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P15274

- AMPD_YEAST

UniProt

P15274 - AMPD_YEAST

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Protein

AMP deaminase

Gene
AMD1, AMD, YML035C
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

AMP deaminase plays a critical role in energy metabolism.

Catalytic activityi

AMP + H2O = IMP + NH3.

Cofactori

Binds 1 zinc ion per subunit By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi362 – 3621Zinc; catalytic By similarity
Metal bindingi364 – 3641Zinc; catalytic By similarity
Binding sitei364 – 3641Substrate By similarity
Metal bindingi630 – 6301Zinc; catalytic By similarity
Binding sitei633 – 6331Substrate By similarity
Active sitei652 – 6521Proton acceptor By similarity
Metal bindingi707 – 7071Zinc; catalytic By similarity

GO - Molecular functioni

  1. AMP deaminase activity Source: SGD
  2. metal ion binding Source: UniProtKB-KW
  3. protein binding Source: IntAct

GO - Biological processi

  1. guanine salvage Source: SGD
  2. IMP salvage Source: UniProtKB-UniPathway
  3. purine nucleotide metabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Nucleotide metabolism

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:YML035C-MONOMER.
UniPathwayiUPA00591; UER00663.

Names & Taxonomyi

Protein namesi
Recommended name:
AMP deaminase (EC:3.5.4.6)
Alternative name(s):
Myoadenylate deaminase
Gene namesi
Name:AMD1
Synonyms:AMD
Ordered Locus Names:YML035C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XIII

Organism-specific databases

CYGDiYML035c.
SGDiS000004498. AMD1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 810810AMP deaminasePRO_0000194414Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei19 – 191Phosphoserine2 Publications
Modified residuei58 – 581Phosphoserine3 Publications
Modified residuei61 – 611Phosphoserine3 Publications
Modified residuei138 – 1381Phosphoserine3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP15274.
PaxDbiP15274.
PeptideAtlasiP15274.

Expressioni

Gene expression databases

GenevestigatoriP15274.

Interactioni

Subunit structurei

Homotetramer.

Binary interactionsi

WithEntry#Exp.IntActNotes
PRP40P332032EBI-2548,EBI-701

Protein-protein interaction databases

BioGridi35135. 83 interactions.
DIPiDIP-1949N.
IntActiP15274. 10 interactions.
MINTiMINT-408221.
STRINGi4932.YML035C.

Structurei

3D structure databases

ProteinModelPortaliP15274.
SMRiP15274. Positions 299-797.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni433 – 4386Substrate binding By similarity
Regioni708 – 7114Substrate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1816.
GeneTreeiENSGT00390000008190.
HOGENOMiHOG000092200.
KOiK01490.
OMAiPRDIPHR.
OrthoDBiEOG7N63W7.

Family and domain databases

InterProiIPR006650. A/AMP_deam_AS.
IPR001365. A/AMP_deaminase_dom.
IPR006329. AMPD.
[Graphical view]
PANTHERiPTHR11359. PTHR11359. 1 hit.
PfamiPF00962. A_deaminase. 1 hit.
[Graphical view]
PIRSFiPIRSF001251. AMP_deaminase_met. 1 hit.
TIGRFAMsiTIGR01429. AMP_deaminase. 1 hit.
PROSITEiPS00485. A_DEAMINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P15274-1 [UniParc]FASTAAdd to Basket

« Hide

MDNQATQRLN DLSLEPAPSH DEQDGSGLVI DIDQRKIGDE QAGVVVDDET    50
PPLEQQDSHE SLAADSRNAN FSYHENQQLL ENGTKQLALD EHDSHSAILE 100
QPSHSTNCSS SNIAAMNKGH DSADHASQNS GGKPRTLSAS AQHILPETLK 150
SFAGAPVVNK QVRTSASYKM GMLADDASQQ FLDDPSSELI DLYSKVAECR 200
NLRAKYQTIS VQNDDQNPKN KPGWVVYPPP PKPSYNSDTK TVVPVTNKPD 250
AEVFDFTKCE IPGEDPDWEF TLNDDDSYVV HRSGKTDELI AQIPTLRDYY 300
LDLEKMISIS SDGPAKSFAY RRLQYLEARW NLYYLLNEYQ ETSVSKRNPH 350
RDFYNVRKVD THVHHSACMN QKHLLRFIKH KLRHSKDEKV IFRDGKLLTL 400
DEVFRSLHLT GYDLSIDTLD MHAHKDTFHR FDKFNLKYNP IGESRLREIF 450
LKTNNYIKGT YLADITKQVI FDLENSKYQN CEYRISVYGR SLDEWDKLAS 500
WVIDNKVISH NVRWLVQIPR LYDIYKKTGI VQSFQDICKN LFQPLFEVTK 550
NPQSHPKLHV FLQRVIGFDS VDDESKVDRR FHRKYPKPSL WEAPQNPPYS 600
YYLYYLYSNV ASLNQWRAKR GFNTLVLRPH CGEAGDPEHL VSAYLLAHGI 650
SHGILLRKVP FVQYLYYLDQ VGIAMSPLSN NALFLTYDKN PFPRYFKRGL 700
NVSLSTDDPL QFSYTREPLI EEYSVAAQIY KLSNVDMCEL ARNSVLQSGW 750
EAQIKKHWIG KDFDKSGVEG NDVVRTNVPD IRINYRYDTL STELELVNHF 800
ANFKRTIEEK 810
Length:810
Mass (Da):93,302
Last modified:February 1, 1996 - v2
Checksum:i7A6DCB43B9B45C93
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti568 – 5681F → C in AAA34420. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M30449 Genomic DNA. Translation: AAA34420.1.
Z46659 Genomic DNA. Translation: CAA86620.1.
BK006946 Genomic DNA. Translation: DAA09864.1.
PIRiS49744.
RefSeqiNP_013677.1. NM_001182392.1.

Genome annotation databases

EnsemblFungiiYML035C; YML035C; YML035C.
GeneIDi854973.
KEGGisce:YML035C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M30449 Genomic DNA. Translation: AAA34420.1 .
Z46659 Genomic DNA. Translation: CAA86620.1 .
BK006946 Genomic DNA. Translation: DAA09864.1 .
PIRi S49744.
RefSeqi NP_013677.1. NM_001182392.1.

3D structure databases

ProteinModelPortali P15274.
SMRi P15274. Positions 299-797.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 35135. 83 interactions.
DIPi DIP-1949N.
IntActi P15274. 10 interactions.
MINTi MINT-408221.
STRINGi 4932.YML035C.

Proteomic databases

MaxQBi P15274.
PaxDbi P15274.
PeptideAtlasi P15274.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YML035C ; YML035C ; YML035C .
GeneIDi 854973.
KEGGi sce:YML035C.

Organism-specific databases

CYGDi YML035c.
SGDi S000004498. AMD1.

Phylogenomic databases

eggNOGi COG1816.
GeneTreei ENSGT00390000008190.
HOGENOMi HOG000092200.
KOi K01490.
OMAi PRDIPHR.
OrthoDBi EOG7N63W7.

Enzyme and pathway databases

UniPathwayi UPA00591 ; UER00663 .
BioCyci YEAST:YML035C-MONOMER.

Miscellaneous databases

NextBioi 978079.

Gene expression databases

Genevestigatori P15274.

Family and domain databases

InterProi IPR006650. A/AMP_deam_AS.
IPR001365. A/AMP_deaminase_dom.
IPR006329. AMPD.
[Graphical view ]
PANTHERi PTHR11359. PTHR11359. 1 hit.
Pfami PF00962. A_deaminase. 1 hit.
[Graphical view ]
PIRSFi PIRSF001251. AMP_deaminase_met. 1 hit.
TIGRFAMsi TIGR01429. AMP_deaminase. 1 hit.
PROSITEi PS00485. A_DEAMINASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-58 AND SER-61, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-58 AND SER-61, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiAMPD_YEAST
AccessioniPrimary (citable) accession number: P15274
Secondary accession number(s): D6VZE0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: February 1, 1996
Last modified: September 3, 2014
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 3910 molecules/cell in log phase SD medium.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

External Data

Dasty 3

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