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Entry version 40 (25 May 2022)
Sequence version 1 (16 Apr 2014)
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Protein

Salicylate synthase

Gene

mbtI

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
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

Involved in the incorporation of salicylate into the virulence-conferring salicylate-based siderophore mycobactin. Catalyzes the initial conversion of chorismate to yield the intermediate isochorismate (isochorismate synthase activity), and the subsequent elimination of the enolpyruvyl side chain to give salicylate (isochorismate pyruvate-lyase activity). In the absence of magnesium, MbtI displays a chorismate mutase activity and converts chorismate to prephenate.

5 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

Mg2+3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 (E)-3-(1-carboxyprop-1-enyloxy)-2-hydroxybenzoic acid (AMT), 3-(1-carboxy-2-phenylvinyloxy)-2-hydroxybenzoic acid (phenyl-AMT), 3-(1-carboxy-3-methylbut-1-enyloxy)-2-hydroxybenzoic acid, 3-(1-carboxybut-1-enyloxy)-2-hydroxybenzoic acid (ethyl-AMT), 3-(1-carboxyprop-1-enyloxy)-2-hydroxybenzoic acid (methyl-AMT), 3-(1-carboxy-2-cyclopropylethenyloxy)-2-hydroxybenzoic acid (cyclopropyl-AMT) and 3-(1-carboxy-3-methylbut-1-enyloxy)-2-hydroxybenzoic acid (isopropyl-AMT).2 Publications

<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

kcat is 2.6 min(-1) for isochorismate pyruvate lyase activity (at pH 8 and 37 degrees Celsius). kcat is 2.8 min(-1) for salicylate synthase activity (at pH 8 and 37 degrees Celsius). kcat is 3.1 min(-1) for isochorismate synthase activity (at pH 7 and 37 degrees Celsius). kcat is 4.5 min(-1) for chorismate mutase activity (without magnesium at pH 7.5 and 37 degrees Celsius).1 Publication
  1. KM=2.6 µM for isochorismate (for isochorismate pyruvate lyase activity at pH 8 and 37 degrees Celsius)1 Publication
  2. KM=6 µM for isochorismate (for salicylate synthase activity at pH 8 and 37 degrees Celsius)1 Publication
  3. KM=21 µM for isochorismate (for salicylate synthase activity at pH 8 and 25 degrees Celsius)1 Publication
  4. KM=26 µM for chorismate (for chorismate mutase activity without magnesium at pH 7.5 and 37 degrees Celsius)1 Publication
  5. KM=34 µM for chorismate (for isochorismate synthase activity at pH 7 and 37 degrees Celsius)1 Publication

pH dependencei

At pH below 7.5, MtbI produces isochorismate and at pH 8 it produces salicylate.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: mycobactin biosynthesis

This protein is involved in the pathway mycobactin biosynthesis, which is part of Siderophore biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway mycobactin biosynthesis and in Siderophore biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei252Proton donorBy similarity1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei268Could activate a water molecule for attack at the C2 of chorismate and involved in recognition/elimination of the C4 hydroxyl1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi297Magnesium1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei385Substrate3 Publications1
Binding sitei405Substrate3 Publications1
Metal bindingi431Magnesium1 Publication1
Metal bindingi434Magnesium1 Publication1
Binding sitei438Substrate3 Publications1

<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

<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 functionIsomerase, Lyase
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
4.2.99.21, 3445
5.4.4.2, 3445

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

More...
UniPathwayi
UPA00011

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000001285

<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%5Fand%5Ftaxonomy%5Fsection">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:
Salicylate synthase1 Publication
Alternative name(s):
Chorismate mutase1 Publication (EC:5.4.99.51 Publication)
Short name:
CM1 Publication
Isochorismate synthase/isochorismate lyase1 Publication (EC:4.2.99.213 Publications, EC:5.4.4.23 Publications)
Mycobactin synthase protein1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:mbtI1 Publication
Synonyms:trpE21 Publication
Ordered Locus Names:Rv2386c
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri83332 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000001584 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

Organism-specific databases

Mycobacterium tuberculosis strain H37Rv genome database

More...
TubercuListi
Rv2386c

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Cells lacking this gene display a reduction in salicylic acid biosynthesis and a drastic decrease in production of mycobactin compared with the wild-type strain.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi205K → A: Only the chorismate mutase activity is observed. 1 Publication1
Mutagenesisi252E → Q: No activity is observed. 1 Publication1
Mutagenesisi268L → A: Only the chorismate mutase activity is observed. 1 Publication1
Mutagenesisi271T → A: Only the chorismate mutase activity is observed. 1 Publication1
Mutagenesisi334H → M: Only the chorismate mutase activity is observed. 1 Publication1
Mutagenesisi405R → A: Only the chorismate mutase activity is observed. 1 Publication1

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002620861 – 450Salicylate synthaseAdd BLAST450

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P9WFX1

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Induced by iron starvation conditions and during infection of human THP-1 macrophages. Transcriptionally repressed by IdeR and iron.1 Publication

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.

5 Publications

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
83332.Rv2386c

<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

Secondary structure

1450
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

AlphaFold Protein Structure Database

More...
AlphaFoldDBi
P9WFX1

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

More...
SMRi
P9WFX1

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni270 – 271Substrate binding2 Publications2
Regioni419 – 421Substrate binding3 Publications3

<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
COG1169, Bacteria

Identification of Orthologs from Complete Genome Data

More...
OMAi
VTDFMTV

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P9WFX1

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.60.120.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR005801, ADC_synthase
IPR019999, Anth_synth_I-like
IPR015890, Chorismate_C
IPR019996, Salicylate_synthase

The PANTHER Classification System

More...
PANTHERi
PTHR11236, PTHR11236, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00425, Chorismate_bind, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00095, ANTSNTHASEI

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF56322, SSF56322, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR03494, salicyl_syn, 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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

P9WFX1-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSELSVATGA VSTASSSIPM PAGVNPADLA AELAAVVTES VDEDYLLYEC
60 70 80 90 100
DGQWVLAAGV QAMVELDSDE LRVIRDGVTR RQQWSGRPGA ALGEAVDRLL
110 120 130 140 150
LETDQAFGWV AFEFGVHRYG LQQRLAPHTP LARVFSPRTR IMVSEKEIRL
160 170 180 190 200
FDAGIRHREA IDRLLATGVR EVPQSRSVDV SDDPSGFRRR VAVAVDEIAA
210 220 230 240 250
GRYHKVILSR CVEVPFAIDF PLTYRLGRRH NTPVRSFLLQ LGGIRALGYS
260 270 280 290 300
PELVTAVRAD GVVITEPLAG TRALGRGPAI DRLARDDLES NSKEIVEHAI
310 320 330 340 350
SVRSSLEEIT DIAEPGSAAV IDFMTVRERG SVQHLGSTIR ARLDPSSDRM
360 370 380 390 400
AALEALFPAV TASGIPKAAG VEAIFRLDEC PRGLYSGAVV MLSADGGLDA
410 420 430 440 450
ALTLRAAYQV GGRTWLRAGA GIIEESEPER EFEETCEKLS TLTPYLVARQ
Length:450
Mass (Da):48,754
Last modified:April 16, 2014 - 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:i79D95307E025D28A
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
AL123456 Genomic DNA Translation: CCP45174.1

NCBI Reference Sequences

More...
RefSeqi
WP_003412287.1, NZ_NVQJ01000029.1
YP_177877.1, NC_000962.3

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
885823

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mtu:Rv2386c

<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
AL123456 Genomic DNA Translation: CCP45174.1
RefSeqiWP_003412287.1, NZ_NVQJ01000029.1
YP_177877.1, NC_000962.3

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2G5FX-ray1.80A/B/C/D2-450[»]
2I6YX-ray2.50A2-450[»]
3LOGX-ray1.73A/B/C/D1-449[»]
3RV6X-ray2.04A/B2-450[»]
3RV7X-ray2.50A/B/C/D2-450[»]
3RV8X-ray2.29A/B/C/D1-450[»]
3RV9X-ray2.14A/B/C/D2-450[»]
3ST6X-ray1.75A/B/C/D1-450[»]
3VEHX-ray2.00A/B/C/D1-449[»]
6ZA4X-ray2.09A/B/C/D1-450[»]
6ZA5X-ray2.11A/B/C/D1-450[»]
6ZA6X-ray1.80A/B/C/D1-450[»]
AlphaFoldDBiP9WFX1
SMRiP9WFX1
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv2386c

Chemistry databases

SwissLipidsiSLP:000001285

Proteomic databases

PaxDbiP9WFX1

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
885823

Genome annotation databases

GeneIDi885823
KEGGimtu:Rv2386c

Organism-specific databases

TubercuListiRv2386c

Phylogenomic databases

eggNOGiCOG1169, Bacteria
OMAiVTDFMTV
PhylomeDBiP9WFX1

Enzyme and pathway databases

UniPathwayiUPA00011
BRENDAi4.2.99.21, 3445
5.4.4.2, 3445

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P9WFX1

Family and domain databases

Gene3Di3.60.120.10, 1 hit
InterProiView protein in InterPro
IPR005801, ADC_synthase
IPR019999, Anth_synth_I-like
IPR015890, Chorismate_C
IPR019996, Salicylate_synthase
PANTHERiPTHR11236, PTHR11236, 1 hit
PfamiView protein in Pfam
PF00425, Chorismate_bind, 1 hit
PRINTSiPR00095, ANTSNTHASEI
SUPFAMiSSF56322, SSF56322, 1 hit
TIGRFAMsiTIGR03494, salicyl_syn, 1 hit

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 nameiMBTI_MYCTU
<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: P9WFX1
Secondary accession number(s): L0T9G8, Q79FE7, Q7D785
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: May 25, 2022
This is version 40 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

3D-structure, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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