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Protein

Catalase-peroxidase

Gene

katG

Organism
Mycobacterium sp. (strain MCS)
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
Sitei110 – 1101Transition state stabilizerUniRule annotation
Active sitei114 – 1141Proton acceptorUniRule annotation
Metal bindingi281 – 2811Iron (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

BioCyciMSP164756:GHQ8-2700-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:Mmcs_2682
OrganismiMycobacterium sp. (strain MCS)
Taxonomic identifieri164756 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 749749Catalase-peroxidasePRO_0000354843Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki113 ↔ 240Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-266)UniRule annotation
Cross-linki240 ↔ 266Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-113)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

Proteomic databases

PRIDEiQ1B8J4.

Interactioni

Subunit structurei

Homodimer or homotetramer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ1B8J4.
SMRiQ1B8J4. Positions 40-746.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

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. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q1B8J4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSDTSDTRP PHSDSGTQSN SESENPIIDS PEPKAHAPLT NKDWWPEQVD
60 70 80 90 100
VSVLHKQNDK GNPLGEDFNY AEAFAQLDLE AFKRDVIEVI QTSQDWWPAD
110 120 130 140 150
YGNYAGLFIR MSWHAAGTYR IFDGRGGAGQ GSQRFAPLNS WPDNANLDKA
160 170 180 190 200
RRLLWPIKQK YGNKISWADL IAYAGNAALE QSGFKTAGFA FGREDIWEPE
210 220 230 240 250
EMLWGQEDTW LGTDKRYGGT NEDKRELAEP FGATTMGLIY VNPEGPEGKP
260 270 280 290 300
DPLAAAHDIR ETFGRMAMND EETAALIVGG HTLGKTHGAA DVNVGPEPEG
310 320 330 340 350
APIEEQGLGW KCPFGTGNAN DTVTSGLEVI WTGTNSEWSN RYLEILYGNE
360 370 380 390 400
WELTKSPAGA WQFEAKNAEA TIPDPFGGPP RKPTMLVTDV SMREDPIYGQ
410 420 430 440 450
ITRRWLDHPE EMDEAFAKAW YKLMHRDMGP ISRYLGPWVA EPEIWQDPVP
460 470 480 490 500
DVDHELVDES DIASLKSKVL ESGLTVQQLV KTAWASASSF RGTDKRGGAN
510 520 530 540 550
GARVRLEPQR SWEGNEPAEL AKVLPTLEQI QQDFNASASG GKKISLADLI
560 570 580 590 600
VLAGSAAVEK AAKDAGYEID VHFAPGRTDA SQEQTDVESF AVLETKADGF
610 620 630 640 650
RNYIRPGQKT SVEKLLVEKA YLLDLTAPEM TALLGGLRVL NVNHGGSKHG
660 670 680 690 700
VFTNSPGALS NDFFVNLLDM NTAWKPSENT ENVFEGRDRA TGEIKWTATA
710 720 730 740
NDLVFGSNSV LRGIAEVYAQ DDSKDKFVED FVAAWVKVMN NDRFDLEKF
Length:749
Mass (Da):82,684
Last modified:July 11, 2006 - v1
Checksum:i573DCEDAC5BE1391
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000384 Genomic DNA. Translation: ABG08790.1.
RefSeqiWP_011560076.1. NC_008146.1.

Genome annotation databases

EnsemblBacteriaiABG08790; ABG08790; Mmcs_2682.
KEGGimmc:Mmcs_2682.
PATRICi18115615. VBIMycSp106721_2756.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000384 Genomic DNA. Translation: ABG08790.1.
RefSeqiWP_011560076.1. NC_008146.1.

3D structure databases

ProteinModelPortaliQ1B8J4.
SMRiQ1B8J4. Positions 40-746.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ1B8J4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABG08790; ABG08790; Mmcs_2682.
KEGGimmc:Mmcs_2682.
PATRICi18115615. VBIMycSp106721_2756.

Phylogenomic databases

HOGENOMiHOG000218110.
KOiK03782.
OMAiVVWTPTP.
OrthoDBiEOG6RRKKM.

Enzyme and pathway databases

BioCyciMSP164756:GHQ8-2700-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. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MCS.

Entry informationi

Entry nameiKATG_MYCSS
AccessioniPrimary (citable) accession number: Q1B8J4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: July 11, 2006
Last modified: December 9, 2015
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.