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

Contribute

Send feedback

Read comments (?) or add your own

P15274 (AMPD_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 125. History...

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

Documents (4) |

Third-party data

text xml rdf/xml gff fasta

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

Names and origin

Protein names

Recommended name:
AMP deaminase
EC=3.5.4.6

Alternative name(s):
Myoadenylate deaminase

Gene names

Name:	AMD1
Synonyms:	AMD
Ordered Locus Names:	YML035C

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	810 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	AMP deaminase plays a critical role in energy metabolism.
Catalytic activity	AMP + H₂O = IMP + NH₃.
Cofactor	Binds 1 zinc ion per subunit By similarity.
Pathway	Purine metabolism; IMP biosynthesis via salvage pathway; IMP from AMP: step 1/1.
Subunit structure	Homotetramer.
Miscellaneous	Present with 3910 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the adenosine and AMP deaminases family.

Ontologies

Keywords
Biological process	Nucleotide metabolism
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	IMP salvage Inferred from electronic annotation. Source: UniProtKB-UniPathway guanine salvage Inferred from mutant phenotype PubMed 19635936. Source: SGD purine nucleotide metabolic process Inferred from mutant phenotype PubMed 19635936 PubMed 20087341. Source: SGD
Cellular_component	cytoplasm Inferred from direct assay PubMed 14562095. Source: SGD
Molecular_function	AMP deaminase activity Inferred from mutant phenotype Ref.1. Source: SGD metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PRP40	P33203	2	EBI-2548,EBI-701

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 810

810

AMP deaminase

PRO_0000194414

Regions

Region

433 – 438

Substrate binding By similarity

Region

708 – 711

Substrate binding By similarity

Sites

Active site

652

Proton acceptor By similarity

Metal binding

362

Zinc; catalytic By similarity

Metal binding

364

Zinc; catalytic By similarity

Metal binding

630

Zinc; catalytic By similarity

Metal binding

707

Zinc; catalytic By similarity

Binding site

364

Substrate By similarity

Binding site

633

Substrate By similarity

Amino acid modifications

Modified residue

Phosphoserine Ref.9

Modified residue

Phosphoserine Ref.9

Modified residue

Phosphoserine Ref.6 Ref.8 Ref.9

Modified residue

Phosphoserine Ref.6 Ref.8 Ref.9

Modified residue

136

Phosphothreonine Ref.8

Modified residue

138

Phosphoserine Ref.5 Ref.6 Ref.7 Ref.8 Ref.9

Modified residue

140

Phosphoserine Ref.9

Experimental info

Sequence conflict

568

F → C in AAA34420. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P15274 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: 7A6DCB43B9B45C93
Show »

FASTA

810

93,302

        10         20         30         40         50         60 
MDNQATQRLN DLSLEPAPSH DEQDGSGLVI DIDQRKIGDE QAGVVVDDET PPLEQQDSHE 

        70         80         90        100        110        120 
SLAADSRNAN FSYHENQQLL ENGTKQLALD EHDSHSAILE QPSHSTNCSS SNIAAMNKGH 

       130        140        150        160        170        180 
DSADHASQNS GGKPRTLSAS AQHILPETLK SFAGAPVVNK QVRTSASYKM GMLADDASQQ 

       190        200        210        220        230        240 
FLDDPSSELI DLYSKVAECR NLRAKYQTIS VQNDDQNPKN KPGWVVYPPP PKPSYNSDTK 

       250        260        270        280        290        300 
TVVPVTNKPD AEVFDFTKCE IPGEDPDWEF TLNDDDSYVV HRSGKTDELI AQIPTLRDYY 

       310        320        330        340        350        360 
LDLEKMISIS SDGPAKSFAY RRLQYLEARW NLYYLLNEYQ ETSVSKRNPH RDFYNVRKVD 

       370        380        390        400        410        420 
THVHHSACMN QKHLLRFIKH KLRHSKDEKV IFRDGKLLTL DEVFRSLHLT GYDLSIDTLD 

       430        440        450        460        470        480 
MHAHKDTFHR FDKFNLKYNP IGESRLREIF LKTNNYIKGT YLADITKQVI FDLENSKYQN 

       490        500        510        520        530        540 
CEYRISVYGR SLDEWDKLAS WVIDNKVISH NVRWLVQIPR LYDIYKKTGI VQSFQDICKN 

       550        560        570        580        590        600 
LFQPLFEVTK NPQSHPKLHV FLQRVIGFDS VDDESKVDRR FHRKYPKPSL WEAPQNPPYS 

       610        620        630        640        650        660 
YYLYYLYSNV ASLNQWRAKR GFNTLVLRPH CGEAGDPEHL VSAYLLAHGI SHGILLRKVP 

       670        680        690        700        710        720 
FVQYLYYLDQ VGIAMSPLSN NALFLTYDKN PFPRYFKRGL NVSLSTDDPL QFSYTREPLI 

       730        740        750        760        770        780 
EEYSVAAQIY KLSNVDMCEL ARNSVLQSGW EAQIKKHWIG KDFDKSGVEG NDVVRTNVPD 

       790        800        810 
IRINYRYDTL STELELVNHF ANFKRTIEEK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of AMD, the AMP deaminase gene in yeast. Production of amd strain, cloning, nucleotide sequence, and properties of the protein." Meyer S.L., Kvalnes-Krick K.L., Schramm V.L. Biochemistry 28:8734-8743(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII." Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. Barrell B.G. Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"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].
[5]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, MASS SPECTROMETRY. Strain: YAL6B.
[6]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58; SER-61 AND SER-138, MASS SPECTROMETRY. Strain: ADR376.
[7]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, MASS SPECTROMETRY.
[8]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58; SER-61; THR-136 AND SER-138, MASS SPECTROMETRY.
[9]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-26; SER-58; SER-61; SER-138 AND SER-140, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M30449 Genomic DNA. Translation: AAA34420.1. Z46659 Genomic DNA. Translation: CAA86620.1. BK006946 Genomic DNA. Translation: DAA09864.1.
PIR	S49744.
RefSeq	NP_013677.1. NM_001182392.1.
3D structure databases
ProteinModelPortal	P15274.
SMR	P15274. Positions 299-797.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1949N.
IntAct	P15274. 10 interactions.
MINT	MINT-408221.
STRING	4932.YML035C.
Proteomic databases
PaxDb	P15274.
PeptideAtlas	P15274.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YML035C; YML035C; YML035C.
GeneID	854973.
KEGG	sce:YML035C.
Organism-specific databases
CYGD	YML035c.
SGD	S000004498. AMD1.
Phylogenomic databases
eggNOG	COG1816.
GeneTree	ENSGT00390000008190.
HOGENOM	HOG000092200.
KO	K01490.
OMA	DMHAHKD.
OrthoDB	EOG44XNR5.
Enzyme and pathway databases
UniPathway	UPA00591; UER00663.
Gene expression databases
Genevestigator	P15274.
GermOnline	YML035C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR006650. A/AMP_deam_AS. IPR001365. A/AMP_deaminase_dom. IPR006329. AMP_deaminase. [Graphical view]
PANTHER	PTHR11359. PTHR11359. 1 hit.
Pfam	PF00962. A_deaminase. 1 hit. [Graphical view]
PIRSF	PIRSF001251. AMP_deaminase_met. 1 hit.
TIGRFAMs	TIGR01429. AMP_deaminase. 1 hit.
PROSITE	PS00485. A_DEAMINASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	978079.

Entry information

Entry name

AMPD_YEAST

Accession

Primary (citable) accession number: P15274
Secondary accession number(s): D6VZE0

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	February 1, 1996
Last modified:	April 3, 2013
This is version 125 of the entry and version 2 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 XIII

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

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

Regions

Sites

Amino acid modifications

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

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents