Reviewed, UniProtKB/Swiss-Prot P22108 (APA2_YEAST)

Names and origin

Protein names

Recommended name:
    5',5'''-P-1,P-4-tetraphosphate phosphorylase 2
    EC=2.7.7.53
Alternative name(s):
    Diadenosine 5',5'''-P1,P4-tetraphosphate phosphorylase
      Short name=AP-4-A phosphorylase
    Ap4A phosphorylase II
      Short name=AP,A phosphorylase
    ATP adenylyltransferase

Gene names

Name:	APA2
Ordered Locus Names:	YDR530C
ORF Names:	D9719.33

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	325 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Sustains the catabolism of Np-4-N' nucleotides, rather than their synthesis.
Catalytic activity	ADP + ATP = phosphate + P1,P(4)-bis(5'-adenosyl) tetraphosphate.
Cofactor	Divalent cations.
Subunit structure	Monomer.
Miscellaneous	Present with 1770 molecules/cell in log phase SD medium. Ref.3
Sequence similarities	To yeast AP-4-A phosphorylase I.

Ontologies

Keywords
Ligand	ATP-binding Nucleotide-binding
Molecular function	Hydrolase Nucleotidyltransferase Transferase
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	nucleotide metabolic process Ref.1 Inferred from genetic interaction. Source: SGD
Cellular component	cytoplasm Inferred from direct assay. Source: SGD nucleus Inferred from direct assay. Source: SGD
Molecular function	ATP adenylyltransferase activity Inferred from electronic annotation. Source: EC ATP binding Inferred from electronic annotation. Source: UniProtKB-KW bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) activity Ref.1 Inferred from direct assay. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 325	325	5',5'''-P-1,P-4-tetraphosphate phosphorylase 2		PRO_0000064613

Sequences

	Sequence		Length	Mass (Da)
	P22108-1 [UniParc]. Last modified August 1, 1991. Version 1. Checksum: F2F2A2C900F1144F	FASTA	325	36,841
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Catabolism of bis(5'-nucleosidyl) tetraphosphates in Saccharomyces cerevisiae." Plateau P., Fromant M., Schmitter J.-M., Blanquet S. J. Bacteriol. 172:6892-6899(1990) [PubMed: 2174863] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-11. Strain: YPAL16.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." 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. Nature 387:75-78(1997) [PubMed: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"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].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M60265 Genomic DNA. Translation: AAA34428.1. U33057 Genomic DNA. Translation: AAB64969.1.
PIR	A37836.
RefSeq	NP_010819.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:4729N.
IntAct	P22108. 1 interaction.
Genome annotation databases
Ensembl	YDR530C. Saccharomyces cerevisiae. [Contig view]
GeneID	852143.
GenomeReviews	Gene locus YDR530C in contig Z71256_GR.
KEGG	sce:YDR530C.
NMPDR	fig|4932.3.peg.1596.
Organism-specific databases
CYGD	YDR530c.
SGD	S000002938. APA2.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P22108.
OMA	P22108. FPNTAGQ.
Enzyme and pathway databases
BRENDA	2.7.7.53. 250.
Gene expression databases
ArrayExpress	P22108.
GermOnline	YDR530C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR009163. ATP_adenylyltransferase. IPR019200. ATP_adenylyltransferase_C. [Graphical view]
Pfam	PF09830. ATP_transf. 1 hit. [Graphical view]
PIRSF	PIRSF000846. ATP_adenylyltr. 1 hit.
ProtoNet	Search...
Other Resources
NextBio	970558.

Entry information

Entry name

APA2_YEAST

Accession

Primary (citable) accession number: P22108

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	August 1, 1991
Last modified:	June 16, 2009
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)