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P50998 (AMPD_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·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:ada1
ORF Names:SPBC106.04
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces ›

Protein attributes

Sequence length831 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. Ref.4

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 By similarity.

Subcellular location

Cytoplasm Ref.5.

Sequence similarities

Belongs to the adenosine and AMP deaminases family.

Ontologies

Keywords
   Biological processNucleotide metabolism
   Cellular componentCytoplasm
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processIMP biosynthetic process

Inferred from sequence model. Source: PomBase

IMP salvage

Inferred from electronic annotation. Source: UniProtKB-UniPathway

regulation of transcription from RNA polymerase II promoter

Inferred from experiment PubMed 21642955. Source: PomBase

   Cellular_componentcytosol

Inferred from direct assay Ref.5. Source: PomBase

   Molecular_functionAMP deaminase activity

Inferred from direct assay Ref.4. Source: PomBase

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 831831AMP deaminase
PRO_0000194413

Regions

Region390 – 3956Substrate binding By similarity
Region665 – 6684Substrate binding By similarity

Sites

Active site6091Proton acceptor By similarity
Metal binding3191Zinc; catalytic By similarity
Metal binding3211Zinc; catalytic By similarity
Metal binding5871Zinc; catalytic By similarity
Metal binding6641Zinc; catalytic By similarity
Binding site3211Substrate By similarity
Binding site5901Substrate By similarity

Amino acid modifications

Modified residue791Phosphoserine Ref.6
Modified residue841Phosphoserine Ref.6
Modified residue7581Phosphoserine Ref.6
Modified residue7761Phosphoserine Ref.6
Modified residue7801Phosphoserine Ref.6
Modified residue7821Phosphoserine Ref.6

Experimental info

Sequence conflict468 – 50538NVRWL…PLFEV → TFVGLFKYLVCMMCIRSPVL LRLLKRSSEMSLNHCSKF in CAA62797. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P50998 [UniParc].

Last modified July 11, 2012. Version 3.
Checksum: F027B33C7AD0C63D

FASTA83195,887
        10         20         30         40         50         60 
MNMEQEDDQV PAVAAETVPL KRYVTNPGAN RDEEVAAAPS SQDTPYFDYA YERSLRHQDA 

        70         80         90        100        110        120 
KFLAMNGTQN GRDGLPSKSP RRPSVSASTV RNSDDVNHSK AGPGSGKLLN DTLQSKISSI 

       130        140        150        160        170        180 
HMPHVQQGDN AVVSSVGGPE TDPGNMETTD PLFSDELAEI YLSIHKCMDM RHKYIRVSLQ 

       190        200        210        220        230        240 
GELDNPIDDD SWIIYPDCKE GEDDTGLFNF ADCKIPGIEN EMEYHMDHQG IFQVYENDSA 

       250        260        270        280        290        300 
YIAGTPSFHI PTIRDYYIDL EFLLSASSDG PSKSFSFRRL QYLEGRWNMY MLLNEYQELA 

       310        320        330        340        350        360 
DTKKVPHRDF YNVRKVDTHV HHSALANQKH LLRFIKAKLR KCPNEKVIWR DGKFLTLQEV 

       370        380        390        400        410        420 
FDSLKLTSYD LSIDTLDMHA HTDTFHRFDK FNLKYNPIGE SRLRTIFLKT DNDINGRYLA 

       430        440        450        460        470        480 
ELTKEVFTDL RTQKYQMAEY RISIYGRNRE EWDKLAAWII DNELFSPNVR WLIQVPRLYD 

       490        500        510        520        530        540 
VYKKSGIVET FEEVVRNVFE PLFEVTKDPR THPKLHVFLQ RVIGFDSVDD ESKPERRTFR 

       550        560        570        580        590        600 
KFPYPKHWDI NLNPPYSYWL YYMYANMTSL NSWRKIRGFN TFVLRPHCGE AGDTDHLASA 

       610        620        630        640        650        660 
FLLSHGINHG ILLRKVPFLQ YLWYLDQIPI AMSPLSNNAL FLAYDKNPFL TYFKRGLNVS 

       670        680        690        700        710        720 
LSTDDPLQFA FTREPLIEEY AVAAQIYKLS AVDMCELARN SVLQSGFERQ LKERWLGVDF 

       730        740        750        760        770        780 
QDIDRTNVPI IRLAYRALTL TQEIALVNKH VQPSKHPSNH DLEELIHKYD AMTGTSDPLS 

       790        800        810        820        830 
ASPRTNDATI SSRLSLHDGH DHGAFFPGLS VISERRRRKD SMASSSQDLK D

« Hide

References

« Hide 'large scale' references
[1]Rochet M., Levesque H., Gaillardin C.
Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 972 / ATCC 24843.
[2]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[3]"Comparative functional genomics of the fission yeasts."
Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N., Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y., Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K. expand/collapse author list , Bayne E.H., Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G., French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A., Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P., Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R., Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J., Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W., Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.
Science 332:930-936(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: REVISION OF GENE MODEL.
[4]"Yeast AMP deaminase. Catalytic activity in Schizosaccharomyces pombe and chromosomal location in Saccharomyces cerevisiae."
Sollitti P., Merkler D.J., Estupinan B., Schramm V.L.
J. Biol. Chem. 268:4549-4555(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY.
[5]"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[6]"Phosphoproteome analysis of fission yeast."
Wilson-Grady J.T., Villen J., Gygi S.P.
J. Proteome Res. 7:1088-1097(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79; SER-84; SER-758; SER-776; SER-780 AND SER-782, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X91498 Genomic DNA. Translation: CAA62797.1. Sequence problems.
CU329671 Genomic DNA. Translation: CAB53720.2.
PIRT39261.
RefSeqNP_595153.2. NM_001021062.2.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRING4896.SPBC106.04-1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC106.04.1; SPBC106.04.1:pep; SPBC106.04.
GeneID2540105.
KEGGspo:SPBC106.04.

Organism-specific databases

PomBaseSPBC106.04.

Phylogenomic databases

eggNOGCOG1816.
HOGENOMHOG000092200.
KOK01490.
OrthoDBEOG44XNR5.

Enzyme and pathway databases

UniPathwayUPA00591; UER00663.

Family and domain databases

InterProIPR006650. A/AMP_deam_AS.
IPR001365. A/AMP_deaminase_dom.
IPR006329. AMP_deaminase.
[Graphical view]
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

NextBio20801241.

Entry information

Entry nameAMPD_SCHPO
AccessionPrimary (citable) accession number: P50998
Secondary accession number(s): Q9URV7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 11, 2012
Last modified: May 1, 2013
This is version 94 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents