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Protein

Tyrosine aminotransferase

Gene

tyrB

Organism
Klebsiella pneumoniae
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

catalyzes the formation of methionine from 2-keto-4-methylthiobutyrate (KMTB) primarily using aromatic amino acids (tyrosine, phenylalanine and tryptophan) or glutamate as the amino donors. Histidine, leucine, asparagine, or arginine are also functional amino donors but to a lesser extent. Can also use alpha-ketoglutarate, oxaloacetate and pyruvate as the amino acceptors.

Catalytic activityi

L-tyrosine + 2-oxoglutarate = 4-hydroxyphenylpyruvate + L-glutamate.
L-tyrosine + 4-(methylthio)-2-oxobutanoate = hydroxyphenylpyruvate + methionine.
An aromatic amino acid + 2-oxoglutarate = an aromatic oxo acid + L-glutamate.
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate.

Cofactori

Enzyme regulationi

Inhibited by malate and nitrotyrosine by approximately 20% at the higher concentration. At 100 µM, canaline and carboxymethoxylamine inhibit aminotransferase activity by 35 and 70%, respectively. Addition of 1.0 mM carboxymethoxylamine lead to a complete inhibition of the aminotransferase activity.1 Publication

Kineticsi

  1. KM=1.42 mM for tryptophan (at pH 7.4 and 10 mM KMTB)1 Publication
  2. KM=2.01 mM for tyrosine (at pH 7.4 and 10 mM KMTB)1 Publication
  3. KM=2.01 mM for phenylalanine (at pH 7.4 and 10 mM KMTB)1 Publication
  4. KM=2.46 mM for KMTB (at pH 7.4 and 5 mM tyrosine)1 Publication
  5. KM=3.00 mM for alpha-ketoglutarate (at pH 7.4 and 5 mM tyrosine)1 Publication
  6. KM=6.00 mM for oxaloacetate (at pH 7.4 and 5 mM tyrosine)1 Publication
  7. KM=11.93 mM for glutamate (at pH 7.4 and 10 mM KMTB)1 Publication
  8. KM=20.13 mM for pyruvate (at pH 7.4 and 5 mM tyrosine)1 Publication
  1. Vmax=0.09 µmol/min/mg enzyme with pyruvate and tyrosine as substrates(at pH 7.4)1 Publication
  2. Vmax=1.80 µmol/min/mg enzyme with phenylalanine and KMTB as substrates (at pH 7.4)1 Publication
  3. Vmax=2.63 µmol/min/mg enzyme with tryptophan and KMTB as substrates(at pH 7.4)1 Publication
  4. Vmax=3.25 µmol/min/mg enzyme with tyrosine and KMTB as substrates(at pH 7.4)1 Publication
  5. Vmax=3.29 µmol/min/mg enzyme with phenylalanine and tyrosine as substrates(at pH 7.4)1 Publication
  6. Vmax=5.21 µmol/min/mg enzyme with alpha-ketoglutarate and tyrosine as substrates(at pH 7.4)1 Publication
  7. Vmax=7.39 µmol/min/mg enzyme with oxaloacetate and tyrosine as substrates(at pH 7.4)1 Publication
  8. Vmax=7.65 µmol/min/mg enzyme with glutamate and KMTB as substrates (at pH 7.4)1 Publication

Pathwayi: L-methionine biosynthesis via salvage pathway

This protein is involved in step 6 of the subpathway that synthesizes L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate.
Proteins known to be involved in the 6 steps of the subpathway in this organism are:
  1. Methylthioribose-1-phosphate isomerase (mtnA), Methylthioribose-1-phosphate isomerase (mtnA), Methylthioribose-1-phosphate isomerase (mtnA), Methylthioribose-1-phosphate isomerase (mtnA), Methylthioribose-1-phosphate isomerase (mtnA), Methylthioribose-1-phosphate isomerase (mtnA), Methylthioribose-1-phosphate isomerase (mtnA), Methylthioribose-1-phosphate isomerase (mtnA), Methylthioribose-1-phosphate isomerase (mtnA), Methylthioribose-1-phosphate isomerase (mtnA), Methylthioribose-1-phosphate isomerase (mtnA), Methylthioribose-1-phosphate isomerase (mtnA), Methylthioribose-1-phosphate isomerase (mtnA)
  2. Methylthioribulose-1-phosphate dehydratase (mtnB), Methylthioribulose-1-phosphate dehydratase (mtnB), Methylthioribulose-1-phosphate dehydratase (mtnB), Methylthioribulose-1-phosphate dehydratase (mtnB), Methylthioribulose-1-phosphate dehydratase (mtnB), Methylthioribulose-1-phosphate dehydratase (mtnB)
  3. Enolase-phosphatase E1 (mtnC), Enolase-phosphatase E1 (mtnC), Enolase-phosphatase E1 (mtnC), Enolase-phosphatase E1 (mtnC), Enolase-phosphatase E1 (mtnC), Enolase-phosphatase E1 (mtnC), Enolase-phosphatase E1 (mtnC), Enolase-phosphatase E1 (mtnC), Enolase-phosphatase E1 (mtnC), Enolase-phosphatase E1 (mtnC), Enolase-phosphatase E1 (mtnC), Enolase-phosphatase E1 (mtnC), Enolase-phosphatase E1 (mtnC)
  4. Enolase-phosphatase E1 (mtnC), Enolase-phosphatase E1 (mtnC), Enolase-phosphatase E1 (mtnC), Enolase-phosphatase E1 (mtnC), Enolase-phosphatase E1 (mtnC), Enolase-phosphatase E1 (mtnC), Enolase-phosphatase E1 (mtnC), Enolase-phosphatase E1 (mtnC), Enolase-phosphatase E1 (mtnC), Enolase-phosphatase E1 (mtnC), Enolase-phosphatase E1 (mtnC), Enolase-phosphatase E1 (mtnC), Enolase-phosphatase E1 (mtnC)
  5. Acireductone dioxygenase (mtnD), Acireductone dioxygenase (mtnD), Acireductone dioxygenase (mtnD), Acireductone dioxygenase (mtnD), Acireductone dioxygenase (mtnD), Acireductone dioxygenase (mtnD)
  6. Tyrosine aminotransferase (tyrB)
This subpathway is part of the pathway L-methionine biosynthesis via salvage pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate, the pathway L-methionine biosynthesis via salvage pathway and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei34Substrate; via amide nitrogenBy similarity1
Binding sitei66SubstrateBy similarity1
Binding sitei131SubstrateBy similarity1
Binding sitei184SubstrateBy similarity1
Binding sitei375SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

  • L-methionine salvage from methylthioadenosine Source: CACAO

Keywordsi

Molecular functionAminotransferase, Transferase
LigandPyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-1302
UniPathwayiUPA00904; UER00879

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine aminotransferase (EC:2.6.1.5)
Short name:
TyrAT
Alternative name(s):
Aromatic-amino-acid transaminase (EC:2.6.1.57)
Aspartate aminotransferase (EC:2.6.1.1)
Gene namesi
Name:tyrB
OrganismiKlebsiella pneumoniae
Taxonomic identifieri573 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeKlebsiella

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003588721 – 397Tyrosine aminotransferaseAdd BLAST397

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei247N6-(pyridoxal phosphate)lysineBy similarity1

Proteomic databases

PRIDEiO85746

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

3D structure databases

ProteinModelPortaliO85746
SMRiO85746
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CGF Bacteria
COG1448 LUCA

Family and domain databases

Gene3Di3.40.640.10, 1 hit
3.90.1150.10, 2 hits
InterProiView protein in InterPro
IPR004839 Aminotransferase_I/II
IPR000796 Asp_trans
IPR004838 NHTrfase_class1_PyrdxlP-BS
IPR015424 PyrdxlP-dep_Trfase
IPR015422 PyrdxlP-dep_Trfase_dom1
IPR015421 PyrdxlP-dep_Trfase_major
PANTHERiPTHR11879 PTHR11879, 1 hit
PfamiView protein in Pfam
PF00155 Aminotran_1_2, 1 hit
PRINTSiPR00799 TRANSAMINASE
SUPFAMiSSF53383 SSF53383, 1 hit
PROSITEiView protein in PROSITE
PS00105 AA_TRANSFER_CLASS_1, 1 hit

Sequencei

Sequence statusi: Complete.

O85746-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFQKVDAYAG DPILSLMERF KEDPRSDKVN LSIGLYYNDD GIIPQLQAVA
60 70 80 90 100
EAEARLNAEP HGASLYLPME GFSGYRQAIA PLLFGAEHTA LKQNRIASIQ
110 120 130 140 150
TVGGSGALKV GADFLKRYFP ESHVWVSDPT WENHIAIFEG AGFEVSTYPW
160 170 180 190 200
FDKATNGVRF ENLLAMLQTL PARDIVLLHP CCHNPTGADL TPAQWDRVVE
210 220 230 240 250
VLKARQLIPF LDIAYQGFGG GLEEDAYAIR AIASAGMPML VSNSFSKIFS
260 270 280 290 300
LYGERVGGLS VVCEDSETAG RVLGQLKATV RRNYSSPPSF GAQVVATVLN
310 320 330 340 350
DAALKATWQA EVDAMRAHIL TMRQALVDAL QQVAPGSKVD YLLKQRGMFS
360 370 380 390
YTGFSAAQVD RLRDEFGVYL IASGRMRVAG LNSRNVQQVA KAFVAVM
Length:397
Mass (Da):43,432
Last modified:November 1, 1998 - v1
Checksum:i43079DDE86C104CE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF074934 Genomic DNA Translation: AAC26140.1

Genome annotation databases

KEGGiag:AAC26140

Similar proteinsi

Entry informationi

Entry nameiTYRB_KLEPN
AccessioniPrimary (citable) accession number: O85746
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: November 1, 1998
Last modified: April 25, 2018
This is version 79 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing
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Main funding by: National Institutes of Health