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 03-AUG-2022, entry version 169.
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; Saccharomycetes;
OC 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., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., 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., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and 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., Manon S.,
RA 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., Dephoure N.,
RA 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 BY
RP 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 insights
RT 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 transaminase
CC 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 medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. Alanine aminotransferase subfamily.
CC {ECO:0000305}.
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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 AlphaFoldDB; P52893; -.
DR SMR; P52893; -.
DR BioGRID; 31362; 434.
DR DIP; DIP-7654N; -.
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; YLR089C.
DR GeneID; 850778; -.
DR KEGG; sce:YLR089C; -.
DR SGD; S000004079; ALT1.
DR VEuPathDB; FungiDB:YLR089C; -.
DR eggNOG; KOG0258; Eukaryota.
DR GeneTree; ENSGT00940000172095; -.
DR HOGENOM; CLU_014254_3_0_1; -.
DR InParanoid; P52893; -.
DR OMA; FGFECPP; -.
DR BioCyc; YEAST:YLR089C-MON; -.
DR BRENDA; 2.6.1.2; 984.
DR Reactome; R-SCE-8964540; Alanine metabolism.
DR UniPathway; UPA00528; UER00586.
DR PRO; PR:P52893; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P52893; protein.
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:0042853; P:L-alanine catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR045088; ALAT1/2-like.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11751; PTHR11751; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 1: Evidence at protein level;
KW Aminotransferase; Mitochondrion; Phosphoprotein; Pyridoxal phosphate;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..592
FT /note="Probable alanine aminotransferase, mitochondrial"
FT /id="PRO_0000001220"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 412
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="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
