P16550 (APA1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein APA1

Including the following 2 domains:

1. 5',5'''-P-1,P-4-tetraphosphate phosphorylase
   EC=2.7.7.53
   Alternative name(s):
   ATP adenylyltransferase
   Diadenosine 5',5'''-P1,P4-tetraphosphate phosphorylase
   Short name=AP,A phosphorylase
   Short name=AP-4-A phosphorylase
2. ADP-sulfurylase
   EC=2.7.7.5

Gene names

Name:	APA1
Synonyms:	DTP1
Ordered Locus Names:	YCL050C
ORF Names:	YCL50C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	321 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Ap4A phosphorylase catabolizes Ap4N nucleotides (where N is A,C,G or U). Additionally this enzyme catalyzes the conversion of adenosine-5-phosphosulfate (AMPs) plus Pi to ADP plus sulfate, the exchange of NDP and phosphate and the synthesis of Ap4A from AMPs plus ATP.
Catalytic activity	ADP + ATP = phosphate + P1,P(4)-bis(5'-adenosyl) tetraphosphate. ADP + sulfate = phosphate + adenylyl sulfate. Adenylylsulfate + ATP = P1,P(4)-bis(5'-adenosyl)tetraphosphate + sulfate.
Cofactor	Divalent cations.
Subunit structure	Monomer.
Miscellaneous	Present with 19600 molecules/cell in log phase SD medium. Ref.6
Sequence similarities	To yeast AP-4-A phosphorylase II.

Ontologies

Keywords
Ligand	ATP-binding Nucleotide-binding
Molecular function	Hydrolase Nucleotidyltransferase Transferase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	nucleotide metabolic process Traceable author statement. 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 activity Traceable author statement. Source: SGD sulfate adenylyltransferase (ADP) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Probable
	Chain	2 – 321	320	Protein APA1		PRO_0000064611
Amino acid modifications
	Modified residue	2	1	N-acetylserine Probable
	Modified residue	60	1	Phosphothreonine Ref.7 Ref.8 Ref.9
	Modified residue	185	1	Phosphothreonine Ref.8
Experimental info
	Sequence conflict	100	1	E → G in AAA34581. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P16550 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: A1273537D91482A5	FASTA	321	36,493
	10 20 30 40 50 60 MSIPADIASL ISDKYKSAFD NGNLKFIQTE TTKTKDPKTS MPYLISHMPS LIEKPERGQT 70 80 90 100 110 120 PEGEDPLGKP EEELTVIPEF GGADNKAYKL LLNKFPVIPE HTLLVTNEYQ HQTDALTPTD 130 140 150 160 170 180 LLTAYKLLCA LDNEESDKRH MVFYNSGPAS GSSLDHKHLQ ILQMPEKFVT FQDRLCNGKE 190 200 210 220 230 240 HFLPTFNTEP LQDAKVSFAH FVLPMPESEE TVDEDLLAMC YISILQRALT FFQDWLNENP 250 260 270 280 290 300 ELKKSYNLML TKEWICVVPR SKAFSDEMKI GFNSTGYCGM ILTKNDEVFS KITEKPELIN 310 320 DILLECGFPN TSGQKPNEYN Y

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequencing and enhanced expression of the gene encoding diadenosine 5',5'''-P1,P4-tetraphosphate (Ap4A) phosphorylase in Saccharomyces cerevisiae." Kaushal V., Avila D.M., Hardies S.C., Barnes L.D. Gene 95:79-84(1990) [PubMed: 2174812] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Isolation, characterization, and inactivation of the APA1 gene encoding yeast diadenosine 5',5'''-P1,P4-tetraphosphate phosphorylase." Plateau P., Fromant M., Schmitter J.-M., Buhler J.-M., Blanquet S. J. Bacteriol. 171:6437-6445(1989) [PubMed: 2556364] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 15-33 AND 39-321.
[3]	"The complete DNA sequence of yeast chromosome III." Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M. , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G. Nature 357:38-46(1992) [PubMed: 1574125] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	Mewes H.-W. Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 100.
[5]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[6]	"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].
[7]	"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: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-60, MASS SPECTROMETRY. Strain: ADR376.
[8]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-60 AND THR-185, MASS SPECTROMETRY.
[9]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-60, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M35204 Genomic DNA. Translation: AAA34581.1. M31791 Genomic DNA. Translation: AAA34427.1. X59720 Genomic DNA. Translation: CAA42394.2. BK006937 Genomic DNA. Translation: DAA07435.1.
PIR	XXBYP1. S12946.
RefSeq	NP_009880.2. NM_001178695.1.
3D structure databases
ProteinModelPortal	P16550.
SMR	P16550. Positions 84-166.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-5139N.
IntAct	P16550. 64 interactions.
MINT	MINT-561161.
STRING	P16550.
Proteomic databases
PeptideAtlas	P16550.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YCL050C; YCL050C; YCL050C.
GeneID	850307.
KEGG	sce:YCL050C.
NMPDR	fig|4932.3.peg.600.
Organism-specific databases
SGD	S000000555. APA1.
Phylogenomic databases
eggNOG	fuNOG08020.
GeneTree	EFGT00050000003278.
HOGENOM	HBG397523.
OrthoDB	EOG4WDHMW.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-12462.
Gene expression databases
ArrayExpress	P16550.
Genevestigator	P16550.
GermOnline	YCL050C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR009163. ATP_adenylyltransferase. IPR019200. ATP_adenylylTrfase_C. IPR011146. His_triad-like_motif. IPR011151. His_triad_motif. [Graphical view]
Gene3D	G3DSA:3.30.428.10. His_triad_motif. 1 hit.
KO	K00959. K00988.
Pfam	PF09830. ATP_transf. 1 hit. [Graphical view]
PIRSF	PIRSF000846. ATP_adenylyltr. 1 hit.
SUPFAM	SSF54197. His_triad-like_motif. 1 hit.
ProtoNet	Search...
Other
NextBio	965697.

Entry information

Entry name

APA1_YEAST

Accession

Primary (citable) accession number: P16550
Secondary accession number(s): D6VQW6

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	January 23, 2007
Last modified:	December 14, 2011
This is version 109 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program