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P23542 (AATC_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length418 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a key role in amino acid metabolism.

Catalytic activity

L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate. Ref.4 Ref.5 Ref.6

Cofactor

Pyridoxal phosphate. Ref.5 Ref.9

Subunit structure

Homodimer. Ref.5 Ref.9

Subcellular location

Cytoplasm. Peroxisome. Note: Targeted to peroxisomes in cells grown in oleate. Ref.6

Miscellaneous

In eukaryotes there are cytoplasmic, mitochondrial and chloroplastic isozymes.

Present with 7700 molecules/cell in log phase SD medium. Ref.7

Sequence similarities

Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.

Biophysicochemical properties

Kinetic parameters:

KM=0.11 mM for L-aspartate Ref.5

KM=20 mM for L-glutamate

KM=0.006 mM for oxaloacetate

KM=0.16 mM for 2-oxoglutarate

pH dependence:

Optimum pH is 8-9.

Sequence caution

The sequence CAA97550.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3 Ref.4
Chain2 – 418417Aspartate aminotransferase, cytoplasmic
PRO_0000123875

Sites

Binding site381Aspartate; via amide nitrogen
Binding site1351Aspartate
Binding site1881Aspartate
Binding site3871Aspartate

Amino acid modifications

Modified residue21N-acetylserine Ref.4
Modified residue2551N6-(pyridoxal phosphate)lysine
Modified residue3891Phosphoserine Ref.8

Experimental info

Sequence conflict951F → L AA sequence Ref.3
Sequence conflict951F → L AA sequence Ref.4
Sequence conflict413 – 4142TI → AT AA sequence Ref.3
Sequence conflict413 – 4142TI → AT AA sequence Ref.4

Secondary structure

1 .................................................................... 418
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P23542 [UniParc].

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

FASTA41846,058
        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

References

« Hide '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. expand/collapse author list , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., 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]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"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.
[4]"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, ACETYLATION AT SER-2, ENZYME ACTIVITY.
[5]"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.
[6]"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.
[7]"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].
[8]"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.
[9]"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) IN COMPLEX WITH PYRODOXAL PHOSPHATE AND MALEIC ACID, COFACTOR, PYRIDOXAL PHOSPHATE AT LYS-255, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z73199 Genomic DNA. Translation: CAA97550.1. Different initiation.
BK006945 Genomic DNA. Translation: DAA09345.1.
PIRS64854.
RefSeqNP_013127.2. NM_001181914.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1YAAX-ray2.05A/B/C/D2-412[»]
ProteinModelPortalP23542.
SMRP23542. Positions 2-412.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-2897N.
IntActP23542. 14 interactions.
MINTMINT-701237.
STRINGP23542.

Proteomic databases

PeptideAtlasP23542.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYLR027C; YLR027C; YLR027C.
GeneID850714.
KEGGsce:YLR027C.
NMPDRfig|4932.3.peg.4118.

Organism-specific databases

SGDS000004017. AAT2.

Phylogenomic databases

eggNOGfuNOG05116.
GeneTreeEFGT00050000000248.
HOGENOMHBG446828.
OMARTCASRL.
OrthoDBEOG4BP4M8.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-13013.

Gene expression databases

ArrayExpressP23542.
GenevestigatorP23542.
GermOnlineYLR027C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR004839. Aminotransferase_I/II.
IPR000796. Asp_trans.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
IPR015424. PyrdxlP-dep_Trfase_major_dom.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
KOK14454.
PANTHERPTHR11879. Asp_trans. 1 hit.
PfamPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
PRINTSPR00799. TRANSAMINASE.
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
PROSITEPS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio966778.

Entry information

Entry nameAATC_YEAST
AccessionPrimary (citable) accession number: P23542
Secondary accession number(s): D6VY29
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 121 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents