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 27-MAR-2024, entry version 122.
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; 284812.Q9Y7S6; -.
DR iPTMnet; Q9Y7S6; -.
DR MaxQB; Q9Y7S6; -.
DR PaxDb; 4896-SPCC569-07-1; -.
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; PYFFLRL; -.
DR PhylomeDB; Q9Y7S6; -.
DR Reactome; R-SPO-71064; Lysine catabolism.
DR Reactome; R-SPO-71240; Tryptophan catabolism.
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: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 CDD; cd00609; AAT_like; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR PANTHER; PTHR42790; AMINOTRANSFERASE; 1.
DR PANTHER; PTHR42790:SF21; AROMATIC_AMINOADIPATE AMINOTRANSFERASE 1; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 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
//
