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Protein

Catalase-peroxidase

Gene

katG

Organism
Polaromonas sp. (strain JS666 / ATCC BAA-500)
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
Sitei93 – 931Transition state stabilizerUniRule annotation
Active sitei97 – 971Proton acceptorUniRule annotation
Metal bindingi260 – 2601Iron (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

BioCyciPSP296591:GHI4-1399-MONOMER.

Protein family/group databases

PeroxiBasei2695. POsCP01.

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:Bpro_0678
OrganismiPolaromonas sp. (strain JS666 / ATCC BAA-500)
Taxonomic identifieri296591 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaePolaromonas
Proteomesi
  • UP000001983 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 731731Catalase-peroxidasePRO_0000354859Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki96 ↔ 219Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-245)UniRule annotation
Cross-linki219 ↔ 245Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-96)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

STRINGi296591.Bpro_0678.

Structurei

3D structure databases

ProteinModelPortaliQ12FQ6.
SMRiQ12FQ6. Positions 23-731.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C1X. Bacteria.
COG0376. LUCA.
HOGENOMiHOG000218110.
KOiK03782.
OMAiNPMGGDF.
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.

Q12FQ6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTEPNCPFS GNARKHTAAG APSNADWWPN QLKLNILHQH SAMSDPMGEA
60 70 80 90 100
FNYAQEFKSL DLEAVKKDLL ALMTNSQDWW PADFGHYGPL FIRMAWHSAG
110 120 130 140 150
TYRVSDGRGG AGSGNQRFAP LNSWPDNVNL DKARRLLWPV KQKYGRKLSW
160 170 180 190 200
ADLMILAGNV ALESMGFKTF GFAGGREDIW EPEEDVYWGS ENTWLDDKRY
210 220 230 240 250
SGDRDLENPL GAVQMGLIYV NPEGPNGNPD PIAAARDIRE TFARMAMNDE
260 270 280 290 300
ETVALIAGGH TFGKTHGAGD VKHVGPEPEA AGIEEQGLGW NSGFGTGKGG
310 320 330 340 350
DTISSGLEVT WSTTPTKWGN NYFDNLFGYE WELTTSPAGA QQWKPKGDAG
360 370 380 390 400
AGTVPDAHDP SKRHAPAMLT TDLSLRLDPA YEKISRRFHE NPDQLADAFA
410 420 430 440 450
RAWFKLTHRD MGPLSRYLGP LVPKEQLLWQ DPIPAVDHKL VDEQDIAALK
460 470 480 490 500
TRILASGLSI SQLVTTAWAS AATFRGSDKR GGANGARIRL APQKNWEVNQ
510 520 530 540 550
PAELAKVLQK LETIQKDFNS AQSGGKKVSL ADLIVLGGCA AVEAAAKKAG
560 570 580 590 600
QDVKVPFSPG RMDASQEQTD VDSFAVLEPA ADGFRNYARK GLEGSAAELL
610 620 630 640 650
VDKAQLMTLT APEMTVLIGG LRALNANVGQ SKHGVFTKQP ETLTNDFFVN
660 670 680 690 700
LLDMSTKWQK SATSEGVLEG RDRATGELKW TGTIVDLVFG SNSQLRALAE
710 720 730
VYACSDSQKS FVRDFVAAWN KVMNLDRFDL A
Length:731
Mass (Da):79,857
Last modified:August 22, 2006 - v1
Checksum:iD81D5A40BCB5AB9A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000316 Genomic DNA. Translation: ABE42636.1.
RefSeqiWP_011481639.1. NC_007948.1.

Genome annotation databases

EnsemblBacteriaiABE42636; ABE42636; Bpro_0678.
KEGGipol:Bpro_0678.
PATRICi22954418. VBIPolSp102244_0696.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000316 Genomic DNA. Translation: ABE42636.1.
RefSeqiWP_011481639.1. NC_007948.1.

3D structure databases

ProteinModelPortaliQ12FQ6.
SMRiQ12FQ6. Positions 23-731.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi296591.Bpro_0678.

Protein family/group databases

PeroxiBasei2695. POsCP01.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABE42636; ABE42636; Bpro_0678.
KEGGipol:Bpro_0678.
PATRICi22954418. VBIPolSp102244_0696.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciPSP296591:GHI4-1399-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: JS666 / ATCC BAA-500.

Entry informationi

Entry nameiKATG_POLSJ
AccessioniPrimary (citable) accession number: Q12FQ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: August 22, 2006
Last modified: December 9, 2015
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, 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.