ID   AATR3_SCHPO             Reviewed;         470 AA.
AC   Q9Y7S6;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 115.
DE   RecName: Full=Aromatic amino acid aminotransferase C569.07;
DE            EC=2.6.1.57;
GN   ORFNames=SPCC569.07;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1] {ECO:0000312|EMBL:CAB42068.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2] {ECO:0000305}
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
CC   -!- FUNCTION: Has aromatic amino acid transaminase activity.
CC       {ECO:0000250|UniProtKB:P53090}.
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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:P00509};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000255}.
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DR   EMBL; CU329672; CAB42068.1; -; Genomic_DNA.
DR   PIR; T41409; T41409.
DR   RefSeq; NP_588566.1; NM_001023553.2.
DR   AlphaFoldDB; Q9Y7S6; -.
DR   SMR; Q9Y7S6; -.
DR   BioGRID; 275360; 5.
DR   STRING; 4896.SPCC569.07.1; -.
DR   iPTMnet; Q9Y7S6; -.
DR   MaxQB; Q9Y7S6; -.
DR   PaxDb; Q9Y7S6; -.
DR   EnsemblFungi; SPCC569.07.1; SPCC569.07.1:pep; SPCC569.07.
DR   GeneID; 2538779; -.
DR   KEGG; spo:SPCC569.07; -.
DR   PomBase; SPCC569.07; -.
DR   VEuPathDB; FungiDB:SPCC569.07; -.
DR   eggNOG; KOG0634; Eukaryota.
DR   HOGENOM; CLU_017584_0_5_1; -.
DR   InParanoid; Q9Y7S6; -.
DR   OMA; EAGPSKM; -.
DR   PhylomeDB; Q9Y7S6; -.
DR   PRO; PR:Q9Y7S6; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0047536; F:2-aminoadipate transaminase activity; IBA:GO_Central.
DR   GO; GO:0008793; F:aromatic-amino-acid:2-oxoglutarate aminotransferase activity; IBA:GO_Central.
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:0019878; P:lysine biosynthetic process via aminoadipic acid; IBA:GO_Central.
DR   GO; GO:0006571; P:tyrosine biosynthetic process; IBA:GO_Central.
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   3: Inferred from homology;
KW   Aminotransferase; Cytoplasm; Pyridoxal phosphate; Reference proteome;
KW   Transferase.
FT   CHAIN           1..470
FT                   /note="Aromatic amino acid aminotransferase C569.07"
FT                   /id="PRO_0000308491"
SQ   SEQUENCE   470 AA;  53614 MW;  E361A1885B80879D CRC64;
     MDNLKKKYQH HLSLESASRE YGPFQMLGRI QSDSDIKMLS FAGGEPNPSK FPIHKLSVSF
     PEVNSWEKDT NKDATVSYEL SNNANEGSLD LLGALQYGQC QGIPELVKFI KDHVGQIHMP
     QYKDWDIKIT NGNTIGLEYC LRLLVNRGDC ILIEKYTYPA AITAMRPLGV KFIPIDMDEN
     GMLPESFEKV METWDSSLGA RPHVLYTIPT GQNPTGSTLT LERRKKFLTL AKKYDIIIVE
     DEPYYFLQME KYDANWKPDK QAFNISSFKK KLIPSLLHLD TDGRVLRVDS FSKLIVPGLR
     LGWITGNSLF IDRITRYAEV CTESPSGVSQ VVLYAILNRW GQNGFLEWLQ DLQNSYTMRR
     NALLLAADKH LPKSVCKYHS PKAGLFLWVE LDKNRLICSN MDKSISEIEM EIFVELVNNG
     VKPVCGQLFM GEPNSADKIF FRFAYSLADL STFEAGLERF TSTIQKYFQL