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Protein

Catalase-peroxidase

Gene

katG

Organism
Jannaschia sp. (strain CCS1)
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 bindingi269 – 2691Iron (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

BioCyciJSP290400:GI1R-1598-MONOMER.

Protein family/group databases

PeroxiBasei3654. JspCP01_CCS1.

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:Jann_1586
OrganismiJannaschia sp. (strain CCS1)
Taxonomic identifieri290400 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeJannaschia
Proteomesi
  • UP000008326 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 735735Catalase-peroxidasePRO_0000354812Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki100 ↔ 228Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-254)UniRule annotation
Cross-linki228 ↔ 254Tryptophyl-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

Proteomic databases

PRIDEiQ28S09.

Interactioni

Subunit structurei

Homodimer or homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi290400.Jann_1586.

Structurei

3D structure databases

ProteinModelPortaliQ28S09.
SMRiQ28S09. Positions 25-733.
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.

Q28S09-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMDGAQTNSG GCPVMHGGGS RPMGATANQH WWPNQLNLKP LSANSEKLDP
60 70 80 90 100
MGEGFDYAEE FQKLDMAAVK ADIANCLKDS QDWWPADYGH YGPLMIRLAW
110 120 130 140 150
HSAGTYRTYD GRGGAGTGTQ RFAPLNSWPD NGNLDKARRI LWPIKEKYGK
160 170 180 190 200
SLSWADLLIL VGNVALEDMG FETFGFAGGR ADVWEPEEDI YWGPETEWLA
210 220 230 240 250
TSDMENTRYG EGRDLHNPLA AVQMGLIYVN PQGPDGNPDP LASAFDIRDT
260 270 280 290 300
FARMAMNDEE TVALVAGGHT FGKAHGAGDP DLVGAEPEGA DVAEMGLGWK
310 320 330 340 350
NGFESGKGVH STTSGVEGPW TPTPTQWDMS YFDVLFGHEW ELTKSPAGAH
360 370 380 390 400
QWRPVDHEND QAPQVDGNGT VPIMMTTADM AMRMDPAYEK ISRDFHANPD
410 420 430 440 450
KFADAFARAW YKLTHRDMGP IQRYLGNDVP SEELLWQDPV PMPQGPQVND
460 470 480 490 500
DEQAELKAAV AATGLTAAEL VRVAWGSAAS YRDSDKRGGA NGARIRLQPA
510 520 530 540 550
RGWTVNNPEE LDKVLPVLDS IADAFNGRGG TQITMADMIV LAGGVGVEMA
560 570 580 590 600
AREAGHNIHV PFTPGRGDAT QEQTDVDSYD VLEPTSDGFR NYHATFSLRE
610 620 630 640 650
PAEMLVDKAA LLGLTAPEMT VLVGGLRAIG ATHGGARHGV LTETPGALNN
660 670 680 690 700
AFFKNVLSMD TVWNQTDSAI LEGKDRASGQ VKWTATIVDL VFGSNSQLRA
710 720 730
VAEVYASADA EAKMVDDFVA AWVKVMENDR FDLHR
Length:735
Mass (Da):79,928
Last modified:April 4, 2006 - v1
Checksum:i3F76E871ACC57D4A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000264 Genomic DNA. Translation: ABD54503.1.

Genome annotation databases

EnsemblBacteriaiABD54503; ABD54503; Jann_1586.
KEGGijan:Jann_1586.
PATRICi22146878. VBIJanSp43325_1709.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000264 Genomic DNA. Translation: ABD54503.1.

3D structure databases

ProteinModelPortaliQ28S09.
SMRiQ28S09. Positions 25-733.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi290400.Jann_1586.

Protein family/group databases

PeroxiBasei3654. JspCP01_CCS1.

Proteomic databases

PRIDEiQ28S09.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABD54503; ABD54503; Jann_1586.
KEGGijan:Jann_1586.
PATRICi22146878. VBIJanSp43325_1709.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciJSP290400:GI1R-1598-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CCS1.

Entry informationi

Entry nameiKATG_JANSC
AccessioniPrimary (citable) accession number: Q28S09
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: April 4, 2006
Last modified: December 9, 2015
This is version 65 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.