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Entry version 37 (16 Oct 2019)
Sequence version 1 (16 Apr 2014)
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Protein

Long-chain-fatty-acid--CoA ligase FadD13

Gene

fadD13

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

Required for maintaining the appropriate mycolic acid composition and permeability of the envelope on its exposure to acidic pH. Catalyzes the activation of long-chain fatty acids as acyl-coenzyme A (acyl-CoA), which are then transferred to the multifunctional polyketide synthase (PKS) type III for further chain extension. It has preference for the fatty acid with long chain length in the following order: hexacosanoic acid (C26), tetracosanoic acid (C24) and palmitic acid (C16).3 Publications

<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 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 0.03 sec(-1) for palmitic acid (at pH 8 and at 37 degrees Celsius).
  1. KM=0.13 mM for CoA (at pH 8 and at 37 degrees Celsius)2 Publications
  2. KM=0.11 mM for CoASH (at pH 8 and at 30 degrees Celsius)2 Publications
  3. KM=19.79 µM for palmitic acid (at pH 8 and at 37 degrees Celsius)2 Publications
  4. KM=0.23 mM for ATP (at pH 8 and at 37 degrees Celsius)2 Publications
  5. KM=0.25 mM for ATP (at pH 8 and at 30 degrees Celsius)2 Publications
  1. Vmax=14.62 pmol/min/µg enzyme (at pH 8 and at 37 degrees Celsius)2 Publications

<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: fatty acid biosynthesis

This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway fatty acid biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Sitei9Membrane interaction1
Sitei17Membrane interaction1
Sitei195Membrane interaction1
Sitei197Membrane interaction1
Sitei214Important for substrate selectivity1
Sitei244Membrane interaction1
Sitei302Important for substrate selectivity1

<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

  • fatty acid biosynthetic process Source: UniProtKB-UniPathway
  • growth of symbiont in host cell Source: MTBBASE
  • response to acidic pH Source: MTBBASE

<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 functionLigase
Biological processFatty acid metabolism, Lipid metabolism
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MTBH37RV:G185E-7351-MONOMER

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

More...
UniPathwayi
UPA00094

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000000980

<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:
Long-chain-fatty-acid--CoA ligase FadD13 (EC:6.2.1.3)
Alternative name(s):
Fatty acyl-CoA ligase
Short name:
FACL
Short name:
FACL13
Fatty acyl-CoA synthetase
Short name:
ACS
Short name:
FACS
Very-long-chain fatty-acyl-CoA synthetase
Short name:
ACSVL
<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:fadD13
Ordered Locus Names:Rv3089
<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>OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
<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 identifieri83332 [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 lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_manual">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
Rv3089

<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

GO - Cellular componenti

Keywords - Cellular componenti

Cell membrane, Membrane

<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

Inactivation of the mymA operon causes altered cell wall structure, reduced contents and altered composition of mycolic acids along with the accumulation of saturated C24 and C26 fatty acids, and enhanced susceptibility to antibiotics, detergents and acidic pH. Also impairs ability to survive in macrophages.2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi9R → A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244. 1 Publication1
Mutagenesisi17R → A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244. 1 Publication1
Mutagenesisi172K → A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis. 1 Publication1
Mutagenesisi195R → A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244. 1 Publication1
Mutagenesisi197R → A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244. 1 Publication1
Mutagenesisi209V → D: Strong reduction of the fatty acyl-CoA ligase activity. No significant change in the total expression level, however the cytoplasmic expression is reduced. Slight increase of susceptibility to proteolysis. 1 Publication1
Mutagenesisi211A → G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation. 1 Publication1
Mutagenesisi214T → W: Shows a marked decrease in the activity with lauric and palmitic acid (C12 and C16 fatty acid) with a simultaneous increase in the activity with caprylic acid (C8 fatty acid). 1 Publication1
Mutagenesisi244R → A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197. 1 Publication1
Mutagenesisi302A → G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation. 2 Publications1
Mutagenesisi302A → W: Does not show activity with small, medium or long acyl chains. 2 Publications1
Mutagenesisi377W → A: Strong reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding. No significant change in the total expression level, however the cytoplasmic expression is low. Slight increase of susceptibility to proteolysis. 1 Publication1
Mutagenesisi382D → A: Strong reduction of the fatty acyl-CoA ligase activity. No significant change in the total expression level, however the cytoplasmic expression is reduced. 1 Publication1
Mutagenesisi397R → A: Reduction of binding affinity for fatty acids. 1 Publication1
Mutagenesisi404S → A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding. 1 Publication1
Mutagenesisi406G → L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA. 1 Publication1
Mutagenesisi487K → A: Strong reduction of the fatty acyl-CoA ligase activity. Reduction of binding affinity for ATP. 3 Publications1

<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_00004209601 – 503Long-chain-fatty-acid--CoA ligase FadD13Add BLAST503

Proteomic databases

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

More...
PaxDbi
P9WQ37

PRoteomics IDEntifications database

More...
PRIDEi
P9WQ37

<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

Expression is controlled by VirS. Induced at acidic pH and in macrophages.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_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

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
83332.Rv3089

<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

1503
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
P9WQ37

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

<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
ENOG4105CEY Bacteria
COG0318 LUCA

Identification of Orthologs from Complete Genome Data

More...
OMAi
GAYLMTM

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P9WQ37

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.50.12780, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR025110 AMP-bd_C
IPR020845 AMP-binding_CS
IPR000873 AMP-dep_Synth/Lig
IPR042099 AMP-dep_Synthh-like_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00501 AMP-binding, 1 hit
PF13193 AMP-binding_C, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00455 AMP_BINDING, 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.

P9WQ37-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKNIGWMLRQ RATVSPRLQA YVEPSTDVRM TYAQMNALAN RCADVLTALG
60 70 80 90 100
IAKGDRVALL MPNSVEFCCL FYGAAKLGAV AVPINTRLAA PEVSFILSDS
110 120 130 140 150
GSKVVIYGAP SAPVIDAIRA QADPPGTVTD WIGADSLAER LRSAAADEPA
160 170 180 190 200
VECGGDDNLF IMYTSGTTGH PKGVVHTHES VHSAASSWAS TIDVRYRDRL
210 220 230 240 250
LLPLPMFHVA ALTTVIFSAM RGVTLISMPQ FDATKVWSLI VEERVCIGGA
260 270 280 290 300
VPAILNFMRQ VPEFAELDAP DFRYFITGGA PMPEALIKIY AAKNIEVVQG
310 320 330 340 350
YALTESCGGG TLLLSEDALR KAGSAGRATM FTDVAVRGDD GVIREHGEGE
360 370 380 390 400
VVIKSDILLK EYWNRPEATR DAFDNGWFRT GDIGEIDDEG YLYIKDRLKD
410 420 430 440 450
MIISGGENVY PAEIESVIIG VPGVSEVAVI GLPDEKWGEI AAAIVVADQN
460 470 480 490 500
EVSEQQIVEY CGTRLARYKL PKKVIFAEAI PRNPTGKILK TVLREQYSAT

VPK
Length:503
Mass (Da):54,459
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:iB4CF011549E7B620
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: CCP45898.1

Protein sequence database of the Protein Information Resource

More...
PIRi
E70853

NCBI Reference Sequences

More...
RefSeqi
NP_217605.1, NC_000962.3
WP_003416081.1, NZ_NVQJ01000011.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
CCP45898; CCP45898; Rv3089

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
888666

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mtu:Rv3089
mtv:RVBD_3089

<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: CCP45898.1
PIRiE70853
RefSeqiNP_217605.1, NC_000962.3
WP_003416081.1, NZ_NVQJ01000011.1

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
3R44X-ray1.80A1-503[»]
3T5BX-ray2.35A1-396[»]
3T5CX-ray2.09A/B1-396[»]
SMRiP9WQ37
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv3089

Chemistry databases

SwissLipidsiSLP:000000980

Proteomic databases

PaxDbiP9WQ37
PRIDEiP9WQ37

Genome annotation databases

EnsemblBacteriaiCCP45898; CCP45898; Rv3089
GeneIDi888666
KEGGimtu:Rv3089
mtv:RVBD_3089

Organism-specific databases

TubercuListiRv3089

Phylogenomic databases

eggNOGiENOG4105CEY Bacteria
COG0318 LUCA
OMAiGAYLMTM
PhylomeDBiP9WQ37

Enzyme and pathway databases

UniPathwayiUPA00094
BioCyciMTBH37RV:G185E-7351-MONOMER

Family and domain databases

Gene3Di3.40.50.12780, 1 hit
InterProiView protein in InterPro
IPR025110 AMP-bd_C
IPR020845 AMP-binding_CS
IPR000873 AMP-dep_Synth/Lig
IPR042099 AMP-dep_Synthh-like_sf
PfamiView protein in Pfam
PF00501 AMP-binding, 1 hit
PF13193 AMP-binding_C, 1 hit
PROSITEiView protein in PROSITE
PS00455 AMP_BINDING, 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 nameiFAC13_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: P9WQ37
Secondary accession number(s): F2GNX9
, L0TEI7, O53306, Q7D654
<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: April 16, 2014
Last sequence update: April 16, 2014
Last modified: October 16, 2019
This is version 37 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, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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