Adenine deaminase - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P53909 (ADE_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 108. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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:	YNL141W
ORF Names:	N1208, N1825

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	347 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. Also exhibits a low activity towards N(6)-substituted adenines that are commonly known as the plant hormones cytokinins. Ref.2 Ref.5 Ref.8 Ref.9
Catalytic activity	Adenine + H₂O = hypoxanthine + NH₃. HAMAP-Rule MF_03145
Cofactor	Binds 1 zinc ion per subunit By similarity.
Subcellular location	Cytoplasm. Nucleus Ref.6.
Induction	Reduced when grown in a poor nitrogen source medium and strongly down-regulated when cells enter quiescence under nutrient-limiting conditions. Ref.5
Post-translational modification	Probably ubiquitinated when cells enter quiescence in response to nutrient limitation, since it is specifically degraded via a process requiring the F-box protein SAF1 and components of the SKP1-Cullin-F-box complex. HAMAP-Rule MF_03145
Miscellaneous	Present with 20700 molecules/cell in log phase SD medium. HAMAP-Rule MF_03145
Sequence similarities	Belongs to the adenosine and AMP deaminases family. Adenine deaminase type 2 subfamily.
Biophysicochemical properties	Kinetic parameters: K_M=55 µM for adenine Ref.9 pH dependence: Optimum pH is 7.0. Temperature dependence: Optimum temperature is 30-37 degrees Celsius.

Ontologies

Keywords
Biological process	Nucleotide metabolism
Cellular component	Cytoplasm Nucleus
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
PTM	Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	adenine catabolic process Inferred from genetic interaction Ref.2. Source: UniProtKB hypoxanthine salvage Inferred from direct assay Ref.5. Source: SGD nucleotide metabolic process Inferred from electronic annotation. Source: UniProtKB-KW 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 direct assay Ref.6. Source: SGD
Molecular_function	adenine deaminase activity Inferred from genetic interaction Ref.2. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SAF1	P38352	2	EBI-2197,EBI-21172

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 347

347

Adenine deaminase HAMAP-Rule MF_03145

PRO_0000194360

Sites

Active site

207

Proton donor By similarity

Metal binding

Zinc; catalytic By similarity

Metal binding

Zinc; catalytic By similarity

Metal binding

204

Zinc; catalytic By similarity

Metal binding

285

Zinc; catalytic By similarity

Binding site

286

Substrate By similarity

Site

228

Important for catalytic activity By similarity

Experimental info

Mutagenesis

I → T in aah1-2; impairs AAH1 degradation during postdiauxic growth and leads to weak interaction with SAF1. Ref.8

Mutagenesis

N → K in aah1-3; impairs AAH1 degradation during postdiauxic growth and leads to weak interaction with SAF1. Ref.8

Mutagenesis

219

D → G in aah1-4; impairs AAH1 degradation during postdiauxic growth and leads to weak interaction with SAF1. Ref.8

Mutagenesis

237

E → V in aah1-6; impairs AAH1 degradation during postdiauxic growth and leads to weak interaction with SAF1. Ref.8

Mutagenesis

329

K → E in aah1-7; impairs AAH1 degradation during postdiauxic growth. Ref.8

Sequences

Sequence

Length

Mass (Da)

Tools

P53909 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: E25573A9F9EB7BB6
Show »

FASTA

347

39,635

        10         20         30         40         50         60 
MVSVEFLQEL PKCEHHLHLE GTLEPDLLFP LAKRNDIILP EGFPKSVEEL NEKYKKFRDL 

        70         80         90        100        110        120 
QDFLDYYYIG TNVLISEQDF FDLAWAYFKK VHKQGLVHAE VFYDPQSHTS RGISIETVTK 

       130        140        150        160        170        180 
GFQRACDKAF SEFGITSKLI MCLLRHIEPE ECLKTIEEAT PFIKDGTISA LGLDSAEKPF 

       190        200        210        220        230        240 
PPHLFVECYG KAASLNKDLK LTAHAGEEGP AQFVSDALDL LQVTRIDHGI NSQYDEELLD 

       250        260        270        280        290        300 
RLSRDQTMLT ICPLSNVKLQ VVQSVSELPL QKFLDRDVPF SLNSDDPAYF GGYILDVYTQ 

       310        320        330        340 
VSKDFPHWDH ETWGRIAKNA IKGSWCDDKR KNGLLSRVDE VVTKYSH

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A 43.5 kb segment of yeast chromosome XIV, which contains MFA2, MEP2, CAP/SRV2, NAM9, FKB1/FPR1/RBP1, MOM22 and CPT1, predicts an adenosine deaminase gene and 14 new open reading frames." Mallet L., Bussereau F., Jacquet M. Yeast 11:1195-1209(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications." Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J. Hani J. Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"Adenine deaminase and adenine utilization in Saccharomyces cerevisiae." Deeley M.C. J. Bacteriol. 174:3102-3110(1992) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INDUCTION.
[6]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[7]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[8]	"Skp1-Cullin-F-box-dependent degradation of Aah1p requires its interaction with the F-box protein Saf1p." Escusa S., Laporte D., Massoni A., Boucherie H., Dautant A., Daignan-Fornier B. J. Biol. Chem. 282:20097-20103(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH SAF1, UBIQUITINATION, MUTAGENESIS OF ILE-69; ASN-72; ASP-219; GLU-237 AND LYS-329.
[9]	"Hydrolytic cleavage of N6-substituted adenine derivatives by eukaryotic adenine and adenosine deaminases." Pospisilova H., Sebela M., Novak O., Frebort I. Biosci. Rep. 28:335-347(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z46843 Genomic DNA. Translation: CAA86885.1. Z71417 Genomic DNA. Translation: CAA96024.1. BK006947 Genomic DNA. Translation: DAA10407.1.
PIR	S55143.
RefSeq	NP_014258.1. NM_001182979.1.
3D structure databases
ProteinModelPortal	P53909.
SMR	P53909. Positions 5-321.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-4342N.
IntAct	P53909. 3 interactions.
MINT	MINT-499127.
STRING	4932.YNL141W.
Proteomic databases
PaxDb	P53909.
PeptideAtlas	P53909.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YNL141W; YNL141W; YNL141W.
GeneID	855581.
KEGG	sce:YNL141W.
Organism-specific databases
CYGD	YNL141w.
SGD	S000005085. AAH1.
Phylogenomic databases
eggNOG	COG1816.
GeneTree	ENSGT00640000091458.
KO	K01488.
OMA	SEVYRTE.
OrthoDB	EOG4P5PJR.
Gene expression databases
Genevestigator	P53909.
GermOnline	YNL141W. Saccharomyces cerevisiae.
Family and domain databases
HAMAP	MF_01962. Adenine_deaminase.
InterPro	IPR006650. A/AMP_deam_AS. IPR001365. A/AMP_deaminase_dom. IPR006330. Ado/ade_deaminase. [Graphical view]
Pfam	PF00962. A_deaminase. 1 hit. [Graphical view]
TIGRFAMs	TIGR01430. aden_deam. 1 hit.
PROSITE	PS00485. A_DEAMINASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	979709.

Entry information

Entry name

ADE_YEAST

Accession

Primary (citable) accession number: P53909
Secondary accession number(s): D6W141

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 108 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome XIV

Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents