P52893 (ALAM_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	ALT1
Ordered Locus Names:	YLR089C
ORF Names:	L9449.15

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	592 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)

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.

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	L-alanine catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway alanine biosynthetic process Inferred from mutant phenotype PubMed 19396236. Source: SGD alanine catabolic process Inferred from mutant phenotype PubMed 19396236. Source: SGD
Cellular_component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from direct assay Ref.3PubMed 14576278PubMed 16823961. Source: SGD
Molecular_function	L-alanine:2-oxoglutarate aminotransferase activity Inferred from mutant phenotype PubMed 19396236. Source: SGD 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	? – 592		Probable alanine aminotransferase, mitochondrial		PRO_0000001220
Amino acid modifications
	Modified residue	412	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P52893 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: EE94F059BE7BAF0B	FASTA	592	66,422
	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

References

	« Hide 'large scale' referencesShow '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. , 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 204511 / S288c / AB972.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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].
+	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.
PIR	S64923.
RefSeq	NP_013190.1. NM_001181976.1.
3D structure databases
ProteinModelPortal	P52893.
SMR	P52893. Positions 111-591.
ModBase	Search...
Protein-protein interaction databases
IntAct	P52893. 5 interactions.
MINT	MINT-2492558.
STRING	4932.YLR089C.
Proteomic databases
PaxDb	P52893.
PeptideAtlas	P52893.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YLR089C; YLR089C; YLR089C.
GeneID	850778.
KEGG	sce:YLR089C.
Organism-specific databases
CYGD	YLR089c.
SGD	S000004079. ALT1.
Phylogenomic databases
eggNOG	COG0436.
GeneTree	ENSGT00650000093331.
HOGENOM	HOG000215020.
KO	K00814.
OMA	CIEEVLH.
OrthoDB	EOG41VPB9.
Enzyme and pathway databases
UniPathway	UPA00528; UER00586.
Gene expression databases
Genevestigator	P52893.
GermOnline	YLR089C. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	3.40.640.10. 1 hit. 3.90.1150.10. 1 hit.
InterPro	IPR004839. Aminotransferase_I/II. IPR015424. PyrdxlP-dep_Trfase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view]
Pfam	PF00155. Aminotran_1_2. 1 hit. [Graphical view]
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
ProtoNet	Search...
Other
NextBio	966960.

Entry information

Entry name

ALAM_YEAST

Accession

Primary (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 1, 2013
This is version 105 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program