Skip Header

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

Aspartate aminotransferase, mitochondrial

Gene

AAT1

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. Important for metabolite exchange between mitochondria and cytosol (By similarity).By similarity

Catalytic activityi

L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate.1 Publication

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei52 – 521Aspartate; via amide nitrogenBy similarity
Binding sitei155 – 1551AspartateBy similarity
Binding sitei216 – 2161AspartateBy similarity
Binding sitei423 – 4231AspartateBy similarity

GO - Molecular functioni

GO - Biological processi

  • 2-oxoglutarate metabolic process Source: UniProtKB
  • aspartate metabolic process Source: UniProtKB
  • biosynthetic process Source: InterPro
  • chronological cell aging Source: SGD
  • glutamate metabolic process Source: UniProtKB
  • replicative cell aging Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciYEAST:YKL106W-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartate aminotransferase, mitochondrial (EC:2.6.1.1)
Alternative name(s):
Transaminase A
Gene namesi
Name:AAT1
Ordered Locus Names:YKL106W
ORF Names:YKL461
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XI

Organism-specific databases

EuPathDBiFungiDB:YKL106W.
SGDiS000001589. AAT1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 451Aspartate aminotransferase, mitochondrialPRO_0000001213
Transit peptidei1 – ?MitochondrionSequence analysis

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei286 – 2861N6-(pyridoxal phosphate)lysineBy similarity

Proteomic databases

MaxQBiQ01802.
PeptideAtlasiQ01802.

PTM databases

iPTMnetiQ01802.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi34028. 39 interactions.
DIPiDIP-4608N.
IntActiQ01802. 4 interactions.
MINTiMINT-536399.

Structurei

3D structure databases

ProteinModelPortaliQ01802.
SMRiQ01802. Positions 27-446.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOGENOMiHOG000185898.
InParanoidiQ01802.
KOiK14455.
OMAiIVEVIFD.
OrthoDBiEOG793BHW.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR004839. Aminotransferase_I/II.
IPR000796. Asp_trans.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[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.

Q01802-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRTRLTNCS LWRPYYTSSL SRVPRAPPDK VLGLSEHFKK VKNVNKIDLT
60 70 80 90 100
VGIYKDGWGK VTTFPSVAKA QKLIESHLEL NKNLSYLPIT GSKEFQENVM
110 120 130 140 150
KFLFKESCPQ FGPFYLAHDR ISFVQTLSGT GALAVAAKFL ALFISRDIWI
160 170 180 190 200
PDPSWANHKN IFQNNGFENI YRYSYYKDGQ IDIDGWIEQL KTFAYNNQQE
210 220 230 240 250
NNKNPPCIIL HACCHNPTGL DPTKEQWEKI IDTIYELKMV PIVDMAYQGL
260 270 280 290 300
ESGNLLKDAY LLRLCLNVNK YPNWSNGIFL CQSFAKNMGL YGERVGSLSV
310 320 330 340 350
ITPATANNGK FNPLQQKNSL QQNIDSQLKK IVRGMYSSPP GYGSRVVNVV
360 370 380 390 400
LSDFKLKQQW FKDVDFMVQR LHHVRQEMFD RLGWPDLVNF AQQHGMFYYT
410 420 430 440 450
RFSPKQVEIL RNNYFVYLTG DGRLSLSGVN DSNVDYLCES LEAVSKMDKL

A
Length:451
Mass (Da):51,795
Last modified:December 6, 2005 - v2
Checksum:i758A90434CDBAA7A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti41 – 411V → A in CAA48188 (PubMed:1482685).Curated
Sequence conflicti414 – 4141Y → S in CAA48188 (PubMed:1482685).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X68052 Genomic DNA. Translation: CAA48188.1.
X71133 Genomic DNA. Translation: CAA50451.1.
Z28106 Genomic DNA. Translation: CAA81946.1.
BK006944 Genomic DNA. Translation: DAA09052.1.
PIRiS37933.
RefSeqiNP_012816.1. NM_001179672.1.

Genome annotation databases

EnsemblFungiiYKL106W; YKL106W; YKL106W.
GeneIDi853755.
KEGGisce:YKL106W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X68052 Genomic DNA. Translation: CAA48188.1.
X71133 Genomic DNA. Translation: CAA50451.1.
Z28106 Genomic DNA. Translation: CAA81946.1.
BK006944 Genomic DNA. Translation: DAA09052.1.
PIRiS37933.
RefSeqiNP_012816.1. NM_001179672.1.

3D structure databases

ProteinModelPortaliQ01802.
SMRiQ01802. Positions 27-446.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34028. 39 interactions.
DIPiDIP-4608N.
IntActiQ01802. 4 interactions.
MINTiMINT-536399.

PTM databases

iPTMnetiQ01802.

Proteomic databases

MaxQBiQ01802.
PeptideAtlasiQ01802.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYKL106W; YKL106W; YKL106W.
GeneIDi853755.
KEGGisce:YKL106W.

Organism-specific databases

EuPathDBiFungiDB:YKL106W.
SGDiS000001589. AAT1.

Phylogenomic databases

HOGENOMiHOG000185898.
InParanoidiQ01802.
KOiK14455.
OMAiIVEVIFD.
OrthoDBiEOG793BHW.

Enzyme and pathway databases

BioCyciYEAST:YKL106W-MONOMER.

Miscellaneous databases

NextBioi974828.
PROiQ01802.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR004839. Aminotransferase_I/II.
IPR000796. Asp_trans.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[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. "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] [Europe PMC] [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] [Europe PMC] [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.
    , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
    Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    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] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiAATM_YEAST
AccessioniPrimary (citable) accession number: Q01802
Secondary accession number(s): D6VXI2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: December 6, 2005
Last modified: May 11, 2016
This is version 140 of the entry and version 2 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 2910 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

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 one 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.