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Protein

Catalase-peroxidase

Gene

katG

Organism
Francisella tularensis subsp. novicida (strain U112)
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
Sitei97 – 971Transition state stabilizerUniRule annotation
Active sitei101 – 1011Proton acceptorUniRule annotation
Metal bindingi262 – 2621Iron (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

BioCyciFNOV401614:GC4M-632-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:FTN_0633
OrganismiFrancisella tularensis subsp. novicida (strain U112)
Taxonomic identifieri401614 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella
Proteomesi
  • UP000000762 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323UniRule annotationAdd
BLAST
Chaini24 – 739716Catalase-peroxidasePRO_0000354793Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki100 ↔ 221Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-247)UniRule annotation
Cross-linki221 ↔ 247Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-100)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

Structurei

3D structure databases

ProteinModelPortaliA0Q5L1.
SMRiA0Q5L1. Positions 32-737.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000218110.
KOiK03782.
OMAiYGATTMG.

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.

A0Q5L1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKKIVTALG MSGMLLASNS AIADDKNTET ATPQSVDLSP LRNLNKLDSP
60 70 80 90 100
MDKDYNYHQA FKKLDPEQLK KDMQDLLTQS QDWWPADFGN YGPFFIRLSW
110 120 130 140 150
HDAGTYRIYD GRGGANRGQQ RFSPLNSWPD NVNLDKARQL LWPIKQKYGD
160 170 180 190 200
AVSWSDLIVL AGTVSLESMG MKPIGFAFGR EDDWQGDDTN WGLSPEEIMS
210 220 230 240 250
SNVRDGKLAP AYAATQMGLI YVNPEGPDGK PDIKGAASEI RQAFRAMGMT
260 270 280 290 300
DKETVALIAG GHTFGKTHGA VPEDKVKEAI GPAPDKAPIE QQGLGWHNSY
310 320 330 340 350
GTGNGDDTMG SGLEGSWTST PTFWNHDFLH NLYNLNWKKT LSPAGAHQWT
360 370 380 390 400
PTNAKPENMV PDAHKLGVKH KPIMFTTDLA LKEDDGFNKY TQEFYNNPEE
410 420 430 440 450
FKEEFAKAWF KLTHRDMGPK SRYIGPWIPE QNFIWQDPVP AADYKQVSTQ
460 470 480 490 500
DIAQLKQDII DSGLTNQQLI KTAWDSASTY RKTDYRGGSN GARIALAPEK
510 520 530 540 550
DWQMNEPAKL EVVLAKLKEI QTNFNNSKTD GTKVSLADLI VLGGNVGVEQ
560 570 580 590 600
AAKQAGYNIQ IPFVPGRTDA TQAQTDIESF NYLKTKSDGF INYTDGSVSA
610 620 630 640 650
DKLPQALVEK ASMLDLNIPE MTVLVGGMRA LNVNYDNSQE GVLTTTPGQL
660 670 680 690 700
NNSFFVNLLD MSTQWKKSDK KDGEYIGIGR KTGKQKWTAS PVDLIFGSNS
710 720 730
ELKAVAQVYA ENGNEQKFVN DFAKAWHKVM MLGRFDVQQ
Length:739
Mass (Da):82,132
Last modified:January 9, 2007 - v1
Checksum:i34C111AB5BD8E577
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000439 Genomic DNA. Translation: ABK89526.1.
RefSeqiWP_003038704.1. NZ_CP009633.1.

Genome annotation databases

EnsemblBacteriaiABK89526; ABK89526; FTN_0633.
KEGGiftn:FTN_0633.
ftx:AW25_1393.
PATRICi17934364. VBIFraNov128299_0652.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000439 Genomic DNA. Translation: ABK89526.1.
RefSeqiWP_003038704.1. NZ_CP009633.1.

3D structure databases

ProteinModelPortaliA0Q5L1.
SMRiA0Q5L1. Positions 32-737.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABK89526; ABK89526; FTN_0633.
KEGGiftn:FTN_0633.
ftx:AW25_1393.
PATRICi17934364. VBIFraNov128299_0652.

Phylogenomic databases

HOGENOMiHOG000218110.
KOiK03782.
OMAiYGATTMG.

Enzyme and pathway databases

BioCyciFNOV401614:GC4M-632-MONOMER.

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_FRATN
AccessioniPrimary (citable) accession number: A0Q5L1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: January 9, 2007
Last modified: September 7, 2016
This is version 64 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

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.