Aspartate aminotransferase, mitochondrial precursor - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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Q01802 (AATM_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 107. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Aspartate aminotransferase, mitochondrial
EC=2.6.1.1

Alternative name(s):
Transaminase A

Gene names

Name:	AAT1
Ordered Locus Names:	YKL106W
ORF Names:	YKL461

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	451 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Plays a key role in amino acid metabolism. Important for metabolite exchange between mitochondria and cytosol By similarity.
Catalytic activity	L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate. Ref.1
Cofactor	Pyridoxal phosphate.
Subunit structure	Homodimer.
Subcellular location	Mitochondrion matrix Ref.5 Ref.7 Ref.8.
Miscellaneous	In eukaryotes there are cytoplasmic, mitochondrial and chloroplastic isozymes. Present with 2910 molecules/cell in log phase SD medium. Ref.6
Sequence similarities	Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	2-oxoglutarate metabolic process Inferred from sequence or structural similarity. Source: UniProtKB aspartate metabolic process Inferred from sequence or structural similarity. Source: UniProtKB biosynthetic process Inferred from electronic annotation. Source: InterPro chronological cell aging Inferred from mutant phenotype. Source: SGD glutamate metabolic process Inferred from sequence or structural similarity. Source: UniProtKB replicative cell aging Inferred from mutant phenotype. Source: SGD
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	L-aspartate:2-oxoglutarate aminotransferase activity Inferred from sequence or structural similarity. Source: UniProtKB L-phenylalanine:2-oxoglutarate aminotransferase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – ?

Mitochondrion Potential

Chain

? – 451

Aspartate aminotransferase, mitochondrial

PRO_0000001213

Sites

Binding site

Aspartate; via amide nitrogen By similarity

Binding site

155

Aspartate By similarity

Binding site

216

Aspartate By similarity

Binding site

423

Aspartate By similarity

Amino acid modifications

Modified residue

286

N6-(pyridoxal phosphate)lysine By similarity

Experimental info

Sequence conflict

V → A in CAA48188. Ref.1

Sequence conflict

414

Y → S in CAA48188. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q01802 [UniParc].

Last modified December 6, 2005. Version 2.
Checksum: 758A90434CDBAA7A
Show »

FASTA

451

51,795

        10         20         30         40         50         60 
MLRTRLTNCS LWRPYYTSSL SRVPRAPPDK VLGLSEHFKK VKNVNKIDLT VGIYKDGWGK 

        70         80         90        100        110        120 
VTTFPSVAKA QKLIESHLEL NKNLSYLPIT GSKEFQENVM KFLFKESCPQ FGPFYLAHDR 

       130        140        150        160        170        180 
ISFVQTLSGT GALAVAAKFL ALFISRDIWI PDPSWANHKN IFQNNGFENI YRYSYYKDGQ 

       190        200        210        220        230        240 
IDIDGWIEQL KTFAYNNQQE NNKNPPCIIL HACCHNPTGL DPTKEQWEKI IDTIYELKMV 

       250        260        270        280        290        300 
PIVDMAYQGL ESGNLLKDAY LLRLCLNVNK YPNWSNGIFL CQSFAKNMGL YGERVGSLSV 

       310        320        330        340        350        360 
ITPATANNGK FNPLQQKNSL QQNIDSQLKK IVRGMYSSPP GYGSRVVNVV LSDFKLKQQW 

       370        380        390        400        410        420 
FKDVDFMVQR LHHVRQEMFD RLGWPDLVNF AQQHGMFYYT RFSPKQVEIL RNNYFVYLTG 

       430        440        450 
DGRLSLSGVN DSNVDYLCES LEAVSKMDKL A

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"AAT1, a gene encoding a mitochondrial aspartate aminotransferase in Saccharomyces cerevisiae." Morin P.J., Subramanian G.S., Gilmore T.D. Biochim. Biophys. Acta 1171:211-214(1992) [PubMed: 1482685] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ENZYME ACTIVITY.
[2]	"The DNA sequence analysis of the HAP4-LAP4 region on chromosome XI of Saccharomyces cerevisiae suggests the presence of a second aspartate aminotransferase gene in yeast." Cheret G., Pallier C., Valens M., Daignan-Fornier B., Fukuhara H., Bolotin-Fukuhara M., Sor F. Yeast 9:1259-1265(1993) [PubMed: 8109175] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"Complete DNA sequence of yeast chromosome XI." Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C. Mewes H.-W. Nature 369:371-378(1994) [PubMed: 8196765] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[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]	"The proteome of Saccharomyces cerevisiae mitochondria." Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P., Pfanner N., Meisinger C. Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003) [PubMed: 14576278] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY. Strain: ATCC 76625 / YPH499.
[8]	"Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics." Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A. J. Proteome Res. 5:1543-1554(2006) [PubMed: 16823961] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X68052 Genomic DNA. Translation: CAA48188.1. X71133 Genomic DNA. Translation: CAA50451.1. Z28106 Genomic DNA. Translation: CAA81946.1. BK006944 Genomic DNA. Translation: DAA09052.1.
PIR	S37933.
RefSeq	NP_012816.1. NM_001179672.1.
3D structure databases
ProteinModelPortal	Q01802.
SMR	Q01802. Positions 17-446.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-4608N.
IntAct	Q01802. 3 interactions.
MINT	MINT-536399.
STRING	Q01802.
Proteomic databases
PeptideAtlas	Q01802.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YKL106W; YKL106W; YKL106W.
GeneID	853755.
KEGG	sce:YKL106W.
NMPDR	fig\|4932.3.peg.3798.
Organism-specific databases
CYGD	YKL106w.
SGD	S000001589. AAT1.
Phylogenomic databases
eggNOG	fuNOG05116.
GeneTree	EFGT00050000000248.
HOGENOM	HBG446828.
OMA	LTVGIYK.
OrthoDB	EOG4R7ZKM.
Gene expression databases
ArrayExpress	Q01802.
Genevestigator	Q01802.
GermOnline	YKL106W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR004839. 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]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
KO	K14455.
PANTHER	PTHR11879. Asp_trans. 1 hit.
Pfam	PF00155. Aminotran_1_2. 1 hit. [Graphical view]
PRINTS	PR00799. TRANSAMINASE.
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
PROSITE	PS00105. AA_TRANSFER_CLASS_1. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	974828.

Entry information

Entry name

AATM_YEAST

Accession

Primary (citable) accession number: Q01802
Secondary accession number(s): D6VXI2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	December 6, 2005
Last modified:	December 14, 2011
This is version 107 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome XI

Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents