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Protein

Catalase-peroxidase

Gene

katG

Organism
Nitrobacter hamburgensis (strain X14 / DSM 10229)
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 bindingi258 – 2581Iron (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

BioCyciNHAM323097:GHP7-37-MONOMER.

Protein family/group databases

PeroxiBasei3630. NhCP01_X14.

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:Nham_0037
OrganismiNitrobacter hamburgensis (strain X14 / DSM 10229)
Taxonomic identifieri323097 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeNitrobacter
Proteomesi
  • UP000001953 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 729729Catalase-peroxidasePRO_0000354849Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki95 ↔ 217Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-243)UniRule annotation
Cross-linki217 ↔ 243Tryptophyl-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

PRIDEiQ1QS58.

Interactioni

Subunit structurei

Homodimer or homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi323097.Nham_0037.

Structurei

3D structure databases

ProteinModelPortaliQ1QS58.
SMRiQ1QS58. Positions 24-727.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C1X. Bacteria.
COG0376. LUCA.
HOGENOMiHOG000218110.
KOiK03782.
OMAiVVWTPTP.
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.

Q1QS58-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDAKTNDKSA GKCPFTSGRS HRIRDWWPGQ LDVQVLHHNS NLSDPMDEDF
60 70 80 90 100
DYAREFESLD LNAVIKDLTA LMTDSQDWWP ADFGHYGGLM IRLAWHSAGT
110 120 130 140 150
YRITDGRGGA GAGQQRFAPL NSWPDNVLLD RGRRLLWPIK QKYGRKISWA
160 170 180 190 200
DLLVLSGNVA LESMGFKTFG FAGGRADVWE PEELYWGPEG TWLGDERYSG
210 220 230 240 250
ERQLAEPLAA VQMGLIYVNP EGPNGKPDPI AAATDIRETF FRMAMNDEET
260 270 280 290 300
VALIAGGHTF GKTHGAGDAS LVGPAPESAP IEDQGLGWNS KFGTGKGGDS
310 320 330 340 350
IGSGLEVTWT QTPTTWDNNF FDTLFKYEWE LTKSPAGAYQ WQAKDAPAIT
360 370 380 390 400
PDAHDTSKKH VPTMLTTDLS LRFDPAYGKI SKHFHENPDQ FADAFARAWY
410 420 430 440 450
KLTHRDMGPR ERYLGPLVPK ETLIWQDPIP AVDHALVDDK DIAELKAKVL
460 470 480 490 500
ASGLTVPQLV STAWASASTF RGSDKRGGAN GARIRLAPQK DWEVNQPAQL
510 520 530 540 550
KTVLARLEAI QSEFNGAQTG GKKVSLADLI VLAGCFAVEK AANDVGIDLK
560 570 580 590 600
VPFTPGRMDA SQDQTDVDSF APLEPRADGF RNYIGSRHQF MTPEEALVDR
610 620 630 640 650
AQLLNLTGPE MTVLVGGLRV LGANAADSRH GVFTKQPGTL TNDFFANLLT
660 670 680 690 700
MDTVWQPVAG QDDVYEGRDR KTNAVQWTGT RVDLIFGSHS QLRAFAEVYA
710 720
CTDAKEKFAR DFVAAWTKVM NADRFDLHR
Length:729
Mass (Da):80,451
Last modified:May 16, 2006 - v1
Checksum:iCA4BCACA39F65C62
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000319 Genomic DNA. Translation: ABE60939.1.
RefSeqiWP_011508646.1. NC_007964.1.

Genome annotation databases

EnsemblBacteriaiABE60939; ABE60939; Nham_0037.
KEGGinha:Nham_0037.
PATRICi22687379. VBINitHam61822_0733.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000319 Genomic DNA. Translation: ABE60939.1.
RefSeqiWP_011508646.1. NC_007964.1.

3D structure databases

ProteinModelPortaliQ1QS58.
SMRiQ1QS58. Positions 24-727.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi323097.Nham_0037.

Protein family/group databases

PeroxiBasei3630. NhCP01_X14.

Proteomic databases

PRIDEiQ1QS58.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABE60939; ABE60939; Nham_0037.
KEGGinha:Nham_0037.
PATRICi22687379. VBINitHam61822_0733.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciNHAM323097:GHP7-37-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: X14 / DSM 10229.

Entry informationi

Entry nameiKATG_NITHX
AccessioniPrimary (citable) accession number: Q1QS58
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: May 16, 2006
Last modified: December 9, 2015
This is version 67 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.