TYRB_SALTY
ID TYRB_SALTY Reviewed; 397 AA.
AC P74861;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 3.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Aromatic-amino-acid aminotransferase;
DE Short=ARAT;
DE Short=AROAT;
DE EC=2.6.1.57;
GN Name=tyrB; OrderedLocusNames=STM4248;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8809108; DOI=10.1016/0167-4781(96)00113-3;
RA Nakai Y., Hayashi H., Kagamiyama H.;
RT "Cloning and characterization of the tyrB gene from Salmonella
RT typhimurium.";
RL Biochim. Biophys. Acta 1308:189-192(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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 -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis; L-
CC phenylalanine from phenylpyruvate (ArAT route): step 1/1.
CC -!- PATHWAY: Amino-acid biosynthesis; L-tyrosine biosynthesis; L-tyrosine
CC from (4-hydroxyphenyl)pyruvate: step 1/1.
CC -!- SUBUNIT: Homodimer. {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; Z68874; CAA93080.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL23072.1; -; Genomic_DNA.
DR PIR; S71928; S71928.
DR RefSeq; NP_463113.1; NC_003197.2.
DR RefSeq; WP_000486903.1; NC_003197.2.
DR AlphaFoldDB; P74861; -.
DR SMR; P74861; -.
DR STRING; 99287.STM4248; -.
DR PaxDb; P74861; -.
DR EnsemblBacteria; AAL23072; AAL23072; STM4248.
DR GeneID; 1255774; -.
DR KEGG; stm:STM4248; -.
DR PATRIC; fig|99287.12.peg.4468; -.
DR HOGENOM; CLU_032440_1_2_6; -.
DR OMA; WDQNKRQ; -.
DR PhylomeDB; P74861; -.
DR BioCyc; SENT99287:STM4248-MON; -.
DR UniPathway; UPA00121; UER00347.
DR UniPathway; UPA00122; UER00350.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR GO; GO:0080130; F:L-phenylalanine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004838; F:L-tyrosine:2-oxoglutarate aminotransferase activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0008483; F:transaminase activity; IBA:GO_Central.
DR GO; GO:0033585; P:L-phenylalanine biosynthetic process from chorismate via phenylpyruvate; IBA:GO_Central.
DR GO; GO:0006571; P:tyrosine biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR000796; Asp_trans.
DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11879; PTHR11879; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR PRINTS; PR00799; TRANSAMINASE.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aminotransferase;
KW Aromatic amino acid biosynthesis; Cytoplasm; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..397
FT /note="Aromatic-amino-acid aminotransferase"
FT /id="PRO_0000123893"
FT BINDING 34
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 66
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 281
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 375
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 247
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 331
FT /note="K -> T (in Ref. 1; CAA93080)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 397 AA; 43527 MW; BD2CE994DB3FF8F2 CRC64;
MFQKVDAYAG DPILSLMERF KDDSRHDKVN LSIGLYYNED GIIPQLKTVA EAEARLNAQP
HGASLYLPME GLNTYRHTIA PLLFGADHPV LQQQRVATIQ TLGGSGALKV GADFLKRYFP
DAGVWVSDPT WENHIAIFAG AGFEVSTYPW YDDATNGIRF NDLLATLNTL PARSIVLLHP
CCHNPTGADL TPSQWDAVIE IVKARDLIPF LDIAYQGFGA GMDDDAYVIR AIASAGLPAL
VSNSFSKIFS LYGERVGGLS VVCEDAEIAA RVLGQLKATV RRIYSSPPCF GAQVVATVLG
DEALKAGWLA EVDAMRNRII SMRQTLVKEL KAEMPDRNFD YLLQQRGMFS YTGLSEEQVD
RLRDEFGVYL IASGRMCVAG LNASNVHRVA KAFAAVM
