AATR2_SCHPO
ID AATR2_SCHPO Reviewed; 481 AA.
AC O94570;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Aromatic amino acid aminotransferase C1773.13;
DE EC=2.6.1.57;
GN ORFNames=SPBC1773.13;
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:CAA21918.1}
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; CU329671; CAA21918.1; -; Genomic_DNA.
DR PIR; T39678; T39678.
DR RefSeq; NP_595128.1; NM_001021035.2.
DR AlphaFoldDB; O94570; -.
DR SMR; O94570; -.
DR STRING; 4896.SPBC1773.13.1; -.
DR PaxDb; O94570; -.
DR EnsemblFungi; SPBC1773.13.1; SPBC1773.13.1:pep; SPBC1773.13.
DR GeneID; 2540092; -.
DR KEGG; spo:SPBC1773.13; -.
DR PomBase; SPBC1773.13; -.
DR VEuPathDB; FungiDB:SPBC1773.13; -.
DR eggNOG; KOG0634; Eukaryota.
DR HOGENOM; CLU_017584_0_5_1; -.
DR InParanoid; O94570; -.
DR OMA; HAPRYEN; -.
DR PhylomeDB; O94570; -.
DR PRO; PR:O94570; -.
DR Proteomes; UP000002485; Chromosome II.
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; ISO:PomBase.
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..481
FT /note="Aromatic amino acid aminotransferase C1773.13"
FT /id="PRO_0000308490"
SQ SEQUENCE 481 AA; 54756 MW; 0476C46731B5E1C5 CRC64;
MIRNSEDFSH HLSRESKARE KGPFQMLGRI KSSTGIDAIS FSSGLPHPNK FAIRELSIKF
PQLGCFKEEN GTYAKEVNVT FNIKADPSEG LLNFSQSLQY GQCQGISELV GFIKEHIRRI
HAPRYENWDI KMSNGNTSGL EYCLRLLVNY GDHVLTEKYT YPAAITAMRA LGVQFVSVDM
DSEGMLPESL EEIMRDWDIS LGPRPHVLYT VPTGQNPTGS TLSLSRRKKL LALARKYDII
IVEDEPYYFL QMEDYNGSLN PAQQKCDGST FLKSLVPSLL SLDTEGRVLR LDSFSKLIAP
GTRLGYITGN SMFIDHITRI AEVCTESPSG ICQSVLYAML HNWGQEGFCA WLQELQYSYT
VRRNAFLNVA NKYLPNSVCI YHVPRAGLFL WVELNLNHYR FSDTKKSVSQ IEMEIFLALV
EKGVKTVCGQ FFMANPERST KIFFRFAYSI ADFEDFEEGI KRFTSVINEH FNVESRVRIC
P
