Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Catalase-peroxidase 2

Gene

katG2

Organism
Shewanella sp. (strain MR-7)
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
Sitei102 – 1021Transition state stabilizerUniRule annotation
Active sitei106 – 1061Proton acceptorUniRule annotation
Metal bindingi268 – 2681Iron (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

BioCyciSSP60481:GHW6-602-MONOMER.

Protein family/group databases

PeroxiBasei3612. SHspCP01_MR-7.

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:Shewmr7_0574
OrganismiShewanella sp. (strain MR-7)
Taxonomic identifieri60481 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
Proteomesi
  • UP000001960 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626UniRule annotationAdd
BLAST
Chaini27 – 739713Catalase-peroxidase 2PRO_5000128535Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki105 ↔ 227Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-253)UniRule annotation
Cross-linki227 ↔ 253Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-105)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

ProteinModelPortaliQ0HZ78.
SMRiQ0HZ78. Positions 31-739.
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.

Q0HZ78-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKSTIPTLS ALTLAMSLAF GGSVIAQEQV TDNQFWWPEQ LNLSPLRQNA
60 70 80 90 100
VESNPYGSDY HYAEAFKSLD LDAVKKDIKA LMTESQDWWP ADYGHYGPFF
110 120 130 140 150
IRMAWHSAGV YRIFDGRGGA AGGQQRFEPL NSWPDNVNLD KARRLLWPIK
160 170 180 190 200
QKYGSKISWG DLMVLTGNVA LESMGFKTFG FAGGRVDDWE AEQVNWGSEK
210 220 230 240 250
AWLDSKRRNE KGELAKPMGA TQMGLIYVNP EGPNGVPDPL ASAKEIRDTF
260 270 280 290 300
GRMAMNDEET VALIAGGHTF GKAHGAHDPS KCVGADPAAS GVEAQGLGWK
310 320 330 340 350
NKCGKGHSED TVTSGLEGAW SSNPTKWTME YLTWLYTFDW VQTKSPAGHI
360 370 380 390 400
QWTPADDKAA NLVPDAHLPD KRHAPMMFTS DIALKEDPIY REITTRFLKN
410 420 430 440 450
PQEFELAFAK AWFKLTHRDM GPKARYLGAD VPAEMLIWQD PIPALDHPVI
460 470 480 490 500
DNADIKALGN KILASGLTVP ELVRTAWASA SSFRGTDMRG GANGARIRLE
510 520 530 540 550
PMMNWQANNP KELAKVLAKL EKVQKDFNGS LKGGKKVSLA DVIVLGGSVA
560 570 580 590 600
VEKAAKEAGV TVSVPFTPGR MDATQAQTDV SSFAVLEPTA DGFRNYYSKD
610 620 630 640 650
SSHSPAEMLI ERANMLNLTV PEMTVLVGGL RALGANSAGV KHGVFTDKPG
660 670 680 690 700
TLSNDFFVNL LDMSTKWSKS EKQEGIYEGQ DRKSGKLKWT ATPVDLVFGS
710 720 730
HSELRAVSEV YGAQDGQDRF VQDFIKAWNK VMNADRFDI
Length:739
Mass (Da):81,291
Last modified:October 3, 2006 - v1
Checksum:i73D96402FBF5C66F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000444 Genomic DNA. Translation: ABI41577.1.
RefSeqiWP_011625084.1. NC_008322.1.

Genome annotation databases

EnsemblBacteriaiABI41577; ABI41577; Shewmr7_0574.
KEGGishm:Shewmr7_0574.
PATRICi23586033. VBISheSp85603_0594.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000444 Genomic DNA. Translation: ABI41577.1.
RefSeqiWP_011625084.1. NC_008322.1.

3D structure databases

ProteinModelPortaliQ0HZ78.
SMRiQ0HZ78. Positions 31-739.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

PeroxiBasei3612. SHspCP01_MR-7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABI41577; ABI41577; Shewmr7_0574.
KEGGishm:Shewmr7_0574.
PATRICi23586033. VBISheSp85603_0594.

Phylogenomic databases

HOGENOMiHOG000218110.
KOiK03782.
OMAiYGATTMG.

Enzyme and pathway databases

BioCyciSSP60481:GHW6-602-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 nameiKATG2_SHESR
AccessioniPrimary (citable) accession number: Q0HZ78
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: October 3, 2006
Last modified: September 7, 2016
This is version 68 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.