ARO8_YEAST
ID ARO8_YEAST Reviewed; 500 AA.
AC P53090; D6VTV2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Aromatic/aminoadipate aminotransferase 1 {ECO:0000303|PubMed:9491083};
DE AltName: Full=2-aminoadipate aminotransferase {ECO:0000303|PubMed:9491083};
DE EC=2.6.1.39 {ECO:0000269|PubMed:9491082};
DE AltName: Full=2-aminoadipate transaminase {ECO:0000303|PubMed:9491083};
DE AltName: Full=Alpha-aminoadipate aminotransferase {ECO:0000303|PubMed:9491083};
DE Short=AadAT {ECO:0000305};
DE AltName: Full=Aromatic amino acid aminotransferase 1 {ECO:0000303|PubMed:9491083};
DE EC=2.6.1.57 {ECO:0000269|PubMed:9491082};
DE AltName: Full=Aromatic amino acid aminotransferase I {ECO:0000303|PubMed:9491083};
DE AltName: Full=Aromatic amino acid-requiring protein 8 {ECO:0000303|PubMed:9491083};
GN Name=ARO8 {ECO:0000303|PubMed:9491083}; OrderedLocusNames=YGL202W;
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], AND FUNCTION.
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=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP FUNCTION.
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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
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 [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 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, AND IDENTIFICATION BY
RP 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 [11]
RP FUNCTION.
RX PubMed=21982920; DOI=10.1016/j.abb.2011.09.008;
RA Karsten W.E., Reyes Z.L., Bobyk K.D., Cook P.F., Chooback L.;
RT "Mechanism of the aromatic aminotransferase encoded by the Aro8 gene from
RT Saccharomyces cerevisiae.";
RL Arch. Biochem. Biophys. 516:67-74(2011).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [13] {ECO:0007744|PDB:4JE5}
RP X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS), AND COFACTOR.
RX PubMed=23893908; DOI=10.1002/pro.2315;
RA Bulfer S.L., Brunzelle J.S., Trievel R.C.;
RT "Crystal structure of Saccharomyces cerevisiae Aro8, a putative alpha-
RT aminoadipate aminotransferase.";
RL Protein Sci. 22:1417-1424(2013).
CC -!- FUNCTION: General aromatic amino acid transaminase involved in several
CC otherwise unrelated metabolic pathways. Responsible for phenylalanine
CC and tyrosine biosynthesis. Active with glutamate, phenylalanine,
CC tyrosine and tryptophan as amino donors and with phenylpyruvate,
CC hydroxyphenylpyruvate, 2-oxoglutarate and pyruvate as amino acceptors.
CC Also active with methionine, alpha-aminoadipate and leucine as amino
CC donors when phenylpyruvate is the amino acceptor and in the reverse
CC reactions with the corresponding oxo acids and phenylalanine as amino
CC donor. Catalyzes the formation of methionine from 2-keto-4-
CC methylthiobutyrate (KMTB) in the methionine salvage pathway primarily
CC using aromatic amino acids (tyrosine, phenylalanine and tryptophan) as
CC the amino donors. Catalyzes the formation of alpha-aminoadipate from
CC alpha-ketoadipate in the lysine biosyntheic pathway.
CC {ECO:0000269|PubMed:18625006, ECO:0000269|PubMed:21982920,
CC ECO:0000269|PubMed:6763508, ECO:0000269|PubMed:9491082,
CC 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: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:9491082};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-2-aminoadipate = 2-oxoadipate + L-
CC glutamate; Xref=Rhea:RHEA:12601, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:57499, ChEBI:CHEBI:58672; EC=2.6.1.39;
CC Evidence={ECO:0000269|PubMed:9491082};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:23893908};
CC -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis; L-
CC phenylalanine from phenylpyruvate (ArAT route): step 1/1.
CC {ECO:0000269|PubMed:9491082}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-tyrosine biosynthesis; L-tyrosine
CC from (4-hydroxyphenyl)pyruvate: step 1/1. {ECO:0000269|PubMed:9491082}.
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:9491082}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA
CC pathway; L-alpha-aminoadipate from 2-oxoglutarate: step 5/5.
CC {ECO:0000269|PubMed:9491082}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1770 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; Y13624; CAA73946.1; -; Genomic_DNA.
DR EMBL; Z72724; CAA96914.1; -; Genomic_DNA.
DR EMBL; AY692962; AAT92981.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07913.1; -; Genomic_DNA.
DR PIR; S64220; S64220.
DR RefSeq; NP_011313.1; NM_001181067.1.
DR PDB; 4JE5; X-ray; 1.91 A; A/B/C/D=1-500.
DR PDBsum; 4JE5; -.
DR AlphaFoldDB; P53090; -.
DR SMR; P53090; -.
DR BioGRID; 33055; 149.
DR DIP; DIP-983N; -.
DR IntAct; P53090; 6.
DR MINT; P53090; -.
DR STRING; 4932.YGL202W; -.
DR iPTMnet; P53090; -.
DR MaxQB; P53090; -.
DR PaxDb; P53090; -.
DR PRIDE; P53090; -.
DR EnsemblFungi; YGL202W_mRNA; YGL202W; YGL202W.
DR GeneID; 852672; -.
DR KEGG; sce:YGL202W; -.
DR SGD; S000003170; ARO8.
DR VEuPathDB; FungiDB:YGL202W; -.
DR eggNOG; KOG0634; Eukaryota.
DR HOGENOM; CLU_017584_0_5_1; -.
DR InParanoid; P53090; -.
DR OMA; TMCKQFS; -.
DR BioCyc; MetaCyc:YGL202W-MON; -.
DR BioCyc; YEAST:YGL202W-MON; -.
DR BRENDA; 2.6.1.39; 984.
DR BRENDA; 2.6.1.57; 984.
DR UniPathway; UPA00033; UER00031.
DR UniPathway; UPA00121; UER00347.
DR UniPathway; UPA00122; UER00350.
DR UniPathway; UPA00904; UER00879.
DR PRO; PR:P53090; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53090; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0047536; F:2-aminoadipate transaminase activity; IDA:SGD.
DR GO; GO:0008793; F:aromatic-amino-acid:2-oxoglutarate aminotransferase activity; IMP:SGD.
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: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 3D-structure; Aminotransferase; Cytoplasm; Phosphoprotein;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..500
FT /note="Aromatic/aminoadipate aminotransferase 1"
FT /id="PRO_0000064678"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:4JE5"
FT HELIX 15..19
FT /evidence="ECO:0007829|PDB:4JE5"
FT HELIX 24..29
FT /evidence="ECO:0007829|PDB:4JE5"
FT TURN 30..33
FT /evidence="ECO:0007829|PDB:4JE5"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:4JE5"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:4JE5"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:4JE5"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:4JE5"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:4JE5"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:4JE5"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:4JE5"
FT HELIX 112..125
FT /evidence="ECO:0007829|PDB:4JE5"
FT STRAND 133..139
FT /evidence="ECO:0007829|PDB:4JE5"
FT HELIX 141..152
FT /evidence="ECO:0007829|PDB:4JE5"
FT STRAND 158..164
FT /evidence="ECO:0007829|PDB:4JE5"
FT HELIX 167..175
FT /evidence="ECO:0007829|PDB:4JE5"
FT STRAND 179..183
FT /evidence="ECO:0007829|PDB:4JE5"
FT HELIX 192..200
FT /evidence="ECO:0007829|PDB:4JE5"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:4JE5"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:4JE5"
FT HELIX 228..241
FT /evidence="ECO:0007829|PDB:4JE5"
FT STRAND 244..248
FT /evidence="ECO:0007829|PDB:4JE5"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:4JE5"
FT HELIX 263..271
FT /evidence="ECO:0007829|PDB:4JE5"
FT HELIX 277..283
FT /evidence="ECO:0007829|PDB:4JE5"
FT HELIX 288..291
FT /evidence="ECO:0007829|PDB:4JE5"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:4JE5"
FT STRAND 297..303
FT /evidence="ECO:0007829|PDB:4JE5"
FT TURN 304..307
FT /evidence="ECO:0007829|PDB:4JE5"
FT HELIX 309..311
FT /evidence="ECO:0007829|PDB:4JE5"
FT STRAND 314..319
FT /evidence="ECO:0007829|PDB:4JE5"
FT HELIX 320..331
FT /evidence="ECO:0007829|PDB:4JE5"
FT TURN 332..334
FT /evidence="ECO:0007829|PDB:4JE5"
FT HELIX 339..382
FT /evidence="ECO:0007829|PDB:4JE5"
FT STRAND 395..405
FT /evidence="ECO:0007829|PDB:4JE5"
FT HELIX 406..408
FT /evidence="ECO:0007829|PDB:4JE5"
FT TURN 410..418
FT /evidence="ECO:0007829|PDB:4JE5"
FT HELIX 420..433
FT /evidence="ECO:0007829|PDB:4JE5"
FT HELIX 441..444
FT /evidence="ECO:0007829|PDB:4JE5"
FT HELIX 456..459
FT /evidence="ECO:0007829|PDB:4JE5"
FT STRAND 466..476
FT /evidence="ECO:0007829|PDB:4JE5"
FT HELIX 478..495
FT /evidence="ECO:0007829|PDB:4JE5"
SQ SEQUENCE 500 AA; 56178 MW; D0D111640D2C560D CRC64;
MTLPESKDFS YLFSDETNAR KPSPLKTCIH LFQDPNIIFL GGGLPLKDYF PWDNLSVDSP
KPPFPQGIGA PIDEQNCIKY TVNKDYADKS ANPSNDIPLS RALQYGFSAG QPELLNFIRD
HTKIIHDLKY KDWDVLATAG NTNAWESTLR VFCNRGDVIL VEAHSFSSSL ASAEAQGVIT
FPVPIDADGI IPEKLAKVME NWTPGAPKPK LLYTIPTGQN PTGTSIADHR KEAIYKIAQK
YDFLIVEDEP YYFLQMNPYI KDLKEREKAQ SSPKQDHDEF LKSLANTFLS LDTEGRVIRM
DSFSKVLAPG TRLGWITGSS KILKPYLSLH EMTIQAPAGF TQVLVNATLS RWGQKGYLDW
LLGLRHEYTL KRDCAIDALY KYLPQSDAFV INPPIAGMFF TVNIDASVHP EFKTKYNSDP
YQLEQSLYHK VVERGVLVVP GSWFKSEGET EPPQPAESKE VSNPNIIFFR GTYAAVSPEK
LTEGLKRLGD TLYEEFGISK
