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Protein

Catalase-peroxidase

Gene

katG

Organism
Synechococcus sp. (strain RCC307)
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
Sitei94 – 941Transition state stabilizerUniRule annotation
Active sitei98 – 981Proton acceptorUniRule annotation
Metal bindingi261 – 2611Iron (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

Protein family/group databases

PeroxiBasei6243. SspCP01_RCC307.

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:SynRCC307_1434
OrganismiSynechococcus sp. (strain RCC307)
Taxonomic identifieri316278 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus
Proteomesi
  • UP000001115 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222UniRule annotationAdd
BLAST
Chaini23 – 732710Catalase-peroxidasePRO_0000354944Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki97 ↔ 220Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-246)UniRule annotation
Cross-linki220 ↔ 246Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-97)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

STRINGi316278.SynRCC307_1434.

Structurei

3D structure databases

ProteinModelPortaliA5GTX8.
SMRiA5GTX8. Positions 21-731.
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.
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.

Sequence processingi: The displayed sequence is further processed into a mature form.

A5GTX8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSMAEMRCPF SGHGAATTPA SATTNQHWWP EQINLGLLHQ HNPAANPLGS
60 70 80 90 100
NFDYRQAFNS LDLNAVKADL MALMTDSQSW WPADWGHYGG LFIRMAWHSA
110 120 130 140 150
GTYRLADGRG GAGHGNQRFA PLNSWPDNTN LDKARRLLWP IKAKYGSNLS
160 170 180 190 200
WADLIILAGN CALESMGLPT AGFAGGREDI WEPEDDIYWG SETSWLSDER
210 220 230 240 250
HDNDGAIESP LAATEMGLIY VNPEGPHGEP DPVASGREVR DTFARMGMNN
260 270 280 290 300
EETVALVAGG HTFGKAHGAA PSAHLGADPE GAALEQLGLG WQNTYASGCG
310 320 330 340 350
ADTITSGIEG AWKPNPTRWD QGYFEMLFGY EWELHQSPAG AWQWHPKDVK
360 370 380 390 400
AEHMIPDAHV PGRSAPPMMT TADLSLRFDP VYEPIARRFL GDPQAFGNAF
410 420 430 440 450
AQAWFKLTHR DLGPRSCYLG ADVPEAVMSW QDPLPTTSHP TIDAPAVDAL
460 470 480 490 500
KQELLNTGLS HGELISTAWA SAASFRQSDR RGGANGARLR LQPQCNWELN
510 520 530 540 550
NPEQLKRVLS VLEAVQMRFN QQHQGGMQVS LADLIVLSGS AAVEQAMAAT
560 570 580 590 600
GQRCRVRFTP GRVDASAEQT DNASFNALKP IADGFRNYLR SDLPLKAEQL
610 620 630 640 650
LVDRAQQLHL SAPEMTALIG GFRVLGLNWD GSDIGVFTSR PGQFSNDFFV
660 670 680 690 700
NLLDMSTQWS PVEGHSNLYQ GIDTETKQPR WRASRVDLVF GSHAQLRAIA
710 720 730
EVYGQAGGSA RLAADFSAAW SKVMELDRFD LL
Length:732
Mass (Da):80,124
Last modified:June 12, 2007 - v1
Checksum:i9F8A4D9287C25390
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CT978603 Genomic DNA. Translation: CAK28337.1.

Genome annotation databases

EnsemblBacteriaiCAK28337; CAK28337; SynRCC307_1434.
KEGGisyr:SynRCC307_1434.
PATRICi23823767. VBISynSp108374_1435.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CT978603 Genomic DNA. Translation: CAK28337.1.

3D structure databases

ProteinModelPortaliA5GTX8.
SMRiA5GTX8. Positions 21-731.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi316278.SynRCC307_1434.

Protein family/group databases

PeroxiBasei6243. SspCP01_RCC307.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAK28337; CAK28337; SynRCC307_1434.
KEGGisyr:SynRCC307_1434.
PATRICi23823767. VBISynSp108374_1435.

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]
ProtoNetiSearch...

Publicationsi

  1. Genoscope
    Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: RCC307.

Entry informationi

Entry nameiKATG_SYNR3
AccessioniPrimary (citable) accession number: A5GTX8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: June 12, 2007
Last modified: December 9, 2015
This is version 56 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.