ARO9_YEAST
ID ARO9_YEAST Reviewed; 513 AA.
AC P38840; D3DL86; P87291;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 3.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Aromatic amino acid aminotransferase 2 {ECO:0000303|PubMed:9491082};
DE EC=2.6.1.57 {ECO:0000269|PubMed:6763508, ECO:0000305|PubMed:9491082};
DE AltName: Full=Aromatic amino acid aminotransferase II {ECO:0000303|PubMed:9491083};
DE AltName: Full=Aromatic amino acid-requiring protein 9 {ECO:0000303|PubMed:9491083};
DE AltName: Full=Kynurenine aminotransferase I {ECO:0000303|PubMed:9491083};
DE Short=KAT I {ECO:0000303|PubMed:9491083};
DE EC=2.6.1.7 {ECO:0000305|PubMed:9491083};
GN Name=ARO9 {ECO:0000303|PubMed:9491083}; OrderedLocusNames=YHR137W;
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 [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC STRAIN=Sigma 1278B;
RX PubMed=9491083; DOI=10.1007/s004380050644;
RA Iraqui I., Vissers S., Cartiaux M., Urrestarazu A.;
RT "Characterisation of Saccharomyces cerevisiae ARO8 and ARO9 genes encoding
RT aromatic aminotransferases I and II reveals a new aminotransferase
RT subfamily.";
RL Mol. Gen. Genet. 257:238-248(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [3]
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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=6763508; DOI=10.1007/bf00415010;
RA Kradolfer P., Niederberger P., Hutter R.;
RT "Tryptophan degradation in Saccharomyces cerevisiae: characterization of
RT two aromatic aminotransferases.";
RL Arch. Microbiol. 133:242-248(1982).
RN [5]
RP FUNCTION.
RX PubMed=9491082; DOI=10.1007/s004380050643;
RA Urrestarazu A., Vissers S., Iraqui I., Grenson M.;
RT "Phenylalanine- and tyrosine-auxotrophic mutants of Saccharomyces
RT cerevisiae impaired in transamination.";
RL Mol. Gen. Genet. 257:230-237(1998).
RN [6]
RP INDUCTION.
RX PubMed=10207060; DOI=10.1128/mcb.19.5.3360;
RA Iraqui I., Vissers S., Andre B., Urrestarazu A.;
RT "Transcriptional induction by aromatic amino acids in Saccharomyces
RT cerevisiae.";
RL Mol. Cell. Biol. 19:3360-3371(1999).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [8]
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [10]
RP FUNCTION.
RX PubMed=18625006; DOI=10.1111/j.1742-4658.2008.06552.x;
RA Pirkov I., Norbeck J., Gustafsson L., Albers E.;
RT "A complete inventory of all enzymes in the eukaryotic methionine salvage
RT pathway.";
RL FEBS J. 275:4111-4120(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90 AND SER-92, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [12]
RP IDENTIFICATION 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 insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: General aromatic amino acid transaminase involved in several
CC otherwise unrelated metabolic pathways. Mainly involved in tryptophan
CC degradation. Active with phenylalanine, tyrosine and tryptophan as
CC amino donors and with phenylpyruvate, hydroxyphenylpyruvate and
CC pyruvate as amino acceptors. Does not accept glutamate or 2-
CC oxoglutarate as substrates. Also active with methionine, leucine,
CC glutamine and kynurenine. Catalyzes the formation of methionine from 2-
CC keto-4-methylthiobutyrate (KMTB) in the methionine salvage pathway
CC primarily using aromatic amino acids (tyrosine, phenylalanine and
CC tryptophan) as the amino donors. Catalyzes the irreversible
CC transamination of the L-tryptophan metabolite L-kynurenine to form
CC kynurenic acid (KA) with pyruvate as amino acceptor.
CC {ECO:0000269|PubMed:18625006, ECO:0000269|PubMed:6763508,
CC ECO:0000269|PubMed:9491082, ECO:0000269|PubMed:9491083}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + an aromatic L-alpha-amino acid = an aromatic
CC oxo-acid + L-glutamate; Xref=Rhea:RHEA:17533, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:73309, ChEBI:CHEBI:84824; EC=2.6.1.57;
CC Evidence={ECO:0000269|PubMed:6763508, ECO:0000305|PubMed:9491082};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-methylsulfanyl-2-oxobutanoate + an aromatic L-alpha-amino
CC acid = an aromatic oxo-acid + L-methionine; Xref=Rhea:RHEA:47800,
CC ChEBI:CHEBI:16723, ChEBI:CHEBI:57844, ChEBI:CHEBI:73309,
CC ChEBI:CHEBI:84824; Evidence={ECO:0000269|PubMed:6763508,
CC ECO:0000305|PubMed:9491082};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-kynurenine = H2O + kynurenate + L-
CC glutamate; Xref=Rhea:RHEA:65560, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57959,
CC ChEBI:CHEBI:58454; EC=2.6.1.7; Evidence={ECO:0000305|PubMed:9491083};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:O84395};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.4 mM for tryptophan {ECO:0000269|PubMed:6763508};
CC KM=0.2 mM for tyrosine {ECO:0000269|PubMed:6763508};
CC KM=0.2 mM for phenylalanine {ECO:0000269|PubMed:6763508};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via salvage
CC pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate:
CC step 6/6. {ECO:0000269|PubMed:6763508}.
CC -!- PATHWAY: Amino-acid degradation; L-kynurenine degradation; kynurenate
CC from L-kynurenine: step 1/2.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: By aromatic amino acids in the growth medium. Expression
CC also induced in ARO8 mutants grown on minimal ammonia medium.
CC {ECO:0000269|PubMed:10207060, ECO:0000269|PubMed:9491083}.
CC -!- MISCELLANEOUS: Present with 7700 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. {ECO:0000305}.
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DR EMBL; Y13625; CAA73950.1; -; Genomic_DNA.
DR EMBL; U10398; AAB68403.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06830.1; -; Genomic_DNA.
DR PIR; S48981; S48981.
DR RefSeq; NP_012005.1; NM_001179267.1.
DR AlphaFoldDB; P38840; -.
DR SMR; P38840; -.
DR BioGRID; 36570; 72.
DR DIP; DIP-4942N; -.
DR IntAct; P38840; 12.
DR MINT; P38840; -.
DR STRING; 4932.YHR137W; -.
DR iPTMnet; P38840; -.
DR MaxQB; P38840; -.
DR PaxDb; P38840; -.
DR PRIDE; P38840; -.
DR EnsemblFungi; YHR137W_mRNA; YHR137W; YHR137W.
DR GeneID; 856539; -.
DR KEGG; sce:YHR137W; -.
DR SGD; S000001179; ARO9.
DR VEuPathDB; FungiDB:YHR137W; -.
DR eggNOG; KOG0634; Eukaryota.
DR GeneTree; ENSGT00390000004594; -.
DR HOGENOM; CLU_017584_0_5_1; -.
DR InParanoid; P38840; -.
DR OMA; EPSAGMF; -.
DR BioCyc; MetaCyc:YHR137W-MON; -.
DR BioCyc; YEAST:YHR137W-MON; -.
DR BRENDA; 2.6.1.57; 984.
DR UniPathway; UPA00334; UER00726.
DR UniPathway; UPA00904; UER00879.
DR PRO; PR:P38840; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38840; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0047536; F:2-aminoadipate transaminase activity; IBA:GO_Central.
DR GO; GO:0008793; F:aromatic-amino-acid:2-oxoglutarate aminotransferase activity; IMP:SGD.
DR GO; GO:0036137; F:kynurenine aminotransferase activity; IMP:SGD.
DR GO; GO:0016212; F:kynurenine-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0080130; F:L-phenylalanine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IBA:GO_Central.
DR GO; GO:1901605; P:alpha-amino acid metabolic process; IBA:GO_Central.
DR GO; GO:0009074; P:aromatic amino acid family catabolic process; IBA:GO_Central.
DR GO; GO:0009072; P:aromatic amino acid family metabolic process; IMP:SGD.
DR GO; GO:0097053; P:L-kynurenine catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniPathway.
DR GO; GO:0009094; P:L-phenylalanine biosynthetic process; IGI:SGD.
DR GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IBA:GO_Central.
DR GO; GO:0006571; P:tyrosine biosynthetic process; IGI:SGD.
DR Gene3D; 3.40.640.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
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; Cytoplasm; Phosphoprotein; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..513
FT /note="Aromatic amino acid aminotransferase 2"
FT /id="PRO_0000064679"
FT BINDING 102
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q93ZN9"
FT BINDING 143..144
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:O84395"
FT BINDING 232
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:O84395"
FT BINDING 232
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O84395,
FT ECO:0000250|UniProtKB:Q93ZN9"
FT BINDING 263
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:O84395"
FT BINDING 314..316
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:O84395"
FT BINDING 324
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q93ZN9"
FT BINDING 481
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q93ZN9"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 317
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:O84395"
FT CONFLICT 460
FT /note="V -> L (in Ref. 1; CAA73950)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 513 AA; 58528 MW; 8DA49174D59C8859 CRC64;
MTAGSAPPVD YTSLKKNFQP FLSRRVENRS LKSFWDASDI SDDVIELAGG MPNERFFPIE
SMDLKISKVP FNDNPKWHNS FTTAHLDLGS PSELPIARSF QYAETKGLPP LLHFVKDFVS
RINRPAFSDE TESNWDVILS GGSNDSMFKV FETICDESTT VMIEEFTFTP AMSNVEATGA
KVIPIKMNLT FDRESQGIDV EYLTQLLDNW STGPYKDLNK PRVLYTIATG QNPTGMSVPQ
WKREKIYQLA QRHDFLIVED DPYGYLYFPS YNPQEPLENP YHSSDLTTER YLNDFLMKSF
LTLDTDARVI RLETFSKIFA PGLRLSFIVA NKFLLQKILD LADITTRAPS GTSQAIVYST
IKAMAESNLS SSLSMKEAMF EGWIRWIMQI ASKYNHRKNL TLKALYETES YQAGQFTVME
PSAGMFIIIK INWGNFDRPD DLPQQMDILD KFLLKNGVKV VLGYKMAVCP NYSKQNSDFL
RLTIAYARDD DQLIEASKRI GSGIKEFFDN YKS
