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Protein

Catalase-peroxidase

Gene

katG

Organism
Symbiobacterium thermophilum (strain T / IAM 14863)
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
Sitei85 – 851Transition state stabilizerUniRule annotation
Active sitei89 – 891Proton acceptorUniRule annotation
Metal bindingi252 – 2521Iron (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

BioCyciSTHE292459:GJMM-2494-MONOMER.

Protein family/group databases

PeroxiBasei2350. SthCP01_IAM14863.

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:STH2416
OrganismiSymbiobacterium thermophilum (strain T / IAM 14863)
Taxonomic identifieri292459 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesSymbiobacteriaceaeSymbiobacterium
Proteomesi
  • UP000000417 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 725725Catalase-peroxidasePRO_0000354940Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki88 ↔ 211Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-237)UniRule annotation
Cross-linki211 ↔ 237Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-88)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

PRIDEiQ67LP5.

Interactioni

Subunit structurei

Homodimer or homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi292459.STH2416.

Structurei

3D structure databases

ProteinModelPortaliQ67LP5.
SMRiQ67LP5. Positions 11-721.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C1X. Bacteria.
COG0376. LUCA.
HOGENOMiHOG000218110.
KOiK03782.
OMAiTESKCPF.
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.

Q67LP5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MREEDIRSTA GHGTSNKDWW PNQLNLRILH QHSEKANPMG PDFNYREEFK
60 70 80 90 100
KLDYWALKED LRKLMTESQD WWPADFGHYG PLIIRMAWHS AGTYRIQDGR
110 120 130 140 150
GGAESGAQRF APLNSWPDNI NLDKARRLLW PIKQKYGRRI SWADLMILAG
160 170 180 190 200
NVALESMGLK TIGFAGGRAD VWEPEEDIYW GSEQQWLGRD RFGEEGKLED
210 220 230 240 250
PLAASEMGLI YVNPEGPGRE PDPLKAAQQI RETFKRMGMN DEETVALIAG
260 270 280 290 300
GHTFGKTHGA ASPSHLGPEP EAAPIEEMGL GWKNSYGTGK GGDTITSGLE
310 320 330 340 350
VTWTSSPTKW TSNFLWNLFG YEWELTKSPA GAWQWRPKNG AGEGTVPDAH
360 370 380 390 400
DPNKRHAPGM LTTDIALRVD PVYEKIARRF LENPDEFAKA FARAWFKLTH
410 420 430 440 450
RDLGPRSRYL GPEVPEEEFI WQDPLPKRDY DLIDEGDIAE LKKRIQASGM
460 470 480 490 500
SIREMVMTAW ASASTFRGSD KRGGANGARI RLAPQIGWEV NEPEQLRPVL
510 520 530 540 550
ETLEGIQQEF NRSQTGRKRV SLADLIVLAG CVGIEQAARN AGFEITVPFT
560 570 580 590 600
PGRVDATQEQ TDVESFSYLE PVHDGFRNYL KRKFSVPAEH LLIDRANLLT
610 620 630 640 650
LTAPEMTVLI GGLRVLDCNW GRTKHGVLTD RPGALTNDFF VNLLDMRWKW
660 670 680 690 700
NATDDENVFE GRDRATGELK WTATRVDLIF GSNAQLRAIA EVYASNDGQE
710 720
KFVQDFVKAW TKVMNLDRFD LLVKK
Length:725
Mass (Da):81,957
Last modified:October 11, 2004 - v1
Checksum:i951B04CA6355A898
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP006840 Genomic DNA. Translation: BAD41401.1.
RefSeqiWP_011196539.1. NC_006177.1.

Genome annotation databases

EnsemblBacteriaiBAD41401; BAD41401; STH2416.
KEGGisth:STH2416.
PATRICi23783002. VBISymThe116959_2412.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP006840 Genomic DNA. Translation: BAD41401.1.
RefSeqiWP_011196539.1. NC_006177.1.

3D structure databases

ProteinModelPortaliQ67LP5.
SMRiQ67LP5. Positions 11-721.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi292459.STH2416.

Protein family/group databases

PeroxiBasei2350. SthCP01_IAM14863.

Proteomic databases

PRIDEiQ67LP5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD41401; BAD41401; STH2416.
KEGGisth:STH2416.
PATRICi23783002. VBISymThe116959_2412.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciSTHE292459:GJMM-2494-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. "Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium that depends on microbial commensalism."
    Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K., Ikeda H., Hattori M., Beppu T.
    Nucleic Acids Res. 32:4937-4944(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: T / IAM 14863.

Entry informationi

Entry nameiKATG_SYMTH
AccessioniPrimary (citable) accession number: Q67LP5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: October 11, 2004
Last modified: January 20, 2016
This is version 83 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.