TYRB_KLEPN
ID TYRB_KLEPN Reviewed; 397 AA.
AC O85746;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Tyrosine aminotransferase;
DE Short=TyrAT;
DE EC=2.6.1.5;
DE AltName: Full=Aromatic-amino-acid transaminase;
DE EC=2.6.1.57;
DE AltName: Full=Aspartate aminotransferase;
DE EC=2.6.1.1;
GN Name=tyrB;
OS Klebsiella pneumoniae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=573;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-22,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND SUBUNIT.
RC STRAIN=ATCC 13883 / DSM 30104 / JCM 1662 / NBRC 14940 / NCIMB 13281 / NCTC
RC 9633;
RX PubMed=10074065; DOI=10.1128/jb.181.6.1739-1747.1999;
RA Heilbronn J., Wilson J., Berger B.J.;
RT "Tyrosine aminotransferase catalyzes the final step of methionine recycling
RT in Klebsiella pneumoniae.";
RL J. Bacteriol. 181:1739-1747(1999).
CC -!- FUNCTION: catalyzes the formation of methionine from 2-keto-4-
CC methylthiobutyrate (KMTB) primarily using aromatic amino acids
CC (tyrosine, phenylalanine and tryptophan) or glutamate as the amino
CC donors. Histidine, leucine, asparagine, or arginine are also functional
CC amino donors but to a lesser extent. Can also use alpha-ketoglutarate,
CC oxaloacetate and pyruvate as the amino acceptors.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-tyrosine = 3-(4-hydroxyphenyl)pyruvate + L-
CC glutamate; Xref=Rhea:RHEA:15093, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:36242, ChEBI:CHEBI:58315; EC=2.6.1.5;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-tyrosine = 3-(4-hydroxyphenyl)pyruvate + L-
CC glutamate; Xref=Rhea:RHEA:15093, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:36242, ChEBI:CHEBI:58315; EC=2.6.1.57;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-methylsulfanyl-2-oxobutanoate + L-tyrosine = 3-(4-
CC hydroxyphenyl)pyruvate + L-methionine; Xref=Rhea:RHEA:47084,
CC ChEBI:CHEBI:16723, ChEBI:CHEBI:36242, ChEBI:CHEBI:57844,
CC ChEBI:CHEBI:58315;
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 -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate;
CC Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000305};
CC -!- ACTIVITY REGULATION: Inhibited by malate and nitrotyrosine by
CC approximately 20% at the higher concentration. At 100 uM, canaline and
CC carboxymethoxylamine inhibit aminotransferase activity by 35 and 70%,
CC respectively. Addition of 1.0 mM carboxymethoxylamine lead to a
CC complete inhibition of the aminotransferase activity.
CC {ECO:0000269|PubMed:10074065}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.42 mM for tryptophan (at pH 7.4 and 10 mM KMTB)
CC {ECO:0000269|PubMed:10074065};
CC KM=2.01 mM for tyrosine (at pH 7.4 and 10 mM KMTB)
CC {ECO:0000269|PubMed:10074065};
CC KM=2.01 mM for phenylalanine (at pH 7.4 and 10 mM KMTB)
CC {ECO:0000269|PubMed:10074065};
CC KM=2.46 mM for KMTB (at pH 7.4 and 5 mM tyrosine)
CC {ECO:0000269|PubMed:10074065};
CC KM=3.00 mM for alpha-ketoglutarate (at pH 7.4 and 5 mM tyrosine)
CC {ECO:0000269|PubMed:10074065};
CC KM=6.00 mM for oxaloacetate (at pH 7.4 and 5 mM tyrosine)
CC {ECO:0000269|PubMed:10074065};
CC KM=11.93 mM for glutamate (at pH 7.4 and 10 mM KMTB)
CC {ECO:0000269|PubMed:10074065};
CC KM=20.13 mM for pyruvate (at pH 7.4 and 5 mM tyrosine)
CC {ECO:0000269|PubMed:10074065};
CC Vmax=0.09 umol/min/mg enzyme with pyruvate and tyrosine as
CC substrates(at pH 7.4) {ECO:0000269|PubMed:10074065};
CC Vmax=1.80 umol/min/mg enzyme with phenylalanine and KMTB as
CC substrates (at pH 7.4) {ECO:0000269|PubMed:10074065};
CC Vmax=2.63 umol/min/mg enzyme with tryptophan and KMTB as
CC substrates(at pH 7.4) {ECO:0000269|PubMed:10074065};
CC Vmax=3.25 umol/min/mg enzyme with tyrosine and KMTB as substrates(at
CC pH 7.4) {ECO:0000269|PubMed:10074065};
CC Vmax=3.29 umol/min/mg enzyme with phenylalanine and tyrosine as
CC substrates(at pH 7.4) {ECO:0000269|PubMed:10074065};
CC Vmax=5.21 umol/min/mg enzyme with alpha-ketoglutarate and tyrosine as
CC substrates(at pH 7.4) {ECO:0000269|PubMed:10074065};
CC Vmax=7.39 umol/min/mg enzyme with oxaloacetate and tyrosine as
CC substrates(at pH 7.4) {ECO:0000269|PubMed:10074065};
CC Vmax=7.65 umol/min/mg enzyme with glutamate and KMTB as substrates
CC (at pH 7.4) {ECO:0000269|PubMed:10074065};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via salvage
CC pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate:
CC step 6/6.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10074065}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AF074934; AAC26140.1; -; Genomic_DNA.
DR AlphaFoldDB; O85746; -.
DR SMR; O85746; -.
DR KEGG; ag:AAC26140; -.
DR BioCyc; MetaCyc:MON-1302; -.
DR SABIO-RK; O85746; -.
DR UniPathway; UPA00904; UER00879.
DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
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; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IDA:CACAO.
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 1: Evidence at protein level;
KW Aminotransferase; Direct protein sequencing; Pyridoxal phosphate;
KW Transferase.
FT CHAIN 1..397
FT /note="Tyrosine aminotransferase"
FT /id="PRO_0000358872"
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 375
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 247
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 397 AA; 43432 MW; 43079DDE86C104CE CRC64;
MFQKVDAYAG DPILSLMERF KEDPRSDKVN LSIGLYYNDD GIIPQLQAVA EAEARLNAEP
HGASLYLPME GFSGYRQAIA PLLFGAEHTA LKQNRIASIQ TVGGSGALKV GADFLKRYFP
ESHVWVSDPT WENHIAIFEG AGFEVSTYPW FDKATNGVRF ENLLAMLQTL PARDIVLLHP
CCHNPTGADL TPAQWDRVVE VLKARQLIPF LDIAYQGFGG GLEEDAYAIR AIASAGMPML
VSNSFSKIFS LYGERVGGLS VVCEDSETAG RVLGQLKATV RRNYSSPPSF GAQVVATVLN
DAALKATWQA EVDAMRAHIL TMRQALVDAL QQVAPGSKVD YLLKQRGMFS YTGFSAAQVD
RLRDEFGVYL IASGRMRVAG LNSRNVQQVA KAFVAVM
