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Protein

Catalase-peroxidase 1

Gene

katG1

Organism
Shewanella sp. (strain ANA-3)
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 bindingi266 – 2661Iron (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

BioCyciSSP94122:GJ9K-323-MONOMER.

Protein family/group databases

PeroxiBasei3616. SHspCP01_ANA-3.

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:Shewana3_0306
OrganismiShewanella sp. (strain ANA-3)
Taxonomic identifieri94122 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
Proteomesi
  • UP000002589 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222UniRule annotationAdd
BLAST
Chaini23 – 728706Catalase-peroxidase 1PRO_0000354923Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki97 ↔ 225Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-251)UniRule annotation
Cross-linki225 ↔ 251Tryptophyl-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

Proteomic databases

PRIDEiA0KRY0.

Interactioni

Subunit structurei

Homodimer or homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi94122.Shewana3_0306.

Structurei

3D structure databases

ProteinModelPortaliA0KRY0.
SMRiA0KRY0. Positions 27-727.
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.
OMAiQPEEMML.
OrthoDBiPOG091H05R1.

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.
[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. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

A0KRY0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDKTQSSQGK CPVMHGANSA VASNNMDWWP KALNLDILHQ HDKKTDPMDP
60 70 80 90 100
KFNYRDAFNS LDLAAVKRDL NALMTDSQDW WPADWGHYGG LMIRMAWHSA
110 120 130 140 150
GTYRVADGRG GAGTGNQRFA PLNSWPDNAN LDKARRLLWP IKKKYGNKLS
160 170 180 190 200
WADLMILAGN VAYESMGLKT YGFAGGREDI WHPEKDIYWG SEKQWLAPTE
210 220 230 240 250
NPNSRYSGER DLENPLAAVM MGLIYVNPEG VDGKPDPLRT AQDVRVTFAR
260 270 280 290 300
MAMNDEETVA LTAGGHTVGK CHGNGKAQDL GPEPEGEELE AQGLGWLNKK
310 320 330 340 350
GPGTGANAVT SGLEGAWTTH PTQWDNGYFH LLLNYDWELK KSPAGASQWE
360 370 380 390 400
PINIKEEDKV VSVGDPNRKF NPIMTDADMA MKMDPEYRKI SEKFYQDPAY
410 420 430 440 450
FSEVFARAWF KLTHRDLGPK SRYLGPEVPN EDLLWQDPIP SVDYRLDASE
460 470 480 490 500
IVELKAKLLA SGLSVSDLVA TAWDSARTFR GSDFRGGANG ARIRLAPQKD
510 520 530 540 550
WQANEPERLQ KVLKVLIELQ ASLSKKVSIA DLIVLGGAAA IEKAAHAAGV
560 570 580 590 600
KITVPFIPGR GDATQEMTDV ESFAVLEPLH DAYRNWQKKD YVVQPEEMML
610 620 630 640 650
DRTQLMGLTA HEMTVLIGGM RVLGTNYGGT RHGVFTDKVG VLTNDFFVNL
660 670 680 690 700
TDMAYNWKPA GSNLYEIVER KTGAVKWTAT RVDLVFGSNS ILRSYAEVYA
710 720
QDDAKEKFVH DFVAAWTKVM NADRFDLA
Length:728
Mass (Da):81,113
Last modified:December 12, 2006 - v1
Checksum:i285760B6474BB5B4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000469 Genomic DNA. Translation: ABK46549.1.
RefSeqiWP_011715540.1. NC_008577.1.

Genome annotation databases

EnsemblBacteriaiABK46549; ABK46549; Shewana3_0306.
KEGGishn:Shewana3_0306.
PATRICi23568178. VBISheSp134792_0553.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000469 Genomic DNA. Translation: ABK46549.1.
RefSeqiWP_011715540.1. NC_008577.1.

3D structure databases

ProteinModelPortaliA0KRY0.
SMRiA0KRY0. Positions 27-727.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi94122.Shewana3_0306.

Protein family/group databases

PeroxiBasei3616. SHspCP01_ANA-3.

Proteomic databases

PRIDEiA0KRY0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABK46549; ABK46549; Shewana3_0306.
KEGGishn:Shewana3_0306.
PATRICi23568178. VBISheSp134792_0553.

Phylogenomic databases

eggNOGiENOG4105C1X. Bacteria.
COG0376. LUCA.
HOGENOMiHOG000218110.
KOiK03782.
OMAiQPEEMML.
OrthoDBiPOG091H05R1.

Enzyme and pathway databases

BioCyciSSP94122:GJ9K-323-MONOMER.

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.
[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. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiKATG1_SHESA
AccessioniPrimary (citable) accession number: A0KRY0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: December 12, 2006
Last modified: September 7, 2016
This is version 65 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.