Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 83 (08 May 2019)
Sequence version 1 (01 Nov 1998)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Tyrosine aminotransferase

Gene

tyrB

Organism
Klebsiella pneumoniae
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

pyridoxal 5'-phosphateCurated

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity 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

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>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), 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), 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_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_2)
  2. Methylthioribulose-1-phosphate dehydratase (mtnB_2), Methylthioribulose-1-phosphate dehydratase (mtnB), Methylthioribulose-1-phosphate dehydratase (mtnB_1), Methylthioribulose-1-phosphate dehydratase (mtnB), Methylthioribulose-1-phosphate dehydratase (mtnB), Methylthioribulose-1-phosphate dehydratase (mtnB_3), Methylthioribulose-1-phosphate dehydratase (mtnB), Methylthioribulose-1-phosphate dehydratase (mtnB_1), Methylthioribulose-1-phosphate dehydratase (mtnB), Methylthioribulose-1-phosphate dehydratase (mtnB_2), Methylthioribulose-1-phosphate dehydratase (mtnB_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), 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), 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), 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), 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), 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), Acireductone dioxygenase (mtnD), Acireductone dioxygenase (mtnD), Acireductone dioxygenase (mtnD), Acireductone dioxygenase (mtnD), Acireductone dioxygenase (mtnD_1), Acireductone dioxygenase (mtnD), Acireductone dioxygenase (mtnD), Acireductone dioxygenase (mtnD), Acireductone dioxygenase (mtnD_2), Acireductone dioxygenase (mtnD), 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
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei34Substrate; via amide nitrogenBy similarity1
Binding sitei66SubstrateBy similarity1
Binding sitei131SubstrateBy similarity1
Binding sitei184SubstrateBy similarity1
Binding sitei375SubstrateBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

  • L-methionine salvage from methylthioadenosine Source: CACAO

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionAminotransferase, Transferase
LigandPyridoxal phosphate

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:MONOMER-1302

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00904;UER00879

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:tyrB
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiKlebsiella pneumoniae
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri573 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeKlebsiella

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00003588721 – 397Tyrosine aminotransferaseAdd BLAST397

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei247N6-(pyridoxal phosphate)lysineBy similarity1

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
O85746

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.

1 Publication

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
O85746

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105CGF Bacteria
COG1448 LUCA

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.640.10, 1 hit
3.90.1150.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View 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

The PANTHER Classification System

More...
PANTHERi
PTHR11879 PTHR11879, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00155 Aminotran_1_2, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00799 TRANSAMINASE

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53383 SSF53383, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00105 AA_TRANSFER_CLASS_1, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i43079DDE86C104CE
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AF074934 Genomic DNA Translation: AAC26140.1

Genome annotation databases

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ag:AAC26140

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

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

3D structure databases

SMRiO85746
ModBaseiSearch...

Proteomic databases

PRIDEiO85746

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
3.90.1150.10, 1 hit
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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiTYRB_KLEPN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: O85746
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: November 1, 1998
Last modified: May 8, 2019
This is version 83 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again