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UniProtKB/Swiss-Prot entry P22108


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name APA2_YEAST
Primary accession number P22108
Secondary accession numbers None
Integrated into Swiss-Prot on August 1, 1991
Sequence was last modified on August 1, 1991 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 63)
Name and origin of the protein
Protein name 5',5'''-P-1,P-4-tetraphosphate phosphorylase 2
Synonyms EC 2.7.7.53
Diadenosine 5',5'''-P1,P4-tetraphosphate phosphorylase
AP-4-A phosphorylase
Ap4A phosphorylase II
AP,A phosphorylase
ATP adenylyltransferase
Gene name
Name: APA2
OrderedLocusNames: YDR530C
ORFNames: D9719.33
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-11.
STRAIN=YPAL16;
PubMed=2174863 [NCBI, ExPASy, EBI, Israel, Japan]
Plateau P., Fromant M., Schmitter J.-M., Blanquet S.;
"Catabolism of bis(5'-nucleosidyl) tetraphosphates in Saccharomyces cerevisiae.";
J. Bacteriol. 172:6892-6899(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169867 [NCBI, ExPASy, EBI, Israel, Japan]
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[3]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
Comments
  • FUNCTION: Sustains the catabolism of Np-4-N' nucleotides, rather than their synthesis.
  • CATALYTIC ACTIVITY: ADP + ATP = phosphate + P1,P4-bis(5'-adenosyl) tetraphosphate.
  • COFACTOR: Divalent cations.
  • SUBUNIT: Monomer.
  • MISCELLANEOUS: Present with 1770 molecules/cell in log phase SD medium.
  • SIMILARITY: To yeast AP-4-A phosphorylase I.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M60265; AAA34428.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U33057; AAB64969.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A37836; A37836.
RefSeq NP_010819.1; -.
3D structure databases
ModBase P22108.
Protein-protein interaction databases
DIP DIP:4729N; -.
IntAct P22108; -.
Organism-specific databases
CYGD YDR530c; -.
SGD S000002938; APA2.
Yeast-GFP YDR530C.
Gene expression databases
ArrayExpress P22108; -.
GermOnline YDR530C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from SGD).
GO:0005634; Cellular component: nucleus (inferred from direct assay from SGD).
GO:0003877; Molecular function: ATP adenylyltransferase activity (inferred from electronic annotation from InterPro).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0004081; Molecular function: bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) activity (inferred from direct assay from SGD).
GO:0009117; Biological process: nucleotide metabolic process (inferred from genetic interaction from SGD).
QuickGo view.
Family and domain databases
InterPro IPR009163; ATP_A_trans.
Graphical view of domain structure.
PIRSF PIRSF000846; ATP_adenylyltr; 1.
ProtoNet P22108.
Genome annotation databases
Ensembl YDR530C; Saccharomyces cerevisiae. [Contig view]
GeneID 852143; -.
GenomeReviews Z71256_GR; YDR530C.
KEGG sce:YDR530C; -.
NMPDR fig|4932.3.peg.1596; -.
Phylogenomic databases
HOGENOM P22108; -.
Other
LinkHub P22108; -.
NextBio 970558; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Direct protein sequencing; Hydrolase; Nucleotidyltransferase; Transferase.
Features
SEVIEWER logo Feature table viewer
KeyFrom To Length Description FTId
CHAIN   1   325  325     5',5'''-P-1,P-4-tetraphosphate phosphorylase 2. PRO_0000064613
Sequence information
Length: 325 AA [This is the length of the unprocessed precursor] Molecular weight: 36841 Da [This is the MW of the unprocessed precursor] CRC64: F2F2A2C900F1144F [This is a checksum on the sequence]
        10         20         30         40         50         60 
MIEENLKQKI HDKFVAAKKN GHLKVTHAES KKLKDPQTTT QYWVTFAPSL ALKPDANKNS 

        70         80         90        100        110        120 
DSKAEDPFAN PDEELVVTED LNGDGEYKLL LNKFPVVPEH SLLVTSEFKD QRSALTPSDL 

       130        140        150        160        170        180 
MTAYNVLCSL QGDKDDDVTC ERYLVFYNCG PHSGSSQDHK HLQIMQMPEK FIPFQDVLCN 

       190        200        210        220        230        240 
GKDHFLPTFN AEPLQDDKVS FAHFVLPLPE SSDQVDEDLL AMCYVSLMQR ALTFFQDWTN 

       250        260        270        280        290        300 
ESPELTKSYN VLLTKKWICV VPRSHAKSGP PLMLNINSTG YCGMILVKDR EKLENLTEDP 

       310        320 
HLVDKSLLQC GFPNTAGQKP TEYHY 

P22108 in FASTA format

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View entry in raw text format (no links)
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