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Protein

Catalase-peroxidase

Gene

katG

Organism
Novosphingobium aromaticivorans (strain DSM 12444 / F199)
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
Sitei113 – 1131Transition state stabilizerUniRule annotation
Active sitei117 – 1171Proton acceptorUniRule annotation
Metal bindingi279 – 2791Iron (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

BioCyciNARO279238:GHBU-2975-MONOMER.

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:Saro_2909
OrganismiNovosphingobium aromaticivorans (strain DSM 12444 / F199)
Taxonomic identifieri279238 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeNovosphingobium
Proteomesi
  • UP000009134 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727UniRule annotationAdd
BLAST
Chaini28 – 747720Catalase-peroxidasePRO_5000106493Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki116 ↔ 238Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-264)UniRule annotation
Cross-linki238 ↔ 264Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-116)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

PRIDEiQ2G479.

Interactioni

Subunit structurei

Homodimer or homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi279238.Saro_2909.

Structurei

3D structure databases

ProteinModelPortaliQ2G479.
SMRiQ2G479. Positions 43-745.
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.
OMAiMSTRWEK.
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.

Q2G479-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRKFSVSKVA LLAATMAPAL LPAAARAEGT AAPAATAPAT PMSNRDWWPN
60 70 80 90 100
RLDLSPLRQH GVESNPMGGK FNYAEEFKTL DLAAVKKDIE ALMTTSQDWW
110 120 130 140 150
PADYGHYGPF FIRMAWHSAG TYRTADGRGG AGGGQQRFEP LNSWPDNVNL
160 170 180 190 200
DKARRLLWPI KQKYGRKISW ADLMVLTGNV ALESMGFKTF GFAGGRADDW
210 220 230 240 250
EADQVFWGPE NKWLADQRYH GDRKLQNPLA AVQMGLIYVN PEGPNGNPDP
260 270 280 290 300
LLAAKDIRET FGRMAMNDEE TVALIAGGHT FGKAHGARKP EGCVGVDPAA
310 320 330 340 350
GAVEDQGLGW NNKCGKGNAE DTVSSGLEGA WTANPIAWTT QYLDNLYAFE
360 370 380 390 400
WVQTRSPAGA IQWVPKEDAT FVPDAHVKDK LHKPIMFTTD LALKTDPAYR
410 420 430 440 450
KITTKFRQNP DAFADAFARA WFKLTHRDMG PRWRYLGAMV PAEELIWQDP
460 470 480 490 500
VPKATYAMID AADVSALKGR ILATGLTGPE LVRAAWASAA SFRGTDMRGG
510 520 530 540 550
TDGGRIRLAP QKDWAANNPA ELARVLKALE GVATEFNRAA KDGKKVSVAN
560 570 580 590 600
LVVLGGNAAI EQAAAKAGVT VEVPFTPGRT DASQAQTDVA SFEFLKPAAD
610 620 630 640 650
GFRNYYDASA NRLSPSEMLV ERANLLTLSV PEMTVLVGGL RALDANAGGA
660 670 680 690 700
RHGVFTDRPG TLSNDFFVNL LGMETKWQKA ATDGVYEGLD RKTGKTRWTA
710 720 730 740
TPVDLVFGSN SELRAVSEVY GSADANAKFV NDFVAAWTKV MNLGRPS
Length:747
Mass (Da):81,101
Last modified:March 21, 2006 - v1
Checksum:i7E5015BBCC7F343C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000248 Genomic DNA. Translation: ABD27344.1.
RefSeqiWP_011446548.1. NC_007794.1.

Genome annotation databases

EnsemblBacteriaiABD27344; ABD27344; Saro_2909.
KEGGinar:Saro_2909.
PATRICi22788638. VBINovAro50627_2976.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000248 Genomic DNA. Translation: ABD27344.1.
RefSeqiWP_011446548.1. NC_007794.1.

3D structure databases

ProteinModelPortaliQ2G479.
SMRiQ2G479. Positions 43-745.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi279238.Saro_2909.

Proteomic databases

PRIDEiQ2G479.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABD27344; ABD27344; Saro_2909.
KEGGinar:Saro_2909.
PATRICi22788638. VBINovAro50627_2976.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciNARO279238:GHBU-2975-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: DSM 12444 / F199.

Entry informationi

Entry nameiKATG_NOVAD
AccessioniPrimary (citable) accession number: Q2G479
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: March 21, 2006
Last modified: December 9, 2015
This is version 75 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.