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Protein

Tyrosine aminotransferase

Gene

tyrB

Organism
Klebsiella pneumoniae
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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)
  2. 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)
  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)
  5. 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei34 – 341Substrate; via amide nitrogenBy similarity
Binding sitei66 – 661SubstrateBy similarity
Binding sitei131 – 1311SubstrateBy similarity
Binding sitei184 – 1841SubstrateBy similarity
Binding sitei375 – 3751SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

  • L-methionine biosynthetic process from methylthioadenosine Source: CACAO
Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Ligandi

Pyridoxal 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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeKlebsiella

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 397397Tyrosine aminotransferasePRO_0000358872Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei247 – 2471N6-(pyridoxal phosphate)lysineBy similarity

Proteomic databases

PRIDEiO85746.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi272620.KPN_04441.

Structurei

3D structure databases

ProteinModelPortaliO85746.
SMRiO85746. Positions 1-397.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CGF. Bacteria.
COG1448. LUCA.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
InterProiIPR004839. Aminotransferase_I/II.
IPR000796. Asp_trans.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PANTHERiPTHR11879. PTHR11879. 1 hit.
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
PRINTSiPR00799. TRANSAMINASE.
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view]

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.

Cross-referencesi

Sequence databases

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

3D structure databases

ProteinModelPortaliO85746.
SMRiO85746. Positions 1-397.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272620.KPN_04441.

Proteomic databases

PRIDEiO85746.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAC26140.

Phylogenomic databases

eggNOGiENOG4105CGF. Bacteria.
COG1448. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00904; UER00879.
BioCyciMetaCyc:MONOMER-1302.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
InterProiIPR004839. Aminotransferase_I/II.
IPR000796. Asp_trans.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PANTHERiPTHR11879. PTHR11879. 1 hit.
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
PRINTSiPR00799. TRANSAMINASE.
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Tyrosine aminotransferase catalyzes the final step of methionine recycling in Klebsiella pneumoniae."
    Heilbronn J., Wilson J., Berger B.J.
    J. Bacteriol. 181:1739-1747(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-22, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBUNIT.
    Strain: ATCC 13883 / DSM 30104 / JCM 1662 / NBRC 14940 / NCIMB 13281 / NCTC 9633.

Entry informationi

Entry nameiTYRB_KLEPN
AccessioniPrimary (citable) accession number: O85746
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: November 1, 1998
Last modified: March 16, 2016
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.