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Protein

Catalase-peroxidase

Gene

katG

Organism
Mycobacterium marinum (strain ATCC BAA-535 / M)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity.UniRule annotation

Catalytic activityi

Donor + H2O2 = oxidized donor + 2 H2O.UniRule annotation
2 H2O2 = O2 + 2 H2O.UniRule annotation

Cofactori

heme bUniRule annotationNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei107 – 1071Transition state stabilizerUniRule annotation
Active sitei111 – 1111Proton acceptorUniRule annotation
Metal bindingi274 – 2741Iron (heme axial ligand)UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciMMAR216594:GJOB-2932-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Catalase-peroxidaseUniRule annotation (EC:1.11.1.21UniRule annotation)
Short name:
CPUniRule annotation
Alternative name(s):
Peroxidase/catalaseUniRule annotation
Gene namesi
Name:katGUniRule annotation
Ordered Locus Names:MMAR_2914
OrganismiMycobacterium marinum (strain ATCC BAA-535 / M)
Taxonomic identifieri216594 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium
Proteomesi
  • UP000001190 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 743743Catalase-peroxidasePRO_0000354838Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki110 ↔ 233Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-259)UniRule annotation
Cross-linki233 ↔ 259Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-110)UniRule annotation

Post-translational modificationi

The covalent Trp-Tyr-Met adduct is important for the catalase, but not the peroxidase activity of the enzyme.UniRule annotation

Interactioni

Subunit structurei

Homodimer or homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi216594.MMAR_2914.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C1X. Bacteria.
COG0376. LUCA.
HOGENOMiHOG000218110.
KOiK03782.
OMAiVVWTPTP.
OrthoDBiEOG6RRKKM.

Family and domain databases

HAMAPiMF_01961. Catal_peroxid.
InterProiIPR000763. Catalase_peroxidase.
IPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamiPF00141. peroxidase. 2 hits.
[Graphical view]
PRINTSiPR00460. BPEROXIDASE.
PR00458. PEROXIDASE.
SUPFAMiSSF48113. SSF48113. 2 hits.
TIGRFAMsiTIGR00198. cat_per_HPI. 1 hit.
PROSITEiPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B2HE73-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSDSRPPQP DTSTQSNSES ESPAISSPTP QDHAPMTNRD WWPNQIDVSM
60 70 80 90 100
LHPHPSQASP LGADFDYPKE FAKLDVDALK ADVMSVMTTS QDWWPADYGH
110 120 130 140 150
YGGLFIRMSW HAAGTYRIQD GRGGGGQGMQ RFAPLNSWPD NVSLDKARRL
160 170 180 190 200
LWPVKQKYGS KISWADLIIF AGNCALDSMG FKTFGFGFGR EDVWQPEEVM
210 220 230 240 250
WGEEDVWLGT DKRYSGKRDL AQPYGATTMG LIYVNPEGPE GKPDPVAAAH
260 270 280 290 300
DIRETFARMA MNDEETAALI VGGHSFGKTH GAGDADLVGP EPEAAPIEQQ
310 320 330 340 350
GFGWKSSFGS GKGKDAITSG LEVVWTPTPT QWGNGFLELL YGYEWELTKS
360 370 380 390 400
PAGAWQFTAK DGAGAGTIPD PFGGPGRAPT MLVTDISMRE DPIYRRITQR
410 420 430 440 450
WLEHPEELTE AFAKAWYKLL HRDMGPVSRY LGPWVAEPQL WQDPVPDVDH
460 470 480 490 500
ELVDAKDVAA LKSKVLASGL TVAQLVKTAW SAASSFRRTD KRGGANGGRL
510 520 530 540 550
RLEPQKSWES NEPADLDQVL SVLEGIQQDF NSSAAGGKKI SLADLIVLAG
560 570 580 590 600
SAAVEKAAKD GGHEVSVPFA PGRTDASQEN TDVESFAVLE PRADGFRNYV
610 620 630 640 650
RVGEKAPLEH LLIERAYRLG VTAPEMTVLV GGLRALGANH GGSKHGVFTD
660 670 680 690 700
NPGVLSNDFF VNLLDMGTEW KASEAAENVY EGCDRSSGQL KWTATANDLV
710 720 730 740
FGSNSVLRAL AEVYAQSDAK QKFAEDFAAA WAKVMNNDRF DLE
Length:743
Mass (Da):81,032
Last modified:June 10, 2008 - v1
Checksum:iEB005AD6563C791E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000854 Genomic DNA. Translation: ACC41353.1.
RefSeqiWP_012394612.1. NC_010612.1.

Genome annotation databases

EnsemblBacteriaiACC41353; ACC41353; MMAR_2914.
KEGGimmi:MMAR_2914.
PATRICi18066865. VBIMycMar75906_3112.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000854 Genomic DNA. Translation: ACC41353.1.
RefSeqiWP_012394612.1. NC_010612.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi216594.MMAR_2914.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACC41353; ACC41353; MMAR_2914.
KEGGimmi:MMAR_2914.
PATRICi18066865. VBIMycMar75906_3112.

Phylogenomic databases

eggNOGiENOG4105C1X. Bacteria.
COG0376. LUCA.
HOGENOMiHOG000218110.
KOiK03782.
OMAiVVWTPTP.
OrthoDBiEOG6RRKKM.

Enzyme and pathway databases

BioCyciMMAR216594:GJOB-2932-MONOMER.

Family and domain databases

HAMAPiMF_01961. Catal_peroxid.
InterProiIPR000763. Catalase_peroxidase.
IPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamiPF00141. peroxidase. 2 hits.
[Graphical view]
PRINTSiPR00460. BPEROXIDASE.
PR00458. PEROXIDASE.
SUPFAMiSSF48113. SSF48113. 2 hits.
TIGRFAMsiTIGR00198. cat_per_HPI. 1 hit.
PROSITEiPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-535 / M.

Entry informationi

Entry nameiKATG_MYCMM
AccessioniPrimary (citable) accession number: B2HE73
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: June 10, 2008
Last modified: November 11, 2015
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.