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Protein

Catalase-peroxidase

Gene

katG

Organism
Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013)
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
Sitei91 – 911Transition state stabilizerUniRule annotation
Active sitei95 – 951Proton acceptorUniRule annotation
Metal bindingi263 – 2631Iron (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

BioCyciSDEN318161:GHKQ-1432-MONOMER.

Protein family/group databases

PeroxiBasei2713. SdeCP01.

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:Sden_1384
OrganismiShewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013)
Taxonomic identifieri318161 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
Proteomesi
  • UP000001982 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121UniRule annotationAdd
BLAST
Chaini22 – 720699Catalase-peroxidasePRO_0000354917Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki94 ↔ 222Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-248)UniRule annotation
Cross-linki222 ↔ 248Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-94)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

Protein-protein interaction databases

STRINGi318161.Sden_1384.

Structurei

3D structure databases

ProteinModelPortaliQ12PF6.
SMRiQ12PF6. Positions 25-719.
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.
OMAiEICERET.
OrthoDBiEOG6RRKKM.

Family and domain databases

HAMAPiMF_01961. Catal_peroxid.
InterProiIPR000763. Catalase_peroxidase.
IPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR019794. Peroxidases_AS.
[Graphical view]
PfamiPF00141. peroxidase. 2 hits.
[Graphical view]
PRINTSiPR00460. BPEROXIDASE.
PR00458. PEROXIDASE.
SUPFAMiSSF48113. SSF48113. 2 hits.
TIGRFAMsiTIGR00198. cat_per_HPI. 1 hit.
PROSITEiPS00436. 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.

Q12PF6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSENKCPVMH GSATTTENSM ANMNWWPKSL SLDILHQHDH KTNPMAADFN
60 70 80 90 100
YQDEVKKLDF VALKNDLHAL MTDSQAWWPA DWGHYGGLMI RLTWHAAGTY
110 120 130 140 150
RIADGRGGAG HGSQRFAPLN SWPDNGNLDK ARRLLWPIKK KYGNKLSWAD
160 170 180 190 200
LIAYAGTIAY ESMGLKTFGF AFGREDIWHP EKDIYWGAEK DWLLPTDNDN
210 220 230 240 250
SRYSGERNLE NPLAAVMMGL IYVNPEGVDG KPDPLKTAQD IRETFARMAM
260 270 280 290 300
NDEETVALTA GGHTVGKAHG NGNADLLGPE PEDADIHDQG FGWLNKAKRG
310 320 330 340 350
IGRDTVTSGI EGAWTTHPTQ WDNGYFTMLL NHEWELCKSP AGAWQWQPIN
360 370 380 390 400
IKEEDKPRDV EDPSISTMPM MTDADMAMKM DPEYRKISEH FHRDPEYFSK
410 420 430 440 450
VFSRAWFKLT HRDMGPKVRY LGPDVPVEDL LWQDPVPTGP KDFNVAVVKK
460 470 480 490 500
AIKETGLSIS DMVTTAWDSA RTFRGSDKRG GANGARIRLA LQKQWAGNEP
510 520 530 540 550
KRLASVLSVL EPIAASHGVS VADVIVLAGN LGIELAAKKA GFDVTVPFIS
560 570 580 590 600
GRGDATDEMT DNESFAVLEP LHDGYRNWLK QDFAVSAEEL MLDRTQLMGL
610 620 630 640 650
TAHEMTVLVG GMRVIGTNYA ETGHGVFTER KGALTNDFFV NLTDMNYIWK
660 670 680 690 700
PIGQNEYEIC ERETGKRKWT ASRVDLIFGS NSVLRSYAEV YAQDDNKQKF
710 720
VNDFISAWTK MMNADRFDVS
Length:720
Mass (Da):80,755
Last modified:August 22, 2006 - v1
Checksum:i776975A1B1174F09
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000302 Genomic DNA. Translation: ABE54670.1.
RefSeqiWP_011495828.1. NC_007954.1.

Genome annotation databases

EnsemblBacteriaiABE54670; ABE54670; Sden_1384.
KEGGisdn:Sden_1384.
PATRICi23488570. VBISheDen79529_1471.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000302 Genomic DNA. Translation: ABE54670.1.
RefSeqiWP_011495828.1. NC_007954.1.

3D structure databases

ProteinModelPortaliQ12PF6.
SMRiQ12PF6. Positions 25-719.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi318161.Sden_1384.

Protein family/group databases

PeroxiBasei2713. SdeCP01.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABE54670; ABE54670; Sden_1384.
KEGGisdn:Sden_1384.
PATRICi23488570. VBISheDen79529_1471.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciSDEN318161:GHKQ-1432-MONOMER.

Family and domain databases

HAMAPiMF_01961. Catal_peroxid.
InterProiIPR000763. Catalase_peroxidase.
IPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR019794. Peroxidases_AS.
[Graphical view]
PfamiPF00141. peroxidase. 2 hits.
[Graphical view]
PRINTSiPR00460. BPEROXIDASE.
PR00458. PEROXIDASE.
SUPFAMiSSF48113. SSF48113. 2 hits.
TIGRFAMsiTIGR00198. cat_per_HPI. 1 hit.
PROSITEiPS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: OS217 / ATCC BAA-1090 / DSM 15013.

Entry informationi

Entry nameiKATG_SHEDO
AccessioniPrimary (citable) accession number: Q12PF6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: August 22, 2006
Last modified: November 11, 2015
This is version 72 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.