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Protein

Catalase-peroxidase

Gene

katG

Organism
Clostridium botulinum (strain Eklund 17B / Type B)
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
Sitei92 – 921Transition state stabilizerUniRule annotation
Active sitei96 – 961Proton acceptorUniRule annotation
Metal bindingi259 – 2591Iron (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

BioCyciCBOT508765:GJ4H-1360-MONOMER.

Protein family/group databases

PeroxiBasei6254. CboCP01.

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:CLL_A1367
OrganismiClostridium botulinum (strain Eklund 17B / Type B)
Taxonomic identifieri935198 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
Proteomesi
  • UP000001195 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 730730Catalase-peroxidasePRO_0000354764Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki95 ↔ 218Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-244)UniRule annotation
Cross-linki218 ↔ 244Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-95)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

PRIDEiB2TJE9.

Interactioni

Subunit structurei

Homodimer or homotetramer.UniRule annotation

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

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.

B2TJE9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTENKCPVTG KMGKATAGSG TTNKDWWPNQ LNLNILHQNS QLSNPMSKDF
60 70 80 90 100
NYAEEFKKLD FQALKVDLYM LMTDSQIWWP ADYGNYGPLF IRMAWHSAGT
110 120 130 140 150
YRVGDGRGGG SLGLQRFAPL NSWPDNINLD KARRLLWPIK KKYGNKISWA
160 170 180 190 200
DLLILTGNCA LESMGLKTLG FGGGRVDVWE PQEDIYWGSE KEWLGDEREK
210 220 230 240 250
GDKELENPLA AVQMGLIYVN PEGPNGNPDP LGSAHDVRET FARMAMNDEE
260 270 280 290 300
TVALIAGGHT FGKCHGAASP SYVGPAPEAA PIEEQGLGWK NTYGSGNGDD
310 320 330 340 350
TIGSGLEGAW KANPTKWTMG YLKTLFKYDW ELVKSPAGAY QWLAKNVDEE
360 370 380 390 400
DMVIDAEDST KKHRPMMTTA DLGLRYDPIY EPIARNYLKN PEKFAHDFAS
410 420 430 440 450
AWFKLTHRDM GPISRYLGPE VPKESFIWQD PIPLVKHKLI TKKDITHIKK
460 470 480 490 500
KILDSGLSIS DLVATAWASA STFRGSDKRG GANGGRIRLE PQKNWEVNEP
510 520 530 540 550
KKLNNVLNTL KQIKENFNSS HSKDKKVSLA DIIILGGCVG IEQAAKRAGY
560 570 580 590 600
NINVPFIPGR TDAIQEQTDV KSFAVLEPKE DGFRNYLKTK YVVKPEDMLI
610 620 630 640 650
DRAQLLTLTA PEMTVLIGGM RVLNCNYNKS KDGVFTNRPE CLTNDFFVNL
660 670 680 690 700
LDMNTVWKPK SEDKDRFEGF DRETGELKWT ATRVDLIFGS NSQLRAIAEV
710 720 730
YACDDNKEKF IQDFIFAWNK IMNADRFEIK
Length:730
Mass (Da):82,089
Last modified:July 1, 2008 - v1
Checksum:i0EBD9CB4530E3A38
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001056 Genomic DNA. Translation: ACD21810.1.

Genome annotation databases

EnsemblBacteriaiACD21810; ACD21810; CLL_A1367.
KEGGicbk:CLL_A1367.
PATRICi19395580. VBICloBot123574_1300.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001056 Genomic DNA. Translation: ACD21810.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

PeroxiBasei6254. CboCP01.

Proteomic databases

PRIDEiB2TJE9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACD21810; ACD21810; CLL_A1367.
KEGGicbk:CLL_A1367.
PATRICi19395580. VBICloBot123574_1300.

Phylogenomic databases

HOGENOMiHOG000218110.
KOiK03782.
OMAiTESKCPF.
OrthoDBiEOG6RRKKM.

Enzyme and pathway databases

BioCyciCBOT508765:GJ4H-1360-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. "Complete sequence of Clostridium botulinum strain Eklund."
    Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A., Smith T.J., Sutton G., Brettin T.S.
    Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Eklund 17B / Type B.

Entry informationi

Entry nameiKATG_CLOBB
AccessioniPrimary (citable) accession number: B2TJE9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: July 1, 2008
Last modified: November 11, 2015
This is version 48 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.