Q8X1T6 (ADE_EMENI) 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
Synonyms:	nadA
ORF Names:	AN6078

Organism

Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)

Taxonomic identifier

227321 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella

Protein attributes

Sequence length	364 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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. Has no activity with adenosine as a substrate. Ref.1
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.
Biophysicochemical properties	Kinetic parameters: KM=290 µM for adenine Ref.1 Vmax=200 nmol/min/mg enzyme

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	adenine catabolic process Inferred from direct assay Ref.1. Source: UniProtKB hypoxanthine salvage Inferred from Biological aspect of Ancestor. Source: RefGenome purine ribonucleoside monophosphate biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytosol Inferred from Biological aspect of Ancestor. Source: RefGenome nucleus Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular function	adenine deaminase activity Inferred from direct assay Ref.1. Source: UniProtKB 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 – 364	364	Adenine deaminase		PRO_0000256234
Sites
	Active site	224	1	Proton donor By similarity
	Metal binding	25	1	Zinc; catalytic By similarity
	Metal binding	27	1	Zinc; catalytic By similarity
	Metal binding	221	1	Zinc; catalytic By similarity
	Metal binding	301	1	Zinc; catalytic By similarity
	Binding site	302	1	Substrate By similarity
	Site	244	1	Important for catalytic activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8X1T6 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 2457E4B365402B35	FASTA	364	40,812
	10 20 30 40 50 60 MCPPNTPYQS QWHAFLHSLP KCEHHVHLEG CLEPPLIFSM ARKNNVSLPS PSSNPAYTSV 70 80 90 100 110 120 ETLSKRYGHF SSLDDFLSFY FIGMTVLKTQ SDFAELAWTY FKRAHAEGVH HTEVFFDPQV 130 140 150 160 170 180 HMERGLEYRV IVDGYVDGCK RAEKELGIST RLIMCFLKHL PLESAQRLYD TALNEGDLGL 190 200 210 220 230 240 DGRNPVIHGL GASSSEVGPP KDLFRPIYLG AKEKSINLTA HAGEEGDASY IAAALDMGAT 250 260 270 280 290 300 RIDHGIRLGE DPELMERVAR EEVLLTVCPV SNLQLKCVKS VAEVPIRKFL DAGVRFSINS 310 320 330 340 350 360 DDPAYFGAYI LECYCAVQEA FNLSVADWRL IAENGVKGSW IGEERKNELL WRIDECVKRF EGVL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sub-families of alpha/beta barrel enzymes: a new adenine deaminase family." Ribard C., Rochet M., Labedan B., Daignan-Fornier B., Alzari P., Scazzocchio C., Oestreicher N. J. Mol. Biol. 334:1117-1131(2003) [PubMed: 14643670] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES. Tissue: Mycelium.
[2]	"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae." Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W. Nature 438:1105-1115(2005) [PubMed: 16372000] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[3]	"The 2008 update of the Aspergillus nidulans genome annotation: a community effort." Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G. , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G. Fungal Genet. Biol. 46:S2-13(2009) [PubMed: 19146970] [Abstract] Cited for: GENOME REANNOTATION. Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF123460 Genomic DNA. Translation: AAL56636.1. AACD01000104 Genomic DNA. Translation: EAA58053.1. BN001301 Genomic DNA. Translation: CBF70232.1.
RefSeq	XP_663682.1. XM_658590.1.
3D structure databases
HSSP	HSSP built from PDB template 2AMX based on UniProtKB Q7RMV2.
ProteinModelPortal	Q8X1T6.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8X1T6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADANIAT00006939; CADANIAP00006939; CADANIAG00006939.
GeneID	2870856.
KEGG	ani:AN6078.2.
Phylogenomic databases
GeneTree	EFGT00050000005551.
OMA	EGIMLTV.
OrthoDB	EOG4P5PJR.
PhylomeDB	Q8X1T6.
Enzyme and pathway databases
BRENDA	3.5.4.2. 517.
Family and domain databases
InterPro	IPR006650. A/AMP_deam_AS. IPR001365. A/AMP_deaminase_dom. IPR006330. A_deaminase. [Graphical view]
KO	K01488.
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_EMENI

Accession

Primary (citable) accession number: Q8X1T6
Secondary accession number(s): C8V2S4, Q5B052

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	March 1, 2002
Last modified:	January 25, 2012
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program