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Entry version 175 (13 Feb 2019)
Sequence version 2 (01 Oct 1993)
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Protein

Catalase-peroxidase

Gene

katG

Organism
Escherichia coli (strain K12)
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. Displays also NADH oxidase, INH lyase and isonicotinoyl-NAD synthase activity.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 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 b1 PublicationNote: Binds 2 heme B (iron-protoporphyrin IX) groups per tetramer.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=35 mM for H2O2 for the catalase reaction (at pH 5.5-6.0)2 Publications
  2. KM=4.2 mM for H2O2 for the catalase reaction (at pH 7.0)2 Publications
  3. KM=3.9 mM for H2O2 for the catalase reaction (at pH 7.5)2 Publications
  4. KM=60 µM for H2O2 for the peroxidase reaction2 Publications
  5. KM=24 µM for ABTS for the peroxidase reaction2 Publications
  1. Vmax=3730 µmol/min/mg enzyme for H2O2 for the catalase reaction (at pH 5.5-6.0)2 Publications
  2. Vmax=2220 µmol/min/mg enzyme for H2O2 for the catalase reaction (at pH 7.0)2 Publications
  3. Vmax=18 µmol/min/mg enzyme for ABTS for the peroxidase reaction2 Publications

pH dependencei

Optimum pH is 4.25 for the peroxidase reaction and 7.5 for the catalase reaction.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>Sitei102Transition state stabilizerUniRule annotation1
<p>This subsection of the ‘Function’ 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 sitei106Proton acceptorUniRule annotation1
<p>This subsection of the ‘Function’ 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 bindingi267Iron (heme axial ligand)1

<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

  • cellular response to hydrogen peroxide Source: EcoCyc
  • hydrogen peroxide catabolic process Source: EcoCyc
  • response to oxidative stress Source: EcoCyc

<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 processHydrogen peroxide
LigandHeme, Iron, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:HYDROPEROXIDI-MONOMER
ECOL316407:JW3914-MONOMER
MetaCyc:HYDROPEROXIDI-MONOMER

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P13029

Protein family/group databases

PeroxiBase, a peroxidase database

More...
PeroxiBasei
2394 EcoCP01_K-12

<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-peroxidaseUniRule annotation (EC:1.11.1.21UniRule annotation)
Short name:
CPUniRule annotation
Alternative name(s):
Hydroperoxidase I1 Publication
Short name:
HPI1 Publication
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:katGUniRule annotation
Ordered Locus Names:b3942, JW3914
<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>OrganismiEscherichia coli (strain K12)
<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 identifieri83333 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<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
  • UP000000318 <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
  • UP000000625 Componenti: Chromosome

Organism-specific databases

Escherichia coli strain K12 genome database

More...
EcoGenei
EG10511 katG

<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

  • cytosol Source: EcoCyc
  • extracellular region Source: GO_Central

<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 are more sensitive to killing by nalidixic acid, the effect is mitigated by pretreatment with 2,2'-bipyridyl and thiourea, both of which inhibit hydroxyl radical accumulation.1 Publication

<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_00000555641 – 726Catalase-peroxidaseAdd BLAST726

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-linki105 ↔ 226Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-252)1 Publication
Cross-linki226 ↔ 252Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-105)1 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

The N-terminus is blocked.
Formation of the three residue Trp-Tyr-Met cross-link is important for the catalase, but not the peroxidase activity of the enzyme.UniRule annotation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P13029

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P13029

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

More...
PaxDbi
P13029

PRoteomics IDEntifications database

More...
PRIDEi
P13029

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...
SWISS-2DPAGEi
P13029

<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 hydrogen peroxide.

<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

Homotetramer.1 Publication

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4263062, 16 interactors

Database of interacting proteins

More...
DIPi
DIP-10053N

Protein interaction database and analysis system

More...
IntActi
P13029, 12 interactors

Molecular INTeraction database

More...
MINTi
P13029

STRING: functional protein association networks

More...
STRINGi
316385.ECDH10B_4131

<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

1726
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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
1U2JX-ray2.30A/B/C/D/E/F/G/H422-726[»]
1U2KX-ray2.00A422-726[»]
1U2LX-ray2.30A/B422-726[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P13029

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

More...
SMRi
P13029

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P13029

<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

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

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000218110

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P13029

KEGG Orthology (KO)

More...
KOi
K03782

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P13029

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>.<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.

P13029-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSTSDDIHNT TATGKCPFHQ GGHDQSAGAG TTTRDWWPNQ LRVDLLNQHS
60 70 80 90 100
NRSNPLGEDF DYRKEFSKLD YYGLKKDLKA LLTESQPWWP ADWGSYAGLF
110 120 130 140 150
IRMAWHGAGT YRSIDGRGGA GRGQQRFAPL NSWPDNVSLD KARRLLWPIK
160 170 180 190 200
QKYGQKISWA DLFILAGNVA LENSGFRTFG FGAGREDVWE PDLDVNWGDE
210 220 230 240 250
KAWLTHRHPE ALAKAPLGAT EMGLIYVNPE GPDHSGEPLS AAAAIRATFG
260 270 280 290 300
NMGMNDEETV ALIAGGHTLG KTHGAGPTSN VGPDPEAAPI EEQGLGWAST
310 320 330 340 350
YGSGVGADAI TSGLEVVWTQ TPTQWSNYFF ENLFKYEWVQ TRSPAGAIQF
360 370 380 390 400
EAVDAPEIIP DPFDPSKKRK PTMLVTDLTL RFDPEFEKIS RRFLNDPQAF
410 420 430 440 450
NEAFARAWFK LTHRDMGPKS RYIGPEVPKE DLIWQDPLPQ PIYNPTEQDI
460 470 480 490 500
IDLKFAIADS GLSVSELVSV AWASASTFRG GDKRGGANGA RLALMPQRDW
510 520 530 540 550
DVNAAAVRAL PVLEKIQKES GKASLADIIV LAGVVGVEKA ASAAGLSIHV
560 570 580 590 600
PFAPGRVDAR QDQTDIEMFE LLEPIADGFR NYRARLDVST TESLLIDKAQ
610 620 630 640 650
QLTLTAPEMT ALVGGMRVLG ANFDGSKNGV FTDRVGVLSN DFFVNLLDMR
660 670 680 690 700
YEWKATDESK ELFEGRDRET GEVKFTASRA DLVFGSNSVL RAVAEVYASS
710 720
DAHEKFVKDF VAAWVKVMNL DRFDLL
Length:726
Mass (Da):80,024
Last modified:October 1, 1993 - v2
<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:i24D32EBED5DE9BD6
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 conflicti621A → G in AAA24040 (PubMed:3045098).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M21516 Genomic DNA Translation: AAA24040.1
U00096 Genomic DNA Translation: AAC76924.1
AP009048 Genomic DNA Translation: BAE77368.1
L19201 Genomic DNA Translation: AAB03074.1
U00006 Genomic DNA Translation: AAC43048.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A65201 CSECHP

NCBI Reference Sequences

More...
RefSeqi
NP_418377.1, NC_000913.3
WP_001295695.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC76924; AAC76924; b3942
BAE77368; BAE77368; BAE77368

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
948431

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW3914
eco:b3942

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|511145.12.peg.4063

<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
M21516 Genomic DNA Translation: AAA24040.1
U00096 Genomic DNA Translation: AAC76924.1
AP009048 Genomic DNA Translation: BAE77368.1
L19201 Genomic DNA Translation: AAB03074.1
U00006 Genomic DNA Translation: AAC43048.1
PIRiA65201 CSECHP
RefSeqiNP_418377.1, NC_000913.3
WP_001295695.1, NZ_LN832404.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1U2JX-ray2.30A/B/C/D/E/F/G/H422-726[»]
1U2KX-ray2.00A422-726[»]
1U2LX-ray2.30A/B422-726[»]
ProteinModelPortaliP13029
SMRiP13029
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263062, 16 interactors
DIPiDIP-10053N
IntActiP13029, 12 interactors
MINTiP13029
STRINGi316385.ECDH10B_4131

Protein family/group databases

PeroxiBasei2394 EcoCP01_K-12

2D gel databases

SWISS-2DPAGEiP13029

Proteomic databases

EPDiP13029
jPOSTiP13029
PaxDbiP13029
PRIDEiP13029

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76924; AAC76924; b3942
BAE77368; BAE77368; BAE77368
GeneIDi948431
KEGGiecj:JW3914
eco:b3942
PATRICifig|511145.12.peg.4063

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...
EchoBASEi
EB0506
EcoGeneiEG10511 katG

Phylogenomic databases

eggNOGiENOG4105C1X Bacteria
COG0376 LUCA
HOGENOMiHOG000218110
InParanoidiP13029
KOiK03782
PhylomeDBiP13029

Enzyme and pathway databases

BioCyciEcoCyc:HYDROPEROXIDI-MONOMER
ECOL316407:JW3914-MONOMER
MetaCyc:HYDROPEROXIDI-MONOMER
SABIO-RKiP13029

Miscellaneous databases

EvolutionaryTraceiP13029

Protein Ontology

More...
PROi
PR:P13029

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

More...
ProtoNeti
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 nameiKATG_ECOLI
<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: P13029
Secondary accession number(s): Q2M8N8
<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: January 1, 1990
Last sequence update: October 1, 1993
Last modified: February 13, 2019
This is version 175 of the entry and version 2 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, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
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