AATR2_DICDI
ID AATR2_DICDI Reviewed; 440 AA.
AC Q54K00;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Aromatic amino acid aminotransferase DDB_G0287711;
DE EC=2.6.1.57;
GN ORFNames=DDB_G0287711;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Has aromatic amino acid transaminase activity. {ECO:0000250}.
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};
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AAFI02000104; EAL63502.1; -; Genomic_DNA.
DR RefSeq; XP_637002.1; XM_631910.1.
DR AlphaFoldDB; Q54K00; -.
DR SMR; Q54K00; -.
DR STRING; 44689.DDB0187583; -.
DR PaxDb; Q54K00; -.
DR EnsemblProtists; EAL63502; EAL63502; DDB_G0287711.
DR GeneID; 8626257; -.
DR KEGG; ddi:DDB_G0287711; -.
DR dictyBase; DDB_G0287711; -.
DR eggNOG; KOG0634; Eukaryota.
DR HOGENOM; CLU_017584_0_6_1; -.
DR InParanoid; Q54K00; -.
DR OMA; GGCFNNY; -.
DR PhylomeDB; Q54K00; -.
DR Reactome; R-DDI-71064; Lysine catabolism.
DR Reactome; R-DDI-71240; Tryptophan catabolism.
DR PRO; PR:Q54K00; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0009058; P:biosynthetic process; IEA:InterPro.
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..440
FT /note="Aromatic amino acid aminotransferase DDB_G0287711"
FT /id="PRO_0000331117"
FT MOD_RES 277
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 440 AA; 49651 MW; 6654C710285BC061 CRC64;
MTEKSNIIKD YTYFLSKRGK LKEASPIRSL FQYSSLPGMI SLGGGLPNAS TFPFKSINIE
LKDGSKLEIE GSDLEEAFQY SPTPGLPRLQ KALKDLQIRQ HNLCPPDEAG KEWNLIISNG
SQESLANAFE VLIDDNDSII TENPTYSGTL SILKPLSLNI CGIETDRYGM IPEKLQRLLS
EWDHSKFKFP RVIYLIPCGQ NPSGTTMNHQ RKLDIYSICS KYNLLIIEDD PYYYLQFESS
ENADDDDGAS CSSLNLGKSL LSMDVDGRVL RFDSLSKILS SGLRIGFVTG NKQLLEKINF
HQQSTTLHSS GLSQAVVLSL LNKWGVEKWN QHISFIQRFY LEKRNQMIDS IDKHLKGLVE
FNIPSAGMFI WFKLPVEDSK TLIFKNAVEK KILLVPGISF STDSTKPSQF VRASYSTASK
EQIDEAIKRF ADLLNEELKK