Aspartokinase - Saccharomyces cerevisiae (Baker's yeast)

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Reviewed, UniProtKB/Swiss-Prot P10869 (AK_YEAST)

Last modified February 9, 2010. Version 93. History...

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

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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 (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

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

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Protein attributes

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

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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. Ref.4
Sequence similarities	Belongs to the aspartokinase family. Contains 2 ACT domains.

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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
Gene Ontology (GO)
Biological process	methionine metabolic process Traceable author statement. Source: SGD response to drug Inferred from mutant phenotype. Source: SGD threonine biosynthetic process Inferred from direct assay. Source: SGD
Cellular component	cytoplasm Inferred from direct assay. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW amino acid binding Inferred from electronic annotation. Source: InterPro aspartate kinase activity Inferred from direct assay. Source: SGD protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
FPR1	P20081	3	EBI-2430,EBI-6961

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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.5 Ref.6 Ref.7

Modified residue

441

Phosphoserine Ref.7

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Sequences

Sequence

Length

Mass (Da)

Tools

P10869-1 [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

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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: 2892836] [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: 2168408] [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: 9169868] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	"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].
[5]	"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-333, MASS SPECTROMETRY.
[6]	"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: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-333, MASS SPECTROMETRY.
[7]	"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-333 AND SER-441, MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
EMBL GenBank DDBJ	J03526 Genomic DNA. Translation: AAA34681.1. U18796 Genomic DNA. Translation: AAB64587.1.
PIR	KIBYD. A35888.
RefSeq	NP_010972.1.
3D structure databases
SMR	P10869. Positions 15-502.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1319N.
IntAct	P10869. 14 interactions.
STRING	P10869.
Proteomic databases
PeptideAtlas	P10869.
PRIDE	P10869.
Genome annotation databases
Ensembl	YER052C; YER052C; YER052C; Saccharomyces cerevisiae. [Genome view]
GeneID	856778.
KEGG	sce:YER052C.
NMPDR	fig\|4932.3.peg.2035.
Organism-specific databases
CYGD	YER052c.
SGD	S000000854. HOM3.
Phylogenomic databases
eggNOG	fuNOG04731.
HOGENOM	HBG724395.
OMA	FLAHIFT.
OrthoDB	EOG9W9KM6.
PhylomeDB	P10869.
Enzyme and pathway databases
BRENDA	2.7.2.4. 250.
Gene expression databases
ArrayExpress	P10869.
Genevestigator	P10869.
GermOnline	YER052C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR002912. ACT_bd. IPR001048. Asp/Glu/Uridylate_kinase. IPR001341. Asp_kinase_dom. IPR018042. Aspartate_kinase_CS. [Graphical view]
Gene3D	G3DSA:3.40.1160.10. Aa_kinase. 1 hit.
Pfam	PF00696. AA_kinase. 1 hit. PF01842. ACT. 1 hit. [Graphical view]
TIGRFAMs	TIGR00657. asp_kinases. 1 hit.
PROSITE	PS00324. ASPARTOKINASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	982982.

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Entry information

Entry name

AK_YEAST

Accession

Primary (citable) accession number: P10869

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	August 1, 1990
Last modified:	February 9, 2010
This is version 93 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Yeast

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

Yeast chromosome V

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

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

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents