLVAAK HRAQKELGIT VELIVCILRH LPVPESHALV DTLLDRGHFN DGTLTGFGMV 190 200 210 220 230 240 SSEKAFPPEL FTDVYARVAK TGTHLTTHAG EEAPPSFITA SLEHLKVSRI DHGLAAAQDP 250 260 270 280 290 300 ELLKKLAANR TLLTFCPWSN VALCNLPELA DAPVREFLDA GVLFSVNSDD PAYFGAYVQE 310 320 330 340 350 VYCRVQDTFN LSVKDWAWIV RGAVEESWCS EERKKEILKE MEQVLEKYKD LDA

References

[1]

"The Fusarium graminearum genome reveals a link between localized polymorphism and pathogen specialization." Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A., Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T., Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S. , Goswami R.S., Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S., Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R., Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T., Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M., Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C. Science 317:1400-1402(2007) [PubMed: 17823352] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AACM01000079 Genomic DNA. Translation: EAA68522.1.
RefSeq	XP_381743.1. XM_381743.1.
3D structure databases
HSSP	HSSP built from PDB template 2AMX based on UniProtKB Q7RMV2.
ProteinModelPortal	Q4IMJ1.
ModBase	Search...
Protein-protein interaction databases
STRING	Q4IMJ1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	FGSG_01567T0; FGSG_01567P0; FGSG_01567.
GeneID	2783912.
KEGG	fgr:FG01567.1.
Phylogenomic databases
eggNOG	fuNOG04795.
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_GIBZE

Accession

Primary (citable) accession number: Q4IMJ1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	August 16, 2005
Last modified:	December 14, 2011
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program