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P52893 (ALAM_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable alanine aminotransferase, mitochondrial

EC=2.6.1.2
Alternative name(s):
Glutamate pyruvate transaminase
Short name=GPT
Glutamic--alanine transaminase
Glutamic--pyruvic transaminase
Gene names
Name:ALT1
Ordered Locus Names:YLR089C
ORF Names:L9449.15
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length592 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

L-alanine + 2-oxoglutarate = pyruvate + L-glutamate.

Cofactor

Pyridoxal phosphate.

Pathway

Amino-acid degradation; L-alanine degradation via transaminase pathway; pyruvate from L-alanine: step 1/1.

Subunit structure

Homodimer By similarity.

Subcellular location

Mitochondrion matrix Ref.3.

Miscellaneous

Present with 9960 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. Alanine aminotransferase subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 592Probable alanine aminotransferase, mitochondrialPRO_0000001220

Amino acid modifications

Modified residue771Phosphoserine Ref.5
Modified residue4121N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P52893 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: EE94F059BE7BAF0B

FASTA59266,422
        10         20         30         40         50         60 
MLSLSAKNHF TVSNSITHVI KSYHIRTLTS SAEKMPHITT PFSTSASSTK LKAFRKVRPV 

        70         80         90        100        110        120 
LQRHSSSWIV AQNHRRSLSG QSSLNDLRHL NRFPHHTLKT SNNEFYPAEQ LTLEDVNENV 

       130        140        150        160        170        180 
LKAKYAVRGA IPMRAEELKA QLEKDPQSLP FDRIINANIG NPQQLQQKPL TYYRQVLSLL 

       190        200        210        220        230        240 
QYPELLNQNE QQLVDSKLFK LDAIKRAKSL MEDIGGSVGA YSSSQGVEGI RKSVAEFITK 

       250        260        270        280        290        300 
RDEGEISYPE DIFLTAGASA AVNYLLSIFC RGPETGVLIP IPQYPLYTAT LALNNSQALP 

       310        320        330        340        350        360 
YYLDENSGWS TNPEEIETVV KEAIQNEIKP TVLVVINPGN PTGAVLSPES IAQIFEVAAK 

       370        380        390        400        410        420 
YGTVVIADEV YQENIFPGTK FHSMKKILRH LQREHPGKFD NVQLASLHST SKGVSGECGQ 

       430        440        450        460        470        480 
RGGYMELTGF SHEMRQVILK LASISLCPVV TGQALVDLMV RPPVEGEESF ESDQAERNSI 

       490        500        510        520        530        540 
HEKLITRAMT LYETFNSLEG IECQKPQGAM YLFPKIDLPF KAVQEARHLE LTPDEFYCKK 

       550        560        570        580        590 
LLESTGICTV PGSGFGQEPG TYHLRTTFLA PGLEWIKKWE SFHKEFFDQY RD 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Yeast mitochondrial dehydrogenases are associated in a supramolecular complex."
Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N., Manon S., Schmitter J.-M.
Biochemistry 40:9758-9769(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[4]"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] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[5]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U53880 Genomic DNA. Translation: AAB67593.1.
Z73261 Genomic DNA. Translation: CAA97650.1.
BK006945 Genomic DNA. Translation: DAA09405.1.
PIRS64923.
RefSeqNP_013190.1. NM_001181976.1.

3D structure databases

ProteinModelPortalP52893.
SMRP52893. Positions 111-591.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31362. 154 interactions.
IntActP52893. 5 interactions.
MINTMINT-2492558.
STRING4932.YLR089C.

Proteomic databases

MaxQBP52893.
PaxDbP52893.
PeptideAtlasP52893.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYLR089C; YLR089C; YLR089C.
GeneID850778.
KEGGsce:YLR089C.

Organism-specific databases

CYGDYLR089c.
SGDS000004079. ALT1.

Phylogenomic databases

eggNOGCOG0436.
GeneTreeENSGT00650000093331.
HOGENOMHOG000215020.
KOK00814.
OMAFPANPQD.
OrthoDBEOG7GXPMR.

Enzyme and pathway databases

BioCycYEAST:YLR089C-MONOMER.
UniPathwayUPA00528; UER00586.

Gene expression databases

GenevestigatorP52893.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProIPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMSSF53383. SSF53383. 1 hit.
ProtoNetSearch...

Other

NextBio966960.

Entry information

Entry nameALAM_YEAST
AccessionPrimary (citable) accession number: P52893
Secondary accession number(s): D6VY89
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 14, 2014
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XII

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

Yeast

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

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways