AMP deaminase - Saccharomyces cerevisiae (Baker's yeast)

Contribute

Send feedback

Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P15274 (AMPD_YEAST)

Last modified June 16, 2009. Version 87. History...

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

Documents (4) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

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 (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

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

Hide | Top

Protein attributes

Sequence length	810 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

Hide | Top

General annotation (Comments)

Function	AMP deaminase plays a critical role in energy metabolism.
Catalytic activity	AMP + H₂O = IMP + NH₃.
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. Ref.3
Sequence similarities	Belongs to the adenosine and AMP deaminases family.

Hide | Top

Ontologies

Keywords
Biological process	Nucleotide metabolism
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	purine base metabolic process Inferred from electronic annotation. Source: InterPro purine ribonucleoside monophosphate biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from direct assay. Source: SGD
Molecular function	AMP deaminase activity Inferred from direct assay. Source: SGD identical protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Hide | Top

Binary interactions

With	Entry	#Exp.	IntAct
itself		1	EBI-2548,EBI-2548
ESS1	P22696	1	EBI-2548,EBI-6679
PRP40	P33203	1	EBI-2548,EBI-701
RSP5	P39940	1	EBI-2548,EBI-16219
SSM4	P40318	1	EBI-2548,EBI-18208
URN1	Q06525	1	EBI-2548,EBI-35138

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 810

810

AMP deaminase

PRO_0000194414

Sites

Active site

422

Potential

Active site

631

Potential

Active site

707

Potential

Active site

708

Potential

Amino acid modifications

Modified residue

Phosphoserine Ref.8

Modified residue

Phosphoserine Ref.8

Modified residue

Phosphoserine Ref.8 Ref.5 Ref.7

Modified residue

Phosphoserine Ref.8 Ref.5 Ref.7

Modified residue

136

Phosphothreonine Ref.7

Modified residue

138

Phosphoserine Ref.8 Ref.5 Ref.7 Ref.4 Ref.6

Modified residue

140

Phosphoserine Ref.8

Experimental info

Sequence conflict

568

F → C in AAA34420. Ref.1

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

P15274-1 [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

Hide | Top

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: 2690949] [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: 9169872] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[4]	"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: 15665377] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, MASS SPECTROMETRY.
[5]	"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: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58; SER-61 AND SER-138, MASS SPECTROMETRY.
[6]	"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: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, MASS SPECTROMETRY.
[7]	"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: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58; SER-61; THR-136 AND SER-138, MASS SPECTROMETRY.
[8]	"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: 18407956] [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.

Hide | Top

Cross-references

Sequence databases
	M30449 Genomic DNA. Translation: AAA34420.1. Z46659 Genomic DNA. Translation: CAA86620.1.
PIR	S49744.
RefSeq	NP_013677.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:1949N.
IntAct	P15274. 9 interactions.
Proteomic databases
PeptideAtlas	P15274.
Genome annotation databases
Ensembl	YML035C. Saccharomyces cerevisiae. [Contig view]
GeneID	854973.
GenomeReviews	Gene locus YML035C in contig Z71257_GR.
KEGG	sce:YML035C.
NMPDR	fig\|4932.3.peg.4717.
Organism-specific databases
CYGD	YML035c.
SGD	S000004498. AMD1.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P15274.
OMA	P15274. DPLQFSY.
Enzyme and pathway databases
BRENDA	3.5.4.6. 250.
Gene expression databases
ArrayExpress	P15274.
GermOnline	YML035C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR006650. A/AMP_deam_AS. IPR001365. A/AMP_deaminase. IPR006329. AMP_deaminase. IPR016297. AMP_deaminase_met. [Graphical view]
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 Resources
NextBio	978079.

Hide | Top

Entry information

Entry name

AMPD_YEAST

Accession

Primary (citable) accession number: P15274

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	February 1, 1996
Last modified:	June 16, 2009
This is version 87 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

Hide | Top

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Yeast

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

Yeast chromosome XIII

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

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents