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Protein

Catalase-peroxidase 2

Gene

katG2

Organism
Shewanella frigidimarina (strain NCIMB 400)
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
Sitei123Transition state stabilizerUniRule annotation1
Active sitei127Proton acceptorUniRule annotation1
Metal bindingi289Iron (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

Protein family/group databases

PeroxiBasei2663. SfrCP02_NCIMB400.

Names & Taxonomyi

Protein namesi
Recommended name:
Catalase-peroxidase 2UniRule annotation (EC:1.11.1.21UniRule annotation)
Short name:
CP 2UniRule annotation
Alternative name(s):
Peroxidase/catalase 2UniRule annotation
Gene namesi
Name:katG2UniRule annotation
Ordered Locus Names:Sfri_3122
OrganismiShewanella frigidimarina (strain NCIMB 400)
Taxonomic identifieri318167 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
Proteomesi
  • UP000000684 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 26UniRule annotationAdd BLAST26
ChainiPRO_500013099827 – 757Catalase-peroxidase 2Add BLAST731

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki126 ↔ 248Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-274)UniRule annotation
Cross-linki248 ↔ 274Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-126)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

PRIDEiQ07YF5.

Interactioni

Subunit structurei

Homodimer or homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi318167.Sfri_3122.

Structurei

3D structure databases

ProteinModelPortaliQ07YF5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105C1X. Bacteria.
COG0376. LUCA.
HOGENOMiHOG000218110.
KOiK03782.
OMAiMSTRWEK.
OrthoDBiPOG091H05R1.

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. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q07YF5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKHPLFNQKV LAGFVSMLLI SGSAFASNNE KSEMTKPKGA VGTGVALENQ
60 70 80 90 100
ARTNQFWWPD QLNLSALRDH DKRSNPYGEN FDYAKAFNSL DLDKVKLDIN
110 120 130 140 150
ALLTTSQDWW PSDYSNYGPF FIRMTWHSAG TYRTLDGRGG AGGGQQRFEP
160 170 180 190 200
LNSWPDNASL DKARRLLWPI KMKYGEAISW SDLIVLAGNV SLENMGFKTY
210 220 230 240 250
GFAGGRHDDW EPDMVYWGPE IEMLASDRED NGGKLQRPLG ATHMGLIYVN
260 270 280 290 300
PEGPKGVPDP LGSAKNIRVA FERMAMNDEE TLALIAGGHT FGKMHGAHKP
310 320 330 340 350
KDCLGAEPAA AGIEEQGLGW KNKCGKGHSE DTITSGLEGA WTQAPTKWTS
360 370 380 390 400
LYLSNLLTFE WKQTRSPAGA IQWIPTDESL HKAVPDAHVK GKFHAPVMTT
410 420 430 440 450
ADLALKYDPE YRKIAERFLA DPEEYRLAFA KAWYKLTHRD MGPSRNFLGK
460 470 480 490 500
EVPKESLIWQ DPIDDKTQSN IDADGVQELK AQILKSNLTV SELVRVAWAS
510 520 530 540 550
AASYRHSDMR GGANGARIAL SPQKDWSVNN PAETAKVIKT LKAIQEDYND
560 570 580 590 600
SLFSKSKVSL ADLIVLGGTA AIEKAAKDAG FTVSVPFNAG RGDATQAMTD
610 620 630 640 650
INAFSLLELT SDGFRNYFDA QQSYKSPVDM LVDKADQLNL SVPEMTVLVG
660 670 680 690 700
GLRALDANYK GLKHGVLTST PGTLNNDFFV NLLDMSTVWK KSSTDGIYEG
710 720 730 740 750
FDRQSGHKKW TATSVDLVFG SNSELRAVSE VYAFDTSKQK FVEDFAAAWT

KVMNLDR
Length:757
Mass (Da):83,632
Last modified:October 31, 2006 - v1
Checksum:iB32EA3AA64FB2459
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000447 Genomic DNA. Translation: ABI72959.1.
RefSeqiWP_011638565.1. NC_008345.1.

Genome annotation databases

EnsemblBacteriaiABI72959; ABI72959; Sfri_3122.
KEGGisfr:Sfri_3122.
PATRICi23500391. VBISheFri14343_3236.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000447 Genomic DNA. Translation: ABI72959.1.
RefSeqiWP_011638565.1. NC_008345.1.

3D structure databases

ProteinModelPortaliQ07YF5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi318167.Sfri_3122.

Protein family/group databases

PeroxiBasei2663. SfrCP02_NCIMB400.

Proteomic databases

PRIDEiQ07YF5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABI72959; ABI72959; Sfri_3122.
KEGGisfr:Sfri_3122.
PATRICi23500391. VBISheFri14343_3236.

Phylogenomic databases

eggNOGiENOG4105C1X. Bacteria.
COG0376. LUCA.
HOGENOMiHOG000218110.
KOiK03782.
OMAiMSTRWEK.
OrthoDBiPOG091H05R1.

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. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiKATG2_SHEFN
AccessioniPrimary (citable) accession number: Q07YF5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: October 31, 2006
Last modified: November 2, 2016
This is version 71 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.