Aspartate aminotransferase, cytoplasmic - Saccharomyces cerevisiae (Baker's yeast)

Names and origin

Protein names

Recommended name:
    Aspartate aminotransferase, cytoplasmic
    EC=2.6.1.1
Alternative name(s):
    Transaminase A

Gene names

Name:	AAT2
Synonyms:	ASP5
Ordered Locus Names:	YLR027C
ORF Names:	L1746

Organism

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

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

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

Hide | Top

Protein attributes

Sequence length	418 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

Hide | Top

General annotation (Comments)

Catalytic activity	L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate. Ref.3 Ref.4 Ref.5
Cofactor	Pyridoxal phosphate. Ref.4
Subunit structure	Homodimer. Ref.4
Subcellular location	Cytoplasm. Peroxisome. Note: Targeted to peroxisomes in cells grown in oleate. Ref.5
Post-translational modification	The N-terminus is blocked.
Miscellaneous	In eukaryotes there are cytoplasmic, mitochondrial and chloroplastic isozymes. Present with 7700 molecules/cell in log phase SD medium. Ref.6
Sequence similarities	Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.
biophysicochemical properties	Kinetic parameters: K_M=0.11 mM for L-aspartate K_M=20 mM for L-glutamate K_M=0.006 mM for oxaloacetate K_M=0.16 mM for 2-oxoglutarate pH dependence: Optimum pH is 8-9.

Hide | Top

Ontologies

Keywords
Cellular component	Cytoplasm Peroxisome
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	aspartate biosynthetic process Ref.5 Inferred from mutant phenotype. Source: SGD
Cellular component	cytosol Ref.5 Inferred from direct assay. Source: SGD peroxisome Ref.5 Inferred from direct assay. Source: SGD
Molecular function	L-aspartate:2-oxoglutarate aminotransferase activity Ref.3 Ref.5 Inferred from direct assay. Source: SGD protein binding Inferred from physical interaction. Source: IntAct pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Hide | Top

Binary interactions

With	Entry	#Exp.	IntAct
	P43582	1	EBI-2002,EBI-22766
ADE16	P54113	1	EBI-2002,EBI-14213
CDC11	P32458	1	EBI-2002,EBI-4178
ESS1	P22696	1	EBI-2002,EBI-6679
INO1	P11986	1	EBI-2002,EBI-9257
LSP1	Q12230	1	EBI-2002,EBI-34978
MLS1	P30952	1	EBI-2002,EBI-10428
PRP40	P33203	1	EBI-2002,EBI-701
SSM4	P40318	1	EBI-2002,EBI-18208
URA7	P28274	1	EBI-2002,EBI-20128
VID30	P53076	1	EBI-2002,EBI-24173

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

Removed Ref.3 Ref.2

Chain

2 – 418

417

Aspartate aminotransferase, cytoplasmic

PRO_0000123875

Amino acid modifications

Modified residue

2

1

N-acetylserine

Modified residue

255

1

N6-(pyridoxal phosphate)lysine

Modified residue

389

1

Phosphoserine Ref.7

Experimental info

Sequence conflict

95

1

F → L Ref.2

Sequence conflict

95

1

F → L Ref.3

Sequence conflict

413 – 414

2

TI → AT Ref.2

Sequence conflict

413 – 414

2

TI → AT Ref.3

Secondary structure

1

.

418

Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

P23542-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: D25F40F6C6DD2B33
Show »

FASTA

418

46,058

        10         20         30         40         50         60 
MSATLFNNIE LLPPDALFGI KQRYGQDQRA TKVDLGIGAY RDDNGKPWVL PSVKAAEKLI 

        70         80         90        100        110        120 
HNDSSYNHEY LGITGLPSLT SNAAKIIFGT QSDAFQEDRV ISVQSLSGTG ALHISAKFFS 

       130        140        150        160        170        180 
KFFPDKLVYL SKPTWANHMA IFENQGLKTA TYPYWANETK SLDLNGFLNA IQKAPEGSIF 

       190        200        210        220        230        240 
VLHSCAHNPT GLDPTSEQWV QIVDAIASKN HIALFDTAYQ GFATGDLDKD AYAVRLGVEK 

       250        260        270        280        290        300 
LSTVSPVFVC QSFAKNAGMY GERVGCFHLA LTKQAQNKTI KPAVTSQLAK IIRSEVSNPP 

       310        320        330        340        350        360 
AYGAKIVAKL LETPELTEQW HKDMVTMSSR ITKMRHALRD HLVKLGTPGN WDHIVNQCGM 

       370        380        390        400        410 
FSFTGLTPQM VKRLEETHAV YLVASGRASI AGLNQGNVEY VAKAIDEVVR FYTIEAKL

« Hide

Hide | Top

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII." Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. Hoheisel J.D. Nature 387:87-90(1997) [PubMed: 9169871] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	"Amino acid sequences of aspartate aminotransferases: the cytosolic isoenzymes from yeast and from human liver." Cronin V.B., Doyle J.M., Doonan S. Biochem. Soc. Trans. 18:256-256(1990) [PubMed: 2199266] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-418.
[3]	"The amino acid sequence of the aspartate aminotransferase from baker's yeast (Saccharomyces cerevisiae)." Cronin V.B., Maras B., Barra D., Doonan S. Biochem. J. 277:335-340(1991) [PubMed: 1859361] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-418, ENZYME ACTIVITY.
[4]	"Aspartate: 2-oxoglutarate aminotransferase from bakers' yeast: crystallization and characterization." Yagi T., Kagamiyama H., Nozaki M. J. Biochem. 92:35-43(1982) [PubMed: 6811576] [Abstract] Cited for: CRYSTALLIZATION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
[5]	"Cytosolic aspartate aminotransferase encoded by the AAT2 gene is targeted to the peroxisomes in oleate-grown Saccharomyces cerevisiae." Verleur N., Elgersma Y., Van Roermund C.W., Tabak H.F., Wanders R.J. Eur. J. Biochem. 247:972-980(1997) [PubMed: 9288922] [Abstract] Cited for: ENZYME ACTIVITY, SUBCELLULAR LOCATION.
[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]	"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 SER-389, MASS SPECTROMETRY.
[8]	"Crystal structure of Saccharomyces cerevisiae cytosolic aspartate aminotransferase." Jeffery C.J., Barry T., Doonan S., Petsko G.A., Ringe D. Protein Sci. 7:1380-1387(1998) [PubMed: 9655342] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS).
+	Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases

Z73199 Genomic DNA. Translation: CAA97550.1. Different initiation.

PIR

S64854.

RefSeq

NP_013127.2.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1YAA	X-ray	2.05	A/B/C/D	2-412	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:2897N.

IntAct

P23542. 25 interactions.

Proteomic databases

PeptideAtlas

P23542.

PRIDE

P23542.

Genome annotation databases

Ensembl

YLR027C. Saccharomyces cerevisiae. [Contig view]

GeneID

850714.

GenomeReviews

Gene locus YLR027C in contig Y13138_GR.

KEGG

sce:YLR027C.

NMPDR

fig|4932.3.peg.4118.

Organism-specific databases

CYGD

YLR027c.

SGD

S000004017. AAT2.

Yeast-GFP

Search...

Phylogenomic databases

HOGENOM

P23542.

OMA

P23542. VLLMRAQ.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-13013.

BRENDA

2.6.1.1. 250.

Gene expression databases

ArrayExpress

P23542.

GermOnline

YLR027C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR004839. Aminotrans_I/II.
IPR000796. Asp_trans.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]

Gene3D

G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.

PANTHER

PTHR11879. Asp_trans. 1 hit.

Pfam

PF00155. Aminotran_1_2. 1 hit.
[Graphical view]

PRINTS

PR00799. TRANSAMINASE.

PROSITE

PS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

966778.

Hide | Top

Entry information

Entry name

AATC_YEAST

Accession

Primary (citable) accession number: P23542

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 91 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

Hide | Top

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Yeast

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

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Experimental info

Secondary structure

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