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Protein

AMP deaminase

Gene

AMD1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: 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

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi362 – 3621Zinc; catalyticBy similarity
Metal bindingi364 – 3641Zinc; catalyticBy similarity
Binding sitei364 – 3641SubstrateBy similarity
Metal bindingi630 – 6301Zinc; catalyticBy similarity
Binding sitei633 – 6331SubstrateBy similarity
Active sitei652 – 6521Proton acceptorPROSITE-ProRule annotation
Metal bindingi707 – 7071Zinc; catalyticBy similarity

GO - Molecular functioni

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

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.
ReactomeiREACT_240981. Purine salvage.
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. 84 interactions.
DIPiDIP-1949N.
IntActiP15274. 10 interactions.
MINTiMINT-408221.
STRINGi4932.YML035C.

Structurei

3D structure databases

ProteinModelPortaliP15274.
SMRiP15274. Positions 299-797.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1816.
GeneTreeiENSGT00390000008190.
HOGENOMiHOG000092200.
InParanoidiP15274.
KOiK01490.
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

        10         20         30         40         50
MDNQATQRLN DLSLEPAPSH DEQDGSGLVI DIDQRKIGDE QAGVVVDDET
60 70 80 90 100
PPLEQQDSHE SLAADSRNAN FSYHENQQLL ENGTKQLALD EHDSHSAILE
110 120 130 140 150
QPSHSTNCSS SNIAAMNKGH DSADHASQNS GGKPRTLSAS AQHILPETLK
160 170 180 190 200
SFAGAPVVNK QVRTSASYKM GMLADDASQQ FLDDPSSELI DLYSKVAECR
210 220 230 240 250
NLRAKYQTIS VQNDDQNPKN KPGWVVYPPP PKPSYNSDTK TVVPVTNKPD
260 270 280 290 300
AEVFDFTKCE IPGEDPDWEF TLNDDDSYVV HRSGKTDELI AQIPTLRDYY
310 320 330 340 350
LDLEKMISIS SDGPAKSFAY RRLQYLEARW NLYYLLNEYQ ETSVSKRNPH
360 370 380 390 400
RDFYNVRKVD THVHHSACMN QKHLLRFIKH KLRHSKDEKV IFRDGKLLTL
410 420 430 440 450
DEVFRSLHLT GYDLSIDTLD MHAHKDTFHR FDKFNLKYNP IGESRLREIF
460 470 480 490 500
LKTNNYIKGT YLADITKQVI FDLENSKYQN CEYRISVYGR SLDEWDKLAS
510 520 530 540 550
WVIDNKVISH NVRWLVQIPR LYDIYKKTGI VQSFQDICKN LFQPLFEVTK
560 570 580 590 600
NPQSHPKLHV FLQRVIGFDS VDDESKVDRR FHRKYPKPSL WEAPQNPPYS
610 620 630 640 650
YYLYYLYSNV ASLNQWRAKR GFNTLVLRPH CGEAGDPEHL VSAYLLAHGI
660 670 680 690 700
SHGILLRKVP FVQYLYYLDQ VGIAMSPLSN NALFLTYDKN PFPRYFKRGL
710 720 730 740 750
NVSLSTDDPL QFSYTREPLI EEYSVAAQIY KLSNVDMCEL ARNSVLQSGW
760 770 780 790 800
EAQIKKHWIG KDFDKSGVEG NDVVRTNVPD IRINYRYDTL STELELVNHF
810
ANFKRTIEEK
Length:810
Mass (Da):93,302
Last modified:February 1, 1996 - v2
Checksum:i7A6DCB43B9B45C93
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti568 – 5681F → C in AAA34420 (PubMed:2690949).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliP15274.
SMRiP15274. Positions 299-797.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35135. 84 interactions.
DIPiDIP-1949N.
IntActiP15274. 10 interactions.
MINTiMINT-408221.
STRINGi4932.YML035C.

Proteomic databases

MaxQBiP15274.
PaxDbiP15274.
PeptideAtlasiP15274.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CYGDiYML035c.
SGDiS000004498. AMD1.

Phylogenomic databases

eggNOGiCOG1816.
GeneTreeiENSGT00390000008190.
HOGENOMiHOG000092200.
InParanoidiP15274.
KOiK01490.
OrthoDBiEOG7N63W7.

Enzyme and pathway databases

UniPathwayiUPA00591; UER00663.
BioCyciYEAST:YML035C-MONOMER.
ReactomeiREACT_240981. Purine salvage.

Miscellaneous databases

NextBioi978079.

Gene expression databases

GenevestigatoriP15274.

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]
ProtoNetiSearch...

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: January 7, 2015
This is version 140 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.1 Publication

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.