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Protein

Catalase-peroxidase

Gene

katG

Organism
Francisella tularensis subsp. mediasiatica (strain FSC147)
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)DescriptionActionsGraphical viewLength
Sitei99Transition state stabilizerUniRule annotation1
Active sitei103Proton acceptorUniRule annotation1
Metal bindingi264Iron (heme axial ligand)UniRule annotation1

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

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:FTM_1361
OrganismiFrancisella tularensis subsp. mediasiatica (strain FSC147)
Taxonomic identifieri441952 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23UniRule annotationAdd BLAST23
ChainiPRO_000035479224 – 741Catalase-peroxidaseAdd BLAST718

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki102 ↔ 223Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-249)UniRule annotation
Cross-linki223 ↔ 249Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-102)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

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000218110.
KOiK03782.
OMAiMSTRWEK.

Family and domain databases

HAMAPiMF_01961. Catal_peroxid. 1 hit.
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.

Sequence processingi: The displayed sequence is further processed into a mature form.

B2SDI5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKKIVTALG MSGMLLASSN AIAEDTTTKN DNLSPQSVDL SPLRNLNKLD
60 70 80 90 100
SPMDKDYNYH QAFKKLDTEQ LKKDMQDLLT QSQDWWPADF GNYGPFFIRL
110 120 130 140 150
SWHDAGTYRI YDGRGGANRG QQRFSPLNSW PDNVNLDKAR QLLWPIKQKY
160 170 180 190 200
GDAVSWSDLI VLAGTVSLES MGMKPIGFAF GREDDWQGDD TNWGLSPEEI
210 220 230 240 250
MSSNVRDGKL APAYAATQMG LIYVNPEGPD GKPDIKGAAS EIRQAFRAMG
260 270 280 290 300
MTDKETVALI AGGHTFGKTH GAVPEDKVKQ AIGPAPDKAP IEQQGLGWHN
310 320 330 340 350
SYGTGNGDDT MGSGLEGSWT STPTFWNHDF LHNLYNLDWK KTLSPAGAHQ
360 370 380 390 400
WTPTNAKPEN MVPDAHKPGV KHKPIMFTTD LALKEDDGFN KYTQEFYNNP
410 420 430 440 450
EEFKEEFAKA WFKLTHRDMG PKSRYIGPWI PEQNFIWQDP VPAADYKQVS
460 470 480 490 500
TQDIAQLEQD IINSGLTNQQ LIKTAWDSAS TYRKTDYRGG SNGARIALAP
510 520 530 540 550
EKDWQMNEPA KLEVVLTKLK EIQTNFNNSK ADGTKVSLAD LIVLGGNVGV
560 570 580 590 600
EQAAKQAGYN IQMPFVPGRT DATQAQTDIE SFNYLKTKSD GFINYTDGSV
610 620 630 640 650
SADKLPQTLV EKASMLDLNI PEMTVLVGGM RALDVNYDNS QKGVLTTTPG
660 670 680 690 700
QLNNSFFVNL LDMSTQWKKS DKKDGEYIGI DRKTGKQKWT ASPVDLIFGS
710 720 730 740
NSELKAVAQV YAENGNEQKF VNDFAKAWHK VMMLGRFDVQ Q
Length:741
Mass (Da):82,470
Last modified:July 1, 2008 - v1
Checksum:iF5B165A02E677E50
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000915 Genomic DNA. Translation: ACD31199.1.
RefSeqiWP_012429725.1. NC_010677.1.

Genome annotation databases

EnsemblBacteriaiACD31199; ACD31199; FTM_1361.
KEGGiftm:FTM_1361.
PATRICi17957640. VBIFraTul67519_1701.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000915 Genomic DNA. Translation: ACD31199.1.
RefSeqiWP_012429725.1. NC_010677.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACD31199; ACD31199; FTM_1361.
KEGGiftm:FTM_1361.
PATRICi17957640. VBIFraTul67519_1701.

Phylogenomic databases

HOGENOMiHOG000218110.
KOiK03782.
OMAiMSTRWEK.

Family and domain databases

HAMAPiMF_01961. Catal_peroxid. 1 hit.
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...

Entry informationi

Entry nameiKATG_FRATM
AccessioniPrimary (citable) accession number: B2SDI5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: July 1, 2008
Last modified: November 2, 2016
This is version 50 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.