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Entry version 118 (08 May 2019)
Sequence version 3 (22 Jul 2008)
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Protein

Catalase-peroxidase

Gene

katG

Organism
Burkholderia pseudomallei (strain K96243)
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, isoniazid hydrazine lyase and isonicotinoyl-NAD synthase activity.UniRule annotation1 Publication

<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 bNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.

<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=56 mM for H2O2 for the catalase reaction (at pH 5.5-6.0)2 Publications
  2. KM=4.5 mM for H2O2 for the catalase reaction (at pH 7.0)2 Publications
  3. KM=700 µM for H2O2 for the peroxidase reaction2 Publications
  4. KM=300 µM for ABTS for the peroxidase reaction2 Publications
  5. KM=12.5 µM for NADH for the oxidase reaction2 Publications
  1. Vmax=11900 µmol/min/mg enzyme for H2O2 for the catalase reaction (at pH 5.5-6.0)2 Publications
  2. Vmax=4300 µmol/min/mg enzyme for H2O2 for the catalase reaction (at pH 7.0)2 Publications
  3. Vmax=6.0 µmol/min/mg enzyme for ABTS for the peroxidase reaction2 Publications

pH dependencei

Optimum pH is 4.5 for the peroxidase reaction, 6.0 for the catalase reaction, and 8.75 for the NADH oxidase 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>Sitei88Transition state stabilizer1
<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 sitei92Proton acceptor1
<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 bindingi259Iron (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

<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

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.11.1.21 1031

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
Q939D2

Protein family/group databases

PeroxiBase, a peroxidase database

More...
PeroxiBasei
2303 BpCP01_K96243

<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):
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:BPSL2865
<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>OrganismiBurkholderia pseudomallei (strain K96243)
<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 identifieri272560 [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 lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group
<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
  • UP000000605 <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 1

<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

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB08638 2-AMINO-3-(1-HYDROPEROXY-1H-INDOL-3-YL)PROPAN-1-OL

<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<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_00003450922 – 728Catalase-peroxidaseAdd BLAST727

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-linki91 ↔ 218Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-244)
Cross-linki218 ↔ 244Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-91)

<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.UniRule annotation

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q939D2

<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
272560.BPSL2865

<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

1728
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
5L02X-ray1.90A/B1-728[»]
5L05X-ray1.70A/B15-728[»]
5SW4X-ray1.90A/B15-728[»]
5SW5X-ray2.05A/B15-728[»]
5SW6X-ray1.90A/B15-728[»]
5SX0X-ray2.00A/B15-728[»]
5SX1X-ray1.80A/B1-728[»]
5SX2X-ray2.15A/B1-728[»]
5SX3X-ray2.00A/B1-728[»]
5SX6X-ray1.90A/B1-728[»]
5SX7X-ray1.95A/B1-728[»]
5SXQX-ray2.10A/B1-728[»]
5SXRX-ray1.69A/B1-728[»]
5SXSX-ray1.89A/B1-728[»]
5SXTX-ray1.90A/B1-728[»]
5SXWX-ray1.60A/B1-728[»]
5SXXX-ray1.70A/B1-728[»]
5SYHX-ray1.65A/B15-728[»]
5SYIX-ray1.70A/B15-728[»]
5SYKX-ray1.80A/B1-728[»]
5SYLX-ray1.95A/B1-728[»]
5SYVX-ray1.75A/B1-728[»]
5SYXX-ray1.77A/B1-728[»]
6CFQX-ray1.72A/B1-728[»]

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

More...
SMRi
Q939D2

Database of comparative protein structure models

More...
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
Q939D2

<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

KEGG Orthology (KO)

More...
KOi
K03782

Identification of Orthologs from Complete Genome Data

More...
OMAi
ADVWEPE

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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

Q939D2-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSNEAKCPFH QAAGNGTSNR DWWPNQLDLS ILHRHSSLSD PMGKDFNYAQ
60 70 80 90 100
AFEKLDLAAV KRDLHALMTT SQDWWPADFG HYGGLFIRMA WHSAGTYRTA
110 120 130 140 150
DGRGGAGEGQ QRFAPLNSWP DNANLDKARR LLWPIKQKYG RAISWADLLI
160 170 180 190 200
LTGNVALESM GFKTFGFAGG RADTWEPEDV YWGSEKIWLE LSGGPNSRYS
210 220 230 240 250
GDRQLENPLA AVQMGLIYVN PEGPDGNPDP VAAARDIRDT FARMAMNDEE
260 270 280 290 300
TVALIAGGHT FGKTHGAGPA SNVGAEPEAA GIEAQGLGWK SAYRTGKGAD
310 320 330 340 350
AITSGLEVTW TTTPTQWSHN FFENLFGYEW ELTKSPAGAH QWVAKGADAV
360 370 380 390 400
IPDAFDPSKK HRPTMLTTDL SLRFDPAYEK ISRRFHENPE QFADAFARAW
410 420 430 440 450
FKLTHRDMGP RARYLGPEVP AEVLLWQDPI PAVDHPLIDA ADAAELKAKV
460 470 480 490 500
LASGLTVSQL VSTAWAAAST FRGSDKRGGA NGARIRLAPQ KDWEANQPEQ
510 520 530 540 550
LAAVLETLEA IRTAFNGAQR GGKQVSLADL IVLAGCAGVE QAAKNAGHAV
560 570 580 590 600
TVPFAPGRAD ASQEQTDVES MAVLEPVADG FRNYLKGKYR VPAEVLLVDK
610 620 630 640 650
AQLLTLSAPE MTVLLGGLRV LGANVGQSRH GVFTAREQAL TNDFFVNLLD
660 670 680 690 700
MGTEWKPTAA DADVFEGRDR ATGELKWTGT RVDLVFGSHS QLRALAEVYG
710 720
SADAQEKFVR DFVAVWNKVM NLDRFDLA
Length:728
Mass (Da):79,446
Last modified:July 22, 2008 - v3
<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:iFB6EC6E5261F6740
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAK72466 differs from that shown. Reason: Erroneous initiation.Curated
The sequence CAH36875 differs from that shown. Reason: Erroneous initiation.Curated

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
AY040244 Genomic DNA Translation: AAK72466.3 Different initiation.
BX571965 Genomic DNA Translation: CAH36875.1 Different initiation.

NCBI Reference Sequences

More...
RefSeqi
WP_004522123.1, NZ_CP009538.1
WP_011205232.1, NC_006350.1
YP_109459.1, NC_006350.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
CAH36875; CAH36875; BPSL2865

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
3092072

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
bps:BPSL2865

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|272560.51.peg.2433

<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
AY040244 Genomic DNA Translation: AAK72466.3 Different initiation.
BX571965 Genomic DNA Translation: CAH36875.1 Different initiation.
RefSeqiWP_004522123.1, NZ_CP009538.1
WP_011205232.1, NC_006350.1
YP_109459.1, NC_006350.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5L02X-ray1.90A/B1-728[»]
5L05X-ray1.70A/B15-728[»]
5SW4X-ray1.90A/B15-728[»]
5SW5X-ray2.05A/B15-728[»]
5SW6X-ray1.90A/B15-728[»]
5SX0X-ray2.00A/B15-728[»]
5SX1X-ray1.80A/B1-728[»]
5SX2X-ray2.15A/B1-728[»]
5SX3X-ray2.00A/B1-728[»]
5SX6X-ray1.90A/B1-728[»]
5SX7X-ray1.95A/B1-728[»]
5SXQX-ray2.10A/B1-728[»]
5SXRX-ray1.69A/B1-728[»]
5SXSX-ray1.89A/B1-728[»]
5SXTX-ray1.90A/B1-728[»]
5SXWX-ray1.60A/B1-728[»]
5SXXX-ray1.70A/B1-728[»]
5SYHX-ray1.65A/B15-728[»]
5SYIX-ray1.70A/B15-728[»]
5SYKX-ray1.80A/B1-728[»]
5SYLX-ray1.95A/B1-728[»]
5SYVX-ray1.75A/B1-728[»]
5SYXX-ray1.77A/B1-728[»]
6CFQX-ray1.72A/B1-728[»]
SMRiQ939D2
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272560.BPSL2865

Chemistry databases

DrugBankiDB08638 2-AMINO-3-(1-HYDROPEROXY-1H-INDOL-3-YL)PROPAN-1-OL

Protein family/group databases

PeroxiBasei2303 BpCP01_K96243

Proteomic databases

PRIDEiQ939D2

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAH36875; CAH36875; BPSL2865
GeneIDi3092072
KEGGibps:BPSL2865
PATRICifig|272560.51.peg.2433

Phylogenomic databases

eggNOGiENOG4105C1X Bacteria
COG0376 LUCA
HOGENOMiHOG000218110
KOiK03782
OMAiADVWEPE

Enzyme and pathway databases

BRENDAi1.11.1.21 1031
SABIO-RKiQ939D2

Miscellaneous databases

EvolutionaryTraceiQ939D2

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_BURPS
<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: Q939D2
Secondary accession number(s): Q63R09
<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: July 22, 2008
Last sequence update: July 22, 2008
Last modified: May 8, 2019
This is version 118 of the entry and version 3 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
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