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Protein

Catalase-peroxidase 1

Gene

katG1

Organism
Escherichia coli O157:H7
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
Sitei102Transition state stabilizerUniRule annotation1
Active sitei106Proton acceptorUniRule annotation1
Metal bindingi267Iron (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

PeroxiBasei2718. EcoH7CP01_Sakai.
3673. EcoH7CP01_EDL933.

Names & Taxonomyi

Protein namesi
Recommended name:
Catalase-peroxidase 1UniRule annotation (EC:1.11.1.21UniRule annotation)
Short name:
CP 1UniRule annotation
Alternative name(s):
Peroxidase/catalase 1UniRule annotation
Gene namesi
Name:katG1UniRule annotation
Ordered Locus Names:Z5497, ECs4871
OrganismiEscherichia coli O157:H7
Taxonomic identifieri83334 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000558 Componenti: Chromosome
  • UP000002519 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003547811 – 726Catalase-peroxidase 1Add BLAST726

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki105 ↔ 226Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-252)UniRule annotation
Cross-linki226 ↔ 252Tryptophyl-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

Proteomic databases

PRIDEiQ7A978.

Interactioni

Subunit structurei

Homodimer or homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi155864.Z5497.

Structurei

3D structure databases

ProteinModelPortaliQ7A978.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C1X. Bacteria.
COG0376. LUCA.
HOGENOMiHOG000218110.
KOiK03782.
OMAiIAEVYAC.

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.

Q7A978-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTSDDIHNT TATGKCPFHQ GGHDQSAGAG TTTRDWWPNQ LRVDLLNQHS
60 70 80 90 100
NRSNPLGEDF DYRKEFSKLD YYGLKKDLKA LLTESQPWWP ADWGSYAGLF
110 120 130 140 150
IRMAWHGAGT YRSIDGRGGA GRGQQRFAPL NSWPDNVSLD KARRLLWPIK
160 170 180 190 200
QKYGQKISWA DLFILAGNVA LENSGFRTFG FGAGREDVWE PDLDVNWGDE
210 220 230 240 250
KAWLTHRHPE ALAKAPLGAT EMGLIYVNPE GPDHSGEPLS AAAAIRATFG
260 270 280 290 300
NMGMNDEETV ALIAGGHTLG KTHGAGPTSN VGPDPEAAPI EEQGLGWAST
310 320 330 340 350
YGSGVGADAI TSGLEVVWTQ TPTQWSNYFF ENLFKYEWVQ TRSPAGAIQF
360 370 380 390 400
EAVDAPEIIP DPFDPSKKRK PTMLVTDLTL RFDPEFEKIS RRFLNDPQAF
410 420 430 440 450
NEAFARAWFK LTHRDMGPKS RYIGPEVPKE DLIWQDPLPQ PIYNPTEQDI
460 470 480 490 500
IDLKFAIADS GLSVSELVSV AWASASTFRG GDKRGGANGA RLALMPQRDW
510 520 530 540 550
DVNAAAVRAL PVLEKIQKES GKASLADIIV LAGVVGVEKA ASAAGLSIHV
560 570 580 590 600
PFAPGRVDAR QDQTDIEMFE LLEPIADGFR NYRARLDVST TESLLIDKAQ
610 620 630 640 650
QLTLTAPEMT ALVGGMRVLG ANFDGSKNGV FTDRVGVLSN DFFVNLLDMR
660 670 680 690 700
YEWKATDESK ELFEGRDRET GEVKYTASRA DLVFGSNSVL RAVAEVYASS
710 720
DAHEKFVKDF VAAWVKVMNL DRFDLL
Length:726
Mass (Da):80,040
Last modified:July 5, 2004 - v1
Checksum:i24D32EA9DEB33A06
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000007 Genomic DNA. Translation: BAB38294.1.
AE005174 Genomic DNA. Translation: AAG59143.1.
PIRiC86085.
G91237.
RefSeqiNP_312898.1. NC_002695.1.
WP_001297636.1. NZ_LPWC02000002.1.

Genome annotation databases

EnsemblBacteriaiAAG59143; AAG59143; Z5497.
BAB38294; BAB38294; BAB38294.
GeneIDi915019.
KEGGiece:Z5497.
ecs:ECs4871.
PATRICi18359416. VBIEscCol44059_4857.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000007 Genomic DNA. Translation: BAB38294.1.
AE005174 Genomic DNA. Translation: AAG59143.1.
PIRiC86085.
G91237.
RefSeqiNP_312898.1. NC_002695.1.
WP_001297636.1. NZ_LPWC02000002.1.

3D structure databases

ProteinModelPortaliQ7A978.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi155864.Z5497.

Protein family/group databases

PeroxiBasei2718. EcoH7CP01_Sakai.
3673. EcoH7CP01_EDL933.

Proteomic databases

PRIDEiQ7A978.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG59143; AAG59143; Z5497.
BAB38294; BAB38294; BAB38294.
GeneIDi915019.
KEGGiece:Z5497.
ecs:ECs4871.
PATRICi18359416. VBIEscCol44059_4857.

Phylogenomic databases

eggNOGiENOG4105C1X. Bacteria.
COG0376. LUCA.
HOGENOMiHOG000218110.
KOiK03782.
OMAiIAEVYAC.

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 nameiKATG1_ECO57
AccessioniPrimary (citable) accession number: Q7A978
Secondary accession number(s): Q8X765
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: July 5, 2004
Last modified: November 2, 2016
This is version 84 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.