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Protein

Aspartate aminotransferase, cytoplasmic

Gene

AAT2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a key role in amino acid metabolism.

Catalytic activityi

L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate.3 Publications

Cofactori

pyridoxal 5'-phosphate2 Publications

Kineticsi

  1. KM=0.11 mM for L-aspartate1 Publication
  2. KM=20 mM for L-glutamate1 Publication
  3. KM=0.006 mM for oxaloacetate1 Publication
  4. KM=0.16 mM for 2-oxoglutarate1 Publication

pH dependencei

Optimum pH is 8-9.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei38 – 381Aspartate; via amide nitrogen1 Publication
Binding sitei135 – 1351Aspartate1 Publication
Binding sitei188 – 1881Aspartate1 Publication
Binding sitei387 – 3871Aspartate1 Publication

GO - Molecular functioni

  1. L-aspartate:2-oxoglutarate aminotransferase activity Source: UniProtKB
  2. L-phenylalanine:2-oxoglutarate aminotransferase activity Source: UniProtKB-EC
  3. pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  1. 2-oxoglutarate metabolic process Source: UniProtKB
  2. aspartate biosynthetic process Source: SGD
  3. aspartate metabolic process Source: UniProtKB
  4. glutamate metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13013.
YEAST:YLR027C-MONOMER.
ReactomeiREACT_286539. Gluconeogenesis.
REACT_288999. Amino acid synthesis and interconversion (transamination).
REACT_350157. Methionine salvage pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartate aminotransferase, cytoplasmic (EC:2.6.1.1)
Alternative name(s):
Transaminase A
Gene namesi
Name:AAT2
Synonyms:ASP5
Ordered Locus Names:YLR027C
ORF Names:L1746
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR027C.
SGDiS000004017. AAT2.

Subcellular locationi

  1. Cytoplasm 1 Publication
  2. Peroxisome 1 Publication

  3. Note: Targeted to peroxisomes in cells grown in oleate.

GO - Cellular componenti

  1. cytosol Source: SGD
  2. peroxisome Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 418417Aspartate aminotransferase, cytoplasmicPRO_0000123875Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications
Modified residuei255 – 2551N6-(pyridoxal phosphate)lysine1 Publication
Modified residuei389 – 3891Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP23542.
PaxDbiP23542.
PeptideAtlasiP23542.

Expressioni

Gene expression databases

GenevestigatoriP23542.

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

BioGridi31301. 178 interactions.
DIPiDIP-2897N.
IntActiP23542. 12 interactions.
MINTiMINT-701237.
STRINGi4932.YLR027C.

Structurei

Secondary structure

1
418
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni3 – 86Combined sources
Helixi18 – 258Combined sources
Helixi51 – 6111Combined sources
Helixi77 – 8812Combined sources
Helixi93 – 964Combined sources
Beta strandi100 – 1067Combined sources
Helixi107 – 12216Combined sources
Beta strandi128 – 1336Combined sources
Helixi138 – 1436Combined sources
Turni144 – 1463Combined sources
Beta strandi149 – 1535Combined sources
Turni157 – 1604Combined sources
Helixi164 – 17310Combined sources
Beta strandi179 – 1835Combined sources
Turni188 – 1903Combined sources
Helixi196 – 20813Combined sources
Beta strandi212 – 2187Combined sources
Turni220 – 2223Combined sources
Beta strandi223 – 2253Combined sources
Helixi227 – 2304Combined sources
Helixi232 – 2409Combined sources
Turni241 – 2444Combined sources
Beta strandi247 – 2526Combined sources
Turni254 – 2563Combined sources
Helixi260 – 2623Combined sources
Beta strandi264 – 2707Combined sources
Helixi277 – 29317Combined sources
Turni294 – 2963Combined sources
Helixi301 – 31212Combined sources
Helixi314 – 34532Combined sources
Helixi353 – 3564Combined sources
Beta strandi359 – 3635Combined sources
Helixi368 – 37811Combined sources
Beta strandi386 – 3894Combined sources
Helixi390 – 3923Combined sources
Turni395 – 3973Combined sources
Helixi398 – 41114Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YAAX-ray2.05A/B/C/D2-412[»]
ProteinModelPortaliP23542.
SMRiP23542. Positions 2-412.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23542.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1448.
GeneTreeiENSGT00390000014081.
HOGENOMiHOG000185898.
InParanoidiP23542.
KOiK14454.
OMAiDSAIWIG.
OrthoDBiEOG793BHW.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
InterProiIPR004839. Aminotransferase_I/II.
IPR000796. Asp_trans.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PANTHERiPTHR11879. PTHR11879. 1 hit.
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
PRINTSiPR00799. TRANSAMINASE.
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P23542-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSATLFNNIE LLPPDALFGI KQRYGQDQRA TKVDLGIGAY RDDNGKPWVL
60 70 80 90 100
PSVKAAEKLI HNDSSYNHEY LGITGLPSLT SNAAKIIFGT QSDAFQEDRV
110 120 130 140 150
ISVQSLSGTG ALHISAKFFS KFFPDKLVYL SKPTWANHMA IFENQGLKTA
160 170 180 190 200
TYPYWANETK SLDLNGFLNA IQKAPEGSIF VLHSCAHNPT GLDPTSEQWV
210 220 230 240 250
QIVDAIASKN HIALFDTAYQ GFATGDLDKD AYAVRLGVEK LSTVSPVFVC
260 270 280 290 300
QSFAKNAGMY GERVGCFHLA LTKQAQNKTI KPAVTSQLAK IIRSEVSNPP
310 320 330 340 350
AYGAKIVAKL LETPELTEQW HKDMVTMSSR ITKMRHALRD HLVKLGTPGN
360 370 380 390 400
WDHIVNQCGM FSFTGLTPQM VKRLEETHAV YLVASGRASI AGLNQGNVEY
410
VAKAIDEVVR FYTIEAKL
Length:418
Mass (Da):46,058
Last modified:January 23, 2007 - v3
Checksum:iD25F40F6C6DD2B33
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti95 – 951F → L AA sequence (PubMed:2199266).Curated
Sequence conflicti95 – 951F → L AA sequence (PubMed:1859361).Curated
Sequence conflicti413 – 4142TI → AT AA sequence (PubMed:2199266).Curated
Sequence conflicti413 – 4142TI → AT AA sequence (PubMed:1859361).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z73199 Genomic DNA. Translation: CAA97550.1. Different initiation.
BK006945 Genomic DNA. Translation: DAA09345.1.
PIRiS64854.
RefSeqiNP_013127.2. NM_001181914.1.

Genome annotation databases

EnsemblFungiiYLR027C; YLR027C; YLR027C.
GeneIDi850714.
KEGGisce:YLR027C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z73199 Genomic DNA. Translation: CAA97550.1. Different initiation.
BK006945 Genomic DNA. Translation: DAA09345.1.
PIRiS64854.
RefSeqiNP_013127.2. NM_001181914.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YAAX-ray2.05A/B/C/D2-412[»]
ProteinModelPortaliP23542.
SMRiP23542. Positions 2-412.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31301. 178 interactions.
DIPiDIP-2897N.
IntActiP23542. 12 interactions.
MINTiMINT-701237.
STRINGi4932.YLR027C.

Proteomic databases

MaxQBiP23542.
PaxDbiP23542.
PeptideAtlasiP23542.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR027C; YLR027C; YLR027C.
GeneIDi850714.
KEGGisce:YLR027C.

Organism-specific databases

EuPathDBiFungiDB:YLR027C.
SGDiS000004017. AAT2.

Phylogenomic databases

eggNOGiCOG1448.
GeneTreeiENSGT00390000014081.
HOGENOMiHOG000185898.
InParanoidiP23542.
KOiK14454.
OMAiDSAIWIG.
OrthoDBiEOG793BHW.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13013.
YEAST:YLR027C-MONOMER.
ReactomeiREACT_286539. Gluconeogenesis.
REACT_288999. Amino acid synthesis and interconversion (transamination).
REACT_350157. Methionine salvage pathway.

Miscellaneous databases

EvolutionaryTraceiP23542.
NextBioi966778.
PROiP23542.

Gene expression databases

GenevestigatoriP23542.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
InterProiIPR004839. Aminotransferase_I/II.
IPR000796. Asp_trans.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PANTHERiPTHR11879. PTHR11879. 1 hit.
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
PRINTSiPR00799. TRANSAMINASE.
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: ENZYME ACTIVITY, SUBCELLULAR LOCATION.
  7. 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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  10. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH PYRODOXAL PHOSPHATE AND MALEIC ACID, COFACTOR, PYRIDOXAL PHOSPHATE AT LYS-255, SUBUNIT.

Entry informationi

Entry nameiAATC_YEAST
AccessioniPrimary (citable) accession number: P23542
Secondary accession number(s): D6VY29
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: January 23, 2007
Last modified: April 29, 2015
This is version 152 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

In eukaryotes there are cytoplasmic, mitochondrial and chloroplastic isozymes.
Present with 7700 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.