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P15274 (AMPD_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
AMP deaminase
EC=3.5.4.6
Alternative name(s):
Myoadenylate deaminase
Gene names
Name:AMD1
Synonyms:AMD
Ordered Locus Names:YML035C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length810 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Ref.4

Sequence similarities

Belongs to the adenosine and AMP deaminases family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PRP40P332032EBI-2548,EBI-701

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 810810AMP deaminase
PRO_0000194414

Regions

Region433 – 4386Substrate binding By similarity
Region708 – 7114Substrate binding By similarity

Sites

Active site6521Proton acceptor By similarity
Metal binding3621Zinc; catalytic By similarity
Metal binding3641Zinc; catalytic By similarity
Metal binding6301Zinc; catalytic By similarity
Metal binding7071Zinc; catalytic By similarity
Binding site3641Substrate By similarity
Binding site6331Substrate By similarity

Amino acid modifications

Modified residue191Phosphoserine Ref.9
Modified residue261Phosphoserine Ref.9
Modified residue581Phosphoserine Ref.6 Ref.8 Ref.9
Modified residue611Phosphoserine Ref.6 Ref.8 Ref.9
Modified residue1361Phosphothreonine Ref.8
Modified residue1381Phosphoserine Ref.5 Ref.6 Ref.7 Ref.8 Ref.9
Modified residue1401Phosphoserine Ref.9

Experimental info

Sequence conflict5681F → C in AAA34420. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P15274 [UniParc].

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

FASTA81093,302
        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' 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. expand/collapse author list , Skelton J., Walsh S.V., Whitehead S., 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]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: 14562106] [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: 15665377] [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: 17330950] [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: 17287358] [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: 17563356] [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: 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.

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.
PIRS49744.
RefSeqNP_013677.1. NM_001182392.1.

3D structure databases

ProteinModelPortalP15274.
SMRP15274. Positions 299-797.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-1949N.
IntActP15274. 12 interactions.
MINTMINT-408221.
STRINGP15274.

Proteomic databases

PeptideAtlasP15274.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYML035C; YML035C; YML035C.
GeneID854973.
KEGGsce:YML035C.
NMPDRfig|4932.3.peg.4717.

Organism-specific databases

CYGDYML035c.
SGDS000004498. AMD1.

Phylogenomic databases

eggNOGfuNOG04148.
GeneTreeEFGT00050000003751.
HOGENOMHBG713563.
OMALQSGWEA.
OrthoDBEOG44XNR5.

Gene expression databases

ArrayExpressP15274.
GenevestigatorP15274.
GermOnlineYML035C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR006650. A/AMP_deam_AS.
IPR001365. A/AMP_deaminase_dom.
IPR006329. AMP_deaminase.
[Graphical view]
KOK01490.
PANTHERPTHR11359. PTHR11359. 1 hit.
PfamPF00962. A_deaminase. 1 hit.
[Graphical view]
PIRSFPIRSF001251. AMP_deaminase_met. 1 hit.
TIGRFAMsTIGR01429. AMP_deaminase. 1 hit.
PROSITEPS00485. A_DEAMINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio978079.

Entry information

Entry nameAMPD_YEAST
AccessionPrimary (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: December 14, 2011
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal 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

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents