O85746 (TYRB_KLEPN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tyrosine aminotransferase
Short name=TyrAT
EC=2.6.1.5

Alternative name(s):
Aromatic-amino-acid transaminase
EC=2.6.1.57
Aspartate aminotransferase
EC=2.6.1.1

Gene names

Name:

tyrB

Organism

Klebsiella pneumoniae

Taxonomic identifier

573 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Klebsiella

Protein attributes

Sequence length	397 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 activity	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.
Cofactor	Pyridoxal phosphate Potential.
Enzyme regulation	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. Ref.1
Pathway	Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 6/6.
Subunit structure	Homodimer. Ref.1
Sequence similarities	Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.
Biophysicochemical properties	Kinetic parameters: KM=1.42 mM for tryptophan (at pH 7.4 and 10 mM KMTB) Ref.1 KM=2.01 mM for tyrosine (at pH 7.4 and 10 mM KMTB) KM=2.01 mM for phenylalanine (at pH 7.4 and 10 mM KMTB) KM=2.46 mM for KMTB (at pH 7.4 and 5 mM tyrosine) KM=3.00 mM for alpha-ketoglutarate (at pH 7.4 and 5 mM tyrosine) KM=6.00 mM for oxaloacetate (at pH 7.4 and 5 mM tyrosine) KM=11.93 mM for glutamate (at pH 7.4 and 10 mM KMTB) KM=20.13 mM for pyruvate (at pH 7.4 and 5 mM tyrosine) Vmax=0.09 µmol/min/mg enzyme with pyruvate and tyrosine as substrates(at pH 7.4) Vmax=1.80 µmol/min/mg enzyme with phenylalanine and KMTB as substrates (at pH 7.4) Vmax=2.63 µmol/min/mg enzyme with tryptophan and KMTB as substrates(at pH 7.4) Vmax=3.25 µmol/min/mg enzyme with tyrosine and KMTB as substrates(at pH 7.4) Vmax=3.29 µmol/min/mg enzyme with phenylalanine and tyrosine as substrates(at pH 7.4) Vmax=5.21 µmol/min/mg enzyme with alpha-ketoglutarate and tyrosine as substrates(at pH 7.4) Vmax=7.39 µmol/min/mg enzyme with oxaloacetate and tyrosine as substrates(at pH 7.4) Vmax=7.65 µmol/min/mg enzyme with glutamate and KMTB as substrates (at pH 7.4)

Ontologies

Keywords
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	biosynthetic process Inferred from electronic annotation. Source: InterPro cellular amino acid metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	L-aspartate:2-oxoglutarate aminotransferase activity Inferred from electronic annotation. Source: EC L-phenylalanine:2-oxoglutarate aminotransferase activity Inferred from electronic annotation. Source: EC L-tyrosine:2-oxoglutarate aminotransferase activity Inferred from electronic annotation. Source: EC aromatic-amino-acid:2-oxoglutarate aminotransferase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 397	397	Tyrosine aminotransferase		PRO_0000358872

Sequences

	Sequence		Length	Mass (Da)
	O85746 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 43079DDE86C104CE	FASTA	397	43,432
	10 20 30 40 50 60 MFQKVDAYAG DPILSLMERF KEDPRSDKVN LSIGLYYNDD GIIPQLQAVA EAEARLNAEP 70 80 90 100 110 120 HGASLYLPME GFSGYRQAIA PLLFGAEHTA LKQNRIASIQ TVGGSGALKV GADFLKRYFP 130 140 150 160 170 180 ESHVWVSDPT WENHIAIFEG AGFEVSTYPW FDKATNGVRF ENLLAMLQTL PARDIVLLHP 190 200 210 220 230 240 CCHNPTGADL TPAQWDRVVE VLKARQLIPF LDIAYQGFGG GLEEDAYAIR AIASAGMPML 250 260 270 280 290 300 VSNSFSKIFS LYGERVGGLS VVCEDSETAG RVLGQLKATV RRNYSSPPSF GAQVVATVLN 310 320 330 340 350 360 DAALKATWQA EVDAMRAHIL TMRQALVDAL QQVAPGSKVD YLLKQRGMFS YTGFSAAQVD 370 380 390 RLRDEFGVYL IASGRMRVAG LNSRNVQQVA KAFVAVM

References

[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: 10074065] [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.

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Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF074934 Genomic DNA. Translation: AAC26140.1.
3D structure databases
HSSP	HSSP built from PDB template 3TAT based on UniProtKB P04693.
ProteinModelPortal	O85746.
SMR	O85746. Positions 1-397.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-1302.
Family and domain databases
InterPro	IPR004839. Aminotransferase_I/II. IPR000796. Asp_trans. IPR004838. NHTrfase_class1_PyrdxlP-BS. IPR015424. PyrdxlP-dep_Trfase_major_dom. IPR015421. PyrdxlP-dep_Trfase_major_sub1. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
PANTHER	PTHR11879. Asp_trans. 1 hit.
Pfam	PF00155. Aminotran_1_2. 1 hit. [Graphical view]
PRINTS	PR00799. TRANSAMINASE.
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
PROSITE	PS00105. AA_TRANSFER_CLASS_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

TYRB_KLEPN

Accession

Primary (citable) accession number: O85746

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	November 1, 1998
Last modified:	November 16, 2011
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program