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

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P10869 (AK_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 124. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Aspartokinase
EC=2.7.2.4

Alternative name(s):
Aspartate kinase

Gene names

Name:	HOM3
Ordered Locus Names:	YER052C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	527 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	ATP + L-aspartate = ADP + 4-phospho-L-aspartate.
Pathway	Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4. Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 1/3. Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 1/5.
Miscellaneous	Present with 48100 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the aspartokinase family. Contains 2 ACT domains.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Threonine biosynthesis
Domain	Repeat
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	homoserine biosynthetic process Inferred from mutant phenotype PubMed 4380684. Source: SGD lysine biosynthetic process via diaminopimelate Inferred from electronic annotation. Source: UniProtKB-UniPathway methionine biosynthetic process Inferred from mutant phenotype PubMed 4380684. Source: SGD threonine biosynthetic process Inferred from direct assay PubMed 18626862. Source: SGD
Cellular_component	cytoplasm Inferred from direct assay PubMed 14562095. Source: SGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW aspartate kinase activity Inferred from direct assay PubMed 18626862. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
FPR1	P20081	5	EBI-2430,EBI-6961

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 527

527

Aspartokinase

PRO_0000066690

Regions

Domain

363 – 433

ACT 1

Domain

438 – 506

ACT 2

Amino acid modifications

Modified residue

333

Phosphothreonine Ref.6 Ref.7 Ref.8

Modified residue

441

Phosphoserine Ref.8

Sequences

Sequence

Length

Mass (Da)

Tools

P10869 [UniParc].

Last modified August 1, 1990. Version 2.
Checksum: D4D28FB8D4374898
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FASTA

527

58,110

        10         20         30         40         50         60 
MPMDFQPTSS HSNWVVQKFG GTSVGKFPVQ IVDDIVKHYS KPDGPNNNVA VVCSARSSYT 

        70         80         90        100        110        120 
KAEGTTSRLL KCCDLASQES EFQDIIEVIR QDHIDNADRF ILNPALQAKL VDDTNKELEL 

       130        140        150        160        170        180 
VKKYLNASKV LGEVSSRTVD LVMSCGEKLS CLFMTALCND RGCKAKYVDL SHIVPSDFSA 

       190        200        210        220        230        240 
SALDNSFYTF LVQALKEKLA PFVSAKERIV PVFTGFFGLV PTGLLNGVGR GYTDLCAALI 

       250        260        270        280        290        300 
AVAVNADELQ VWKEVDGIFT ADPRKVPEAR LLDSVTPEEA SELTYYGSEV IHPFTMEQVI 

       310        320        330        340        350        360 
RAKIPIRIKN VQNPLGNGTI IYPDNVAKKG ESTPPHPPEN LSSSFYEKRK RGATAITTKN 

       370        380        390        400        410        420 
DIFVINIHSN KKTLSHGFLA QIFTILDKYK LVVDLISTSE VHVSMALPIP DADSLKSLRQ 

       430        440        450        460        470        480 
AEEKLRILGS VDITKKLSIV SLVGKHMKQY IGIAGTMFTT LAEEGINIEM ISQGANEINI 

       490        500        510        520 
SCVINESDSI KALQCIHAKL LSERTNTSNQ FEHAIDERLE QLKRLGI

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure of the yeast HOM3 gene which encodes aspartokinase." Rafalski J.A., Falco S.C. J. Biol. Chem. 263:2146-2151(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Structure of the yeast HOM3 gene which encodes aspartokinase." Rafalski J.A., Falco S.C. J. Biol. Chem. 265:15346-15346(1990) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION.
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome V." Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. Davis R.W. Nature 387:78-81(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"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] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[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 THR-333, MASS SPECTROMETRY. 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 THR-333, MASS SPECTROMETRY.
[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 THR-333 AND SER-441, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J03526 Genomic DNA. Translation: AAA34681.1. U18796 Genomic DNA. Translation: AAB64587.1. BK006939 Genomic DNA. Translation: DAA07708.1.
PIR	KIBYD. A35888.
RefSeq	NP_010972.1. NM_001178943.1.
3D structure databases
ProteinModelPortal	P10869.
SMR	P10869. Positions 16-501.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1319N.
IntAct	P10869. 10 interactions.
MINT	MINT-392511.
STRING	4932.YER052C.
Proteomic databases
PaxDb	P10869.
PeptideAtlas	P10869.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YER052C; YER052C; YER052C.
GeneID	856778.
KEGG	sce:YER052C.
Organism-specific databases
CYGD	YER052c.
SGD	S000000854. HOM3.
Phylogenomic databases
eggNOG	COG0527.
HOGENOM	HOG000293094.
KO	K00928.
OMA	TWIEREK.
OrthoDB	EOG4GTPNQ.
Enzyme and pathway databases
BRENDA	2.7.2.4. 984.
SABIO-RK	P10869.
UniPathway	UPA00034; UER00015. UPA00050; UER00461. UPA00051; UER00462.
Gene expression databases
Genevestigator	P10869.
GermOnline	YER052C. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	3.40.1160.10. 2 hits.
InterPro	IPR001048. Asp/Glu/Uridylate_kinase. IPR001341. Asp_kinase_dom. IPR018042. Aspartate_kinase_CS. [Graphical view]
Pfam	PF00696. AA_kinase. 1 hit. [Graphical view]
SUPFAM	SSF53633. Aa_kinase. 1 hit.
TIGRFAMs	TIGR00657. asp_kinases. 1 hit.
PROSITE	PS00324. ASPARTOKINASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	982982.

Entry information

Entry name

AK_YEAST

Accession

Primary (citable) accession number: P10869
Secondary accession number(s): D3DLV4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	August 1, 1990
Last modified:	May 1, 2013
This is version 124 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome V

Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents