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Entry version 46 (16 Oct 2019)
Sequence version 1 (16 Apr 2014)
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Protein

Catalase-peroxidase

Gene

katG

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

Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity, oxidizing various electron donors including NADP(H) (PubMed:9006925, PubMed:18178143). Protects M.tuberculosis against toxic reactive oxygen species (ROS) including hydrogen peroxide as well as organic peroxides and thus contributes to its survival within host macrophages by countering the phagocyte oxidative burst (PubMed:8658136, PubMed:15165233). Also displays efficient peroxynitritase activity, which may help the bacterium to persist in macrophages (PubMed:10080924).UniRule annotation5 Publications
Might be involved in DNA repair. Partly complements recA-deficient E.coli cells exposed to UV radiation, mitomycin C or hydrogen peroxide. Increases resistance to mitomycin C in E.coli cells deficient for either uvrA, uvrB or uvrC.1 Publication
Catalyzes the oxidative activation of the antitubercular pro-drug isoniazid (INH) to generate an isonicotinoyl radical that then reacts nonenzymatically with NAD to form an isonicotinoyl-NAD adduct which inhibits InhA.5 Publications

Miscellaneous

In contrast to the Synechocystis sp. enzyme, no Trp radical is formed on the distal Trp residue (Trp-91).1 Publication
Was identified as a high-confidence drug target.1 Publication
Many isoniazid-resistant clinical isolates contain mutations in katG, leading to abolition or reduction of catalase/peroxidase activity which results in lack of INH activation, or to a reduced affinity for INH. Other mechanisms of INH resistance include deletion of the katG gene, and down-regulation of katG expression due to mutations in the furA-katG intergenic region.Curated

<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

heme b2 PublicationsNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.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 10100 sec(-1) for the catalase reaction (at pH 7.0 and 25 degrees Celsius).1 Publication
  1. KM=2.4 mM for H2O2 in the catalase reaction (at pH 7.0)1 Publication
  2. KM=225 mM for H2O2 in the catalase reaction (at pH 5.5-6.0)1 Publication
  3. KM=5.18 mM for H2O2 in the catalase reaction (at pH 7.0 and 25 degrees Celsius)1 Publication
  4. KM=360 µM for H2O2 in the peroxidase reaction1 Publication
  5. KM=67 µM for ABTS1 Publication
  6. KM=192 µM for isoniazid (at pH 7.2)1 Publication
  1. Vmax=7620 µmol/min/mg enzyme for the catalase reaction (at pH 5.5-6.0)1 Publication
  2. Vmax=5700 µmol/min/mg enzyme for the catalase reaction (at pH 7.0)1 Publication
  3. Vmax=14 µmol/min/mg enzyme for the peroxidase reaction with ABTS as substrate1 Publication

pH dependencei

Optimum pH is 7.0 for the catalase activity and 4.5-5.5 for the peroxidase activity (PubMed:9006925). Optimum pH is 4.75 for the peroxidase activity (PubMed:18178143).2 Publications

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>Sitei104Transition state stabilizerUniRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei108Proton acceptorUniRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi270Iron (heme axial ligand); via tele nitrogenCombined sources3 Publications1
Active sitei321Tryptophan radical intermediate1 Publication1

<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 functionOxidoreductase, Peroxidase
Biological processAntibiotic resistance, Hydrogen peroxide, Virulence
LigandHeme, Iron, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:G185E-6105-MONOMER
MTBH37RV:G185E-6105-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-1222387 Tolerance of reactive oxygen produced by macrophages

<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:
Catalase-peroxidase2 PublicationsUniRule annotation (EC:1.11.1.21UniRule annotation2 Publications)
Short name:
CP1 PublicationUniRule annotation
Alternative name(s):
Peroxidase/catalaseUniRule annotation
<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:katG1 Publication
Ordered Locus Names:Rv1908c
ORF Names:MTCY180.10
<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
Rv1908c

<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

<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 are devoid of catalase activity, supersensitive to H2O2 exposure and highly resistant to the antitubercular drug isoniazid (INH) in vitro. This mutant strain is markedly attenuated for virulence in mice and displays impaired growth in infected macrophages, but its growth and survival is indistinguishable from wild-type in macrophages lacking the ROS-generating NADPH oxidase (Phox).1 Publication

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>Mutagenesisi137D → S: Exhibits 8-fold increased catalytic efficiency for the activation of INH (INH-NAD formation). Possesses an enlarged substrate access channel. 1 Publication1
Mutagenesisi229Y → F: Exhibits 2-fold increased affinity for INH. 1 Publication1
Mutagenesisi315S → T: 20-fold decrease in the rate of INH-NAD adduct formation. Exhibits significantly reduced affinity for INH (KM is increased by 43-fold). 2 Publications1
Mutagenesisi321W → F: Nearly no effect on the kinetic parameters for the activation of INH. 1 Publication1
Mutagenesisi418R → L: Exhibits 1.7-fold decreased catalytic efficiency for the activation of INH. 1 Publication1
Mutagenesisi463R → L: Nearly no effect on the kinetic parameters for the catalase and peroxidase activity. Activates INH and mediates InhA inactivation as efficiently as wild-type. 1 Publication1

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB00609 Ethionamide
DB00951 Isoniazid

<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_00000555741 – 740Catalase-peroxidaseAdd BLAST740

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki107 ↔ 229Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-255); alternateUniRule annotation1 Publication
Cross-linki229 ↔ 255Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-107); alternateUniRule annotation1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Formation of the three residue Trp-Tyr-Met cross-link is important for the catalase, but not the peroxidase activity of the enzyme (By similarity). The formation of the Trp-Tyr-Met cross-link is autocatalytic (PubMed:15840564).UniRule annotation1 Publication

Keywords - PTMi

Organic radical

Proteomic databases

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

More...
PaxDbi
P9WIE5

<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

By treatment with H2O2 (PubMed:8658136). Repressed by FurA (PubMed:11401695).2 Publications

<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.

3 Publications

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
83332.Rv1908c

<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

1740
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
P9WIE5

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 general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Consists of two related domains. The catalase-peroxidase activity is associated with the N-terminal domain but no definite function has been assigned to the C-terminal domain, although it may play a role in substrate binding.1 Publication

<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

Belongs to the peroxidase family. Peroxidase/catalase subfamily.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105C1X Bacteria
COG0376 LUCA

KEGG Orthology (KO)

More...
KOi
K03782

Identification of Orthologs from Complete Genome Data

More...
OMAi
GPETTWL

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P9WIE5

Family and domain databases

HAMAP database of protein families

More...
HAMAPi
MF_01961 Catal_peroxid, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000763 Catalase_peroxidase
IPR002016 Haem_peroxidase
IPR010255 Haem_peroxidase_sf
IPR019794 Peroxidases_AS
IPR019793 Peroxidases_heam-ligand_BS

The PANTHER Classification System

More...
PANTHERi
PTHR30555 PTHR30555, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00141 peroxidase, 2 hits

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00460 BPEROXIDASE
PR00458 PEROXIDASE

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48113 SSF48113, 2 hits

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00198 cat_per_HPI, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00435 PEROXIDASE_1, 1 hit
PS00436 PEROXIDASE_2, 1 hit
PS50873 PEROXIDASE_4, 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.

P9WIE5-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPEQHPPITE TTTGAASNGC PVVGHMKYPV EGGGNQDWWP NRLNLKVLHQ
60 70 80 90 100
NPAVADPMGA AFDYAAEVAT IDVDALTRDI EEVMTTSQPW WPADYGHYGP
110 120 130 140 150
LFIRMAWHAA GTYRIHDGRG GAGGGMQRFA PLNSWPDNAS LDKARRLLWP
160 170 180 190 200
VKKKYGKKLS WADLIVFAGN CALESMGFKT FGFGFGRVDQ WEPDEVYWGK
210 220 230 240 250
EATWLGDERY SGKRDLENPL AAVQMGLIYV NPEGPNGNPD PMAAAVDIRE
260 270 280 290 300
TFRRMAMNDV ETAALIVGGH TFGKTHGAGP ADLVGPEPEA APLEQMGLGW
310 320 330 340 350
KSSYGTGTGK DAITSGIEVV WTNTPTKWDN SFLEILYGYE WELTKSPAGA
360 370 380 390 400
WQYTAKDGAG AGTIPDPFGG PGRSPTMLAT DLSLRVDPIY ERITRRWLEH
410 420 430 440 450
PEELADEFAK AWYKLIHRDM GPVARYLGPL VPKQTLLWQD PVPAVSHDLV
460 470 480 490 500
GEAEIASLKS QIRASGLTVS QLVSTAWAAA SSFRGSDKRG GANGGRIRLQ
510 520 530 540 550
PQVGWEVNDP DGDLRKVIRT LEEIQESFNS AAPGNIKVSF ADLVVLGGCA
560 570 580 590 600
AIEKAAKAAG HNITVPFTPG RTDASQEQTD VESFAVLEPK ADGFRNYLGK
610 620 630 640 650
GNPLPAEYML LDKANLLTLS APEMTVLVGG LRVLGANYKR LPLGVFTEAS
660 670 680 690 700
ESLTNDFFVN LLDMGITWEP SPADDGTYQG KDGSGKVKWT GSRVDLVFGS
710 720 730 740
NSELRALVEV YGADDAQPKF VQDFVAAWDK VMNLDRFDVR
Length:740
Mass (Da):80,605
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:iB43C033B533CDD89
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti234G → A in CAA48213 (PubMed:8320241).Curated1
Sequence conflicti500 – 512QPQVG…NDPDG → CSHKSGGRSTTRR in AAA72374 (PubMed:10463167).CuratedAdd BLAST13

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti300W → G in strain: H0892/92; INH-resistant. 1
Natural varianti315S → T in strain: H0181/94, H0452/92, H0948/92 and H0169/93; INH-resistant. 1
Natural varianti463R → L in strain: H0169/93; INH-resistant. 1
Natural varianti501P → A in strain: H0948/92; INH-resistant. 1
Natural varianti525Q → P in strain: H0251/90; INH-resistant. 1
Natural varianti587L → P in strain: 15726/89; INH-resistant. 1
Natural varianti700S → P in strain: H0004/93; INH-resistant. 1

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
X68081 Genomic DNA Translation: CAA48213.1
U06258 Unassigned DNA Translation: AAB04159.1
U40593 Genomic DNA Translation: AAA85167.1
U40595 Genomic DNA Translation: AAA85169.1
U41305 Genomic DNA Translation: AAA85171.1
U41306 Genomic DNA Translation: AAA85172.1
U41307 Genomic DNA Translation: AAA85173.1
U41308 Genomic DNA Translation: AAA85174.1
U41309 Genomic DNA Translation: AAA85175.1
U41310 Genomic DNA Translation: AAA85176.1
U41311 Genomic DNA Translation: AAA85177.1
U41312 Genomic DNA Translation: AAA85178.1
U41313 Genomic DNA Translation: AAA85179.1
U41314 Genomic DNA Translation: AAA85180.1
JX303265 Genomic DNA Translation: AFR90354.1
JX303270 Genomic DNA Translation: AFR90359.1
JX303273 Genomic DNA Translation: AFR90362.1
JX303276 Genomic DNA Translation: AFR90365.1
JX303277 Genomic DNA Translation: AFR90366.1
JX303278 Genomic DNA Translation: AFR90367.1
JX303280 Genomic DNA Translation: AFR90369.1
AL123456 Genomic DNA Translation: CCP44675.1
AF002194 Genomic DNA Translation: AAB63371.1
L14268 Genomic DNA Translation: AAA72374.1

Protein sequence database of the Protein Information Resource

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PIRi
A70519 A40662

NCBI Reference Sequences

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RefSeqi
NP_216424.1, NC_000962.3
WP_003899075.1, NZ_NVQJ01000034.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
CCP44675; CCP44675; Rv1908c

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
885638

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mtu:Rv1908c

<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
X68081 Genomic DNA Translation: CAA48213.1
U06258 Unassigned DNA Translation: AAB04159.1
U40593 Genomic DNA Translation: AAA85167.1
U40595 Genomic DNA Translation: AAA85169.1
U41305 Genomic DNA Translation: AAA85171.1
U41306 Genomic DNA Translation: AAA85172.1
U41307 Genomic DNA Translation: AAA85173.1
U41308 Genomic DNA Translation: AAA85174.1
U41309 Genomic DNA Translation: AAA85175.1
U41310 Genomic DNA Translation: AAA85176.1
U41311 Genomic DNA Translation: AAA85177.1
U41312 Genomic DNA Translation: AAA85178.1
U41313 Genomic DNA Translation: AAA85179.1
U41314 Genomic DNA Translation: AAA85180.1
JX303265 Genomic DNA Translation: AFR90354.1
JX303270 Genomic DNA Translation: AFR90359.1
JX303273 Genomic DNA Translation: AFR90362.1
JX303276 Genomic DNA Translation: AFR90365.1
JX303277 Genomic DNA Translation: AFR90366.1
JX303278 Genomic DNA Translation: AFR90367.1
JX303280 Genomic DNA Translation: AFR90369.1
AL123456 Genomic DNA Translation: CCP44675.1
AF002194 Genomic DNA Translation: AAB63371.1
L14268 Genomic DNA Translation: AAA72374.1
PIRiA70519 A40662
RefSeqiNP_216424.1, NC_000962.3
WP_003899075.1, NZ_NVQJ01000034.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SFZmodel-A1-740[»]
1SJ2X-ray2.41A/B2-740[»]
2CCAX-ray2.00A/B1-740[»]
2CCDX-ray2.10A/B1-740[»]
4C50X-ray2.50A/B1-740[»]
4C51X-ray3.10A/B1-740[»]
SMRiP9WIE5
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv1908c

Chemistry databases

DrugBankiDB00609 Ethionamide
DB00951 Isoniazid

Proteomic databases

PaxDbiP9WIE5

Genome annotation databases

EnsemblBacteriaiCCP44675; CCP44675; Rv1908c
GeneIDi885638
KEGGimtu:Rv1908c

Organism-specific databases

TubercuListiRv1908c

Phylogenomic databases

eggNOGiENOG4105C1X Bacteria
COG0376 LUCA
KOiK03782
OMAiGPETTWL
PhylomeDBiP9WIE5

Enzyme and pathway databases

BioCyciMetaCyc:G185E-6105-MONOMER
MTBH37RV:G185E-6105-MONOMER
ReactomeiR-HSA-1222387 Tolerance of reactive oxygen produced by macrophages

Family and domain databases

HAMAPiMF_01961 Catal_peroxid, 1 hit
InterProiView protein in InterPro
IPR000763 Catalase_peroxidase
IPR002016 Haem_peroxidase
IPR010255 Haem_peroxidase_sf
IPR019794 Peroxidases_AS
IPR019793 Peroxidases_heam-ligand_BS
PANTHERiPTHR30555 PTHR30555, 1 hit
PfamiView protein in Pfam
PF00141 peroxidase, 2 hits
PRINTSiPR00460 BPEROXIDASE
PR00458 PEROXIDASE
SUPFAMiSSF48113 SSF48113, 2 hits
TIGRFAMsiTIGR00198 cat_per_HPI, 1 hit
PROSITEiView protein in PROSITE
PS00435 PEROXIDASE_1, 1 hit
PS00436 PEROXIDASE_2, 1 hit
PS50873 PEROXIDASE_4, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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 nameiKATG_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: P9WIE5
Secondary accession number(s): J9VFD2
, O08221, Q08129, Q50544, Q50546, Q50551, Q50552, Q50553, Q50554, Q50555, Q50762, Q57215, Q57274
<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 46 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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