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UniProtKB/Swiss-Prot entry P23542


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name AATC_YEAST
Primary accession number P23542
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1991
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 84)
Name and origin of the protein
Protein name Aspartate aminotransferase, cytoplasmic
Synonyms EC 2.6.1.1
Transaminase A
Gene name
Name: AAT2
Synonyms: ASP5
OrderedLocusNames: YLR027C
ORFNames: L1746
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=9169871 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
Nature 387:87-90(1997).
[2]
PROTEIN SEQUENCE OF 2-418.
PubMed=2199266 [NCBI, ExPASy, EBI, Israel, Japan]
Cronin V.B., Doyle J.M., Doonan S.;
"Amino acid sequences of aspartate aminotransferases: the cytosolic isoenzymes from yeast and from human liver.";
Biochem. Soc. Trans. 18:256-256(1990).
[3]
PROTEIN SEQUENCE OF 2-418, AND ENZYME ACTIVITY.
PubMed=1859361 [NCBI, ExPASy, EBI, Israel, Japan]
Cronin V.B., Maras B., Barra D., Doonan S.;
"The amino acid sequence of the aspartate aminotransferase from baker's yeast (Saccharomyces cerevisiae).";
Biochem. J. 277:335-340(1991).
[4]
CRYSTALLIZATION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
PubMed=6811576 [NCBI, ExPASy, EBI, Israel, Japan]
Yagi T., Kagamiyama H., Nozaki M.;
"Aspartate: 2-oxoglutarate aminotransferase from bakers' yeast: crystallization and characterization.";
J. Biochem. 92:35-43(1982).
[5]
ENZYME ACTIVITY, AND SUBCELLULAR LOCATION.
DOI=10.1111/j.1432-1033.1997.00972.x; PubMed=9288922 [NCBI, ExPASy, EBI, Israel, Japan]
Verleur N., Elgersma Y., Van Roermund C.W., Tabak H.F., Wanders R.J.;
"Cytosolic aspartate aminotransferase encoded by the AAT2 gene is targeted to the peroxisomes in oleate-grown Saccharomyces cerevisiae.";
Eur. J. Biochem. 247:972-980(1997).
[6]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0607084104; PubMed=17287358 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[8]
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS).
PubMed=9655342 [NCBI, ExPASy, EBI, Israel, Japan]
Jeffery C.J., Barry T., Doonan S., Petsko G.A., Ringe D.;
"Crystal structure of Saccharomyces cerevisiae cytosolic aspartate aminotransferase.";
Protein Sci. 7:1380-1387(1998).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Z73199; CAA97550.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S64854; S64854.
RefSeq NP_013127.2; -.
3D structure databases
PDB
1YAA; X-ray; 2.05 A; A/B/C/D=1-412.[ExPASy / RCSB / EBI]
PDBsum 1YAA; -.
ModBase P23542.
Protein-protein interaction databases
DIP DIP:2897N; -.
IntAct P23542; -.
Enzyme and pathway databases
BioCyc MetaCyc:MON-13013; -.
Organism-specific databases
CYGD YLR027c; -.
SGD S000004017; AAT2.
Yeast-GFP YLR027C.
Gene expression databases
ArrayExpress P23542; -.
GermOnline YLR027C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from direct assay from SGD).
GO:0005777; Cellular component: peroxisome (inferred from electronic annotation from UniProtKB-KW).
GO:0004069; Molecular function: aspartate transaminase activity (inferred from electronic annotation from EC).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0030170; Molecular function: pyridoxal phosphate binding (inferred from electronic annotation from InterPro).
GO:0006532; Biological process: aspartate biosynthetic process (inferred from mutant phenotype from SGD).
QuickGo view.
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 of domain structure.
Gene3D G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1.
PANTHER PTHR11879; Asp_trans; 1.
Pfam PF00155; Aminotran_1_2; 1.
Pfam graphical view of domain structure.
PRINTS PR00799; TRANSAMINASE.
PROSITE PS00105; AA_TRANSFER_CLASS_1; 1.
BLOCKS P23542.
ProtoNet P23542.
Proteomic databases
PeptideAtlas P23542; -.
Genome annotation databases
Ensembl YLR027C; Saccharomyces cerevisiae. [Contig view]
GeneID 850714; -.
GenomeReviews Y13138_GR; YLR027C.
KEGG sce:YLR027C; -.
NMPDR fig|4932.3.peg.4118; -.
Phylogenomic databases
HOGENOM P23542; -.
Other
LinkHub P23542; -.
NextBio 966778; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Aminotransferase; Complete proteome; Cytoplasm; Direct protein sequencing; Peroxisome; Phosphoprotein; Pyridoxal phosphate; Transferase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   418  417     Aspartate aminotransferase, cytoplasmic. PRO_0000123875
BINDING   255   255        Pyridoxal phosphate (covalent). 
MOD_RES   2     2        N-acetylserine. 
MOD_RES   389   389        Phosphoserine. 
CONFLICT   95    95        F -> L (in Ref. 2 and 3). 
CONFLICT   413   414        TI -> AT (in Ref. 2 and 3). 
TURN   2     7  6      
HELIX   17    24  8      
HELIX   50    60  11      
HELIX   76    87  12      
HELIX   92    95  4      
STRAND   99   105  7      
HELIX   106   121  16      
STRAND   127   132  6      
HELIX   137   142  6      
TURN   143   145  3      
STRAND   148   152  5      
TURN   156   159  4      
HELIX   163   172  10      
STRAND   178   182  5      
TURN   187   189  3      
HELIX   195   207  13      
STRAND   211   217  7      
TURN   219   221  3      
STRAND   222   224  3      
HELIX   226   229  4      
TURN   230   233  4      
TURN   239   243  5      
STRAND   246   251  6      
TURN   253   255  3      
HELIX   259   261  3      
STRAND   263   269  7      
HELIX   276   292  17      
TURN   293   295  3      
HELIX   300   311  12      
HELIX   313   344  32      
HELIX   352   355  4      
STRAND   358   362  5      
HELIX   367   377  11      
STRAND   385   388  4      
HELIX   389   391  3      
TURN   394   396  3      
HELIX   397   410  14      
Sequence information
Length: 418 AA [This is the length of the unprocessed precursor] Molecular weight: 46058 Da [This is the MW of the unprocessed precursor] CRC64: D25F40F6C6DD2B33 [This is a checksum on the sequence]
        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 

P23542 in FASTA format

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