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Database: UniProt/SWISS-PROT
Entry: ALAM_YEAST
LinkDB: ALAM_YEAST
Original site: ALAM_YEAST 
ID   ALAM_YEAST              Reviewed;         592 AA.
AC   P52893; D6VY89;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   05-DEC-2018, entry version 151.
DE   RecName: Full=Probable alanine aminotransferase, mitochondrial;
DE            EC=2.6.1.2;
DE   AltName: Full=Glutamate pyruvate transaminase;
DE            Short=GPT;
DE   AltName: Full=Glutamic--alanine transaminase;
DE   AltName: Full=Glutamic--pyruvic transaminase;
DE   Flags: Precursor;
GN   Name=ALT1; OrderedLocusNames=YLR089C; ORFNames=L9449.15;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B.,
RA   Ansorge W., Benes V., Brueckner M., Delius H., Dubois E.,
RA   Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U.,
RA   Heumann K., Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K.,
RA   Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T.,
RA   Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E.,
RA   Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M.,
RA   Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C.,
RA   Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M.,
RA   Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H.,
RA   Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A.,
RA   Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(1997).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   SUBCELLULAR LOCATION.
RX   PubMed=11502169; DOI=10.1021/bi010277r;
RA   Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N.,
RA   Manon S., Schmitter J.-M.;
RT   "Yeast mitochondrial dehydrogenases are associated in a supramolecular
RT   complex.";
RL   Biochemistry 40:9758-9769(2001).
RN   [4]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides
RT   insights into evolution.";
RL   Science 325:1682-1686(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-alanine = L-glutamate + pyruvate;
CC         Xref=Rhea:RHEA:19453, ChEBI:CHEBI:15361, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:57972; EC=2.6.1.2;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC   -!- PATHWAY: Amino-acid degradation; L-alanine degradation via
CC       transaminase pathway; pyruvate from L-alanine: step 1/1.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000269|PubMed:11502169}.
CC   -!- MISCELLANEOUS: Present with 9960 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. Alanine aminotransferase subfamily.
CC       {ECO:0000305}.
DR   EMBL; U53880; AAB67593.1; -; Genomic_DNA.
DR   EMBL; Z73261; CAA97650.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09405.1; -; Genomic_DNA.
DR   PIR; S64923; S64923.
DR   RefSeq; NP_013190.1; NM_001181976.1.
DR   ProteinModelPortal; P52893; -.
DR   SMR; P52893; -.
DR   BioGrid; 31362; 428.
DR   IntAct; P52893; 5.
DR   MINT; P52893; -.
DR   STRING; 4932.YLR089C; -.
DR   iPTMnet; P52893; -.
DR   MaxQB; P52893; -.
DR   PaxDb; P52893; -.
DR   PRIDE; P52893; -.
DR   EnsemblFungi; YLR089C_mRNA; YLR089C_mRNA; YLR089C.
DR   GeneID; 850778; -.
DR   KEGG; sce:YLR089C; -.
DR   SGD; S000004079; ALT1.
DR   GeneTree; ENSGT00940000172095; -.
DR   HOGENOM; HOG000215020; -.
DR   InParanoid; P52893; -.
DR   KO; K00814; -.
DR   OMA; SKELPWP; -.
DR   OrthoDB; EOG092C291F; -.
DR   BioCyc; YEAST:YLR089C-MONOMER; -.
DR   Reactome; R-SCE-70614; Amino acid synthesis and interconversion (transamination).
DR   UniPathway; UPA00528; UER00586.
DR   PRO; PR:P52893; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR   GO; GO:0004021; F:L-alanine:2-oxoglutarate aminotransferase activity; IMP:SGD.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006523; P:alanine biosynthetic process; IMP:SGD.
DR   GO; GO:0006524; P:alanine catabolic process; IMP:SGD.
DR   GO; GO:0001300; P:chronological cell aging; IMP:SGD.
DR   GO; GO:0042853; P:L-alanine catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 2.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   1: Evidence at protein level;
KW   Aminotransferase; Complete proteome; Mitochondrion; Phosphoprotein;
KW   Pyridoxal phosphate; Reference proteome; Transferase; Transit peptide.
FT   TRANSIT       1      ?       Mitochondrion. {ECO:0000255}.
FT   CHAIN         ?    592       Probable alanine aminotransferase,
FT                                mitochondrial.
FT                                /FTId=PRO_0000001220.
FT   MOD_RES      77     77       Phosphoserine.
FT                                {ECO:0000244|PubMed:19779198}.
FT   MOD_RES     412    412       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000250}.
SQ   SEQUENCE   592 AA;  66422 MW;  EE94F059BE7BAF0B CRC64;
     MLSLSAKNHF TVSNSITHVI KSYHIRTLTS SAEKMPHITT PFSTSASSTK LKAFRKVRPV
     LQRHSSSWIV AQNHRRSLSG QSSLNDLRHL NRFPHHTLKT SNNEFYPAEQ LTLEDVNENV
     LKAKYAVRGA IPMRAEELKA QLEKDPQSLP FDRIINANIG NPQQLQQKPL TYYRQVLSLL
     QYPELLNQNE QQLVDSKLFK LDAIKRAKSL MEDIGGSVGA YSSSQGVEGI RKSVAEFITK
     RDEGEISYPE DIFLTAGASA AVNYLLSIFC RGPETGVLIP IPQYPLYTAT LALNNSQALP
     YYLDENSGWS TNPEEIETVV KEAIQNEIKP TVLVVINPGN PTGAVLSPES IAQIFEVAAK
     YGTVVIADEV YQENIFPGTK FHSMKKILRH LQREHPGKFD NVQLASLHST SKGVSGECGQ
     RGGYMELTGF SHEMRQVILK LASISLCPVV TGQALVDLMV RPPVEGEESF ESDQAERNSI
     HEKLITRAMT LYETFNSLEG IECQKPQGAM YLFPKIDLPF KAVQEARHLE LTPDEFYCKK
     LLESTGICTV PGSGFGQEPG TYHLRTTFLA PGLEWIKKWE SFHKEFFDQY RD
//
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