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Protein

Probable alanine aminotransferase, mitochondrial

Gene

ALT1

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

Catalytic activityi

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

Cofactori

Pathwayi

GO - Molecular functioni

  1. L-alanine:2-oxoglutarate aminotransferase activity Source: SGD
  2. pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  1. alanine biosynthetic process Source: SGD
  2. alanine catabolic process Source: SGD
  3. chronological cell aging Source: SGD
  4. L-alanine catabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciYEAST:YLR089C-MONOMER.
ReactomeiREACT_288999. Amino acid synthesis and interconversion (transamination).
UniPathwayiUPA00528; UER00586.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:ALT1
Ordered Locus Names:YLR089C
ORF Names:L9449.15
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XII

Organism-specific databases

CYGDiYLR089c.
EuPathDBiFungiDB:YLR089C.
SGDiS000004079. ALT1.

Subcellular locationi

  1. Mitochondrion matrix 1 Publication

GO - Cellular componenti

  1. mitochondrial matrix Source: UniProtKB-SubCell
  2. mitochondrion Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 592Probable alanine aminotransferase, mitochondrialPRO_0000001220
Transit peptidei1 – ?MitochondrionSequence Analysis

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei77 – 771Phosphoserine1 Publication
Modified residuei412 – 4121N6-(pyridoxal phosphate)lysineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP52893.
PaxDbiP52893.
PeptideAtlasiP52893.

Expressioni

Gene expression databases

GenevestigatoriP52893.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi31362. 155 interactions.
IntActiP52893. 5 interactions.
MINTiMINT-2492558.
STRINGi4932.YLR089C.

Structurei

3D structure databases

ProteinModelPortaliP52893.
SMRiP52893. Positions 111-591.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0436.
GeneTreeiENSGT00650000093331.
HOGENOMiHOG000215020.
InParanoidiP52893.
KOiK00814.
OMAiYSATHIT.
OrthoDBiEOG7GXPMR.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P52893-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSLSAKNHF TVSNSITHVI KSYHIRTLTS SAEKMPHITT PFSTSASSTK
60 70 80 90 100
LKAFRKVRPV LQRHSSSWIV AQNHRRSLSG QSSLNDLRHL NRFPHHTLKT
110 120 130 140 150
SNNEFYPAEQ LTLEDVNENV LKAKYAVRGA IPMRAEELKA QLEKDPQSLP
160 170 180 190 200
FDRIINANIG NPQQLQQKPL TYYRQVLSLL QYPELLNQNE QQLVDSKLFK
210 220 230 240 250
LDAIKRAKSL MEDIGGSVGA YSSSQGVEGI RKSVAEFITK RDEGEISYPE
260 270 280 290 300
DIFLTAGASA AVNYLLSIFC RGPETGVLIP IPQYPLYTAT LALNNSQALP
310 320 330 340 350
YYLDENSGWS TNPEEIETVV KEAIQNEIKP TVLVVINPGN PTGAVLSPES
360 370 380 390 400
IAQIFEVAAK YGTVVIADEV YQENIFPGTK FHSMKKILRH LQREHPGKFD
410 420 430 440 450
NVQLASLHST SKGVSGECGQ RGGYMELTGF SHEMRQVILK LASISLCPVV
460 470 480 490 500
TGQALVDLMV RPPVEGEESF ESDQAERNSI HEKLITRAMT LYETFNSLEG
510 520 530 540 550
IECQKPQGAM YLFPKIDLPF KAVQEARHLE LTPDEFYCKK LLESTGICTV
560 570 580 590
PGSGFGQEPG TYHLRTTFLA PGLEWIKKWE SFHKEFFDQY RD
Length:592
Mass (Da):66,422
Last modified:October 1, 1996 - v1
Checksum:iEE94F059BE7BAF0B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U53880 Genomic DNA. Translation: AAB67593.1.
Z73261 Genomic DNA. Translation: CAA97650.1.
BK006945 Genomic DNA. Translation: DAA09405.1.
PIRiS64923.
RefSeqiNP_013190.1. NM_001181976.1.

Genome annotation databases

EnsemblFungiiYLR089C; YLR089C; YLR089C.
GeneIDi850778.
KEGGisce:YLR089C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U53880 Genomic DNA. Translation: AAB67593.1.
Z73261 Genomic DNA. Translation: CAA97650.1.
BK006945 Genomic DNA. Translation: DAA09405.1.
PIRiS64923.
RefSeqiNP_013190.1. NM_001181976.1.

3D structure databases

ProteinModelPortaliP52893.
SMRiP52893. Positions 111-591.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31362. 155 interactions.
IntActiP52893. 5 interactions.
MINTiMINT-2492558.
STRINGi4932.YLR089C.

Proteomic databases

MaxQBiP52893.
PaxDbiP52893.
PeptideAtlasiP52893.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR089C; YLR089C; YLR089C.
GeneIDi850778.
KEGGisce:YLR089C.

Organism-specific databases

CYGDiYLR089c.
EuPathDBiFungiDB:YLR089C.
SGDiS000004079. ALT1.

Phylogenomic databases

eggNOGiCOG0436.
GeneTreeiENSGT00650000093331.
HOGENOMiHOG000215020.
InParanoidiP52893.
KOiK00814.
OMAiYSATHIT.
OrthoDBiEOG7GXPMR.

Enzyme and pathway databases

UniPathwayiUPA00528; UER00586.
BioCyciYEAST:YLR089C-MONOMER.
ReactomeiREACT_288999. Amino acid synthesis and interconversion (transamination).

Miscellaneous databases

NextBioi966960.
PROiP52893.

Gene expression databases

GenevestigatoriP52893.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
ProtoNetiSearch...

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. "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. 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].

Entry informationi

Entry nameiALAM_YEAST
AccessioniPrimary (citable) accession number: P52893
Secondary accession number(s): D6VY89
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 29, 2015
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 9960 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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

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 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.