Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P23542

- AATC_YEAST

UniProt

P23542 - AATC_YEAST

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Aspartate aminotransferase, cytoplasmic

Gene

AAT2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - 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 phosphate.2 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_189018. 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: Chromosome XII

Organism-specific databases

SGDiS000004017. AAT2.

Subcellular locationi

Cytoplasm 1 Publication. Peroxisome 1 Publication
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 – 86
Helixi18 – 258
Helixi51 – 6111
Helixi77 – 8812
Helixi93 – 964
Beta strandi100 – 1067
Helixi107 – 12216
Beta strandi128 – 1336
Helixi138 – 1436
Turni144 – 1463
Beta strandi149 – 1535
Turni157 – 1604
Helixi164 – 17310
Beta strandi179 – 1835
Turni188 – 1903
Helixi196 – 20813
Beta strandi212 – 2187
Turni220 – 2223
Beta strandi223 – 2253
Helixi227 – 2304
Helixi232 – 2409
Turni241 – 2444
Beta strandi247 – 2526
Turni254 – 2563
Helixi260 – 2623
Beta strandi264 – 2707
Helixi277 – 29317
Turni294 – 2963
Helixi301 – 31212
Helixi314 – 34532
Helixi353 – 3564
Beta strandi359 – 3635
Helixi368 – 37811
Beta strandi386 – 3894
Helixi390 – 3923
Turni395 – 3973
Helixi398 – 41114

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.
OMAiSSRIRQM.
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.

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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
Z73199 Genomic DNA. Translation: CAA97550.1 . Different initiation.
BK006945 Genomic DNA. Translation: DAA09345.1 .
PIRi S64854.
RefSeqi NP_013127.2. NM_001181914.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1YAA X-ray 2.05 A/B/C/D 2-412 [» ]
ProteinModelPortali P23542.
SMRi P23542. Positions 2-412.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 31301. 178 interactions.
DIPi DIP-2897N.
IntActi P23542. 12 interactions.
MINTi MINT-701237.
STRINGi 4932.YLR027C.

Proteomic databases

MaxQBi P23542.
PaxDbi P23542.
PeptideAtlasi P23542.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YLR027C ; YLR027C ; YLR027C .
GeneIDi 850714.
KEGGi sce:YLR027C.

Organism-specific databases

SGDi S000004017. AAT2.

Phylogenomic databases

eggNOGi COG1448.
GeneTreei ENSGT00390000014081.
HOGENOMi HOG000185898.
InParanoidi P23542.
KOi K14454.
OMAi SSRIRQM.
OrthoDBi EOG793BHW.

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-13013.
YEAST:YLR027C-MONOMER.
Reactomei REACT_189018. Methionine salvage pathway.

Miscellaneous databases

EvolutionaryTracei P23542.
NextBioi 966778.
PROi P23542.

Gene expression databases

Genevestigatori P23542.

Family and domain databases

Gene3Di 3.40.640.10. 1 hit.
InterProi IPR004839. Aminotransferase_I/II.
IPR000796. Asp_trans.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view ]
PANTHERi PTHR11879. PTHR11879. 1 hit.
Pfami PF00155. Aminotran_1_2. 1 hit.
[Graphical view ]
PRINTSi PR00799. TRANSAMINASE.
SUPFAMi SSF53383. SSF53383. 1 hit.
PROSITEi PS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

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].
  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: October 29, 2014
This is version 147 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