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Protein

Catalase-peroxidase

Gene

katG

Organism
Geobacillus thermodenitrificans (strain NG80-2)
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
Sitei97 – 971Transition state stabilizerUniRule annotation
Active sitei101 – 1011Proton acceptorUniRule annotation
Metal bindingi264 – 2641Iron (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

BioCyciGTHE420246:GIXT-1634-MONOMER.

Protein family/group databases

PeroxiBasei7319. GthCP01.

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:GTNG_1561
OrganismiGeobacillus thermodenitrificans (strain NG80-2)
Taxonomic identifieri420246 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus
Proteomesi
  • UP000001578 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 735735Catalase-peroxidasePRO_0000354800Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki100 ↔ 223Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-249)UniRule annotation
Cross-linki223 ↔ 249Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-100)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

PRIDEiA4INM5.

Interactioni

Subunit structurei

Homodimer or homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi420246.GTNG_1561.

Structurei

3D structure databases

ProteinModelPortaliA4INM5.
SMRiA4INM5. Positions 24-725.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

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.

A4INM5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MENQNRQNAS QCPFHGSITN QSSNRTTNKD WWPNQLNLSI LHQHDRKTNP
60 70 80 90 100
HDEEFDYAAE FQKLDYWALK EDLRKLMTES QDWWPADYGH YGPLFIRMAW
110 120 130 140 150
HSAGTYRIGD GRGGASTGTQ RFAPLNSWPD NANLDKARRL LWPIKKKYGN
160 170 180 190 200
KISWADLFIL AGNVAIESMG GKTIGFGGGR VDVWHPEEDI YWGAEKEWLA
210 220 230 240 250
SERHSDDGEL EHPLAASVMG LIYVNPEGPD GKPDPKAAAR DIRETFRRMG
260 270 280 290 300
MNDEETVALI AGGHTFGKAH GAGPATHVGP EPEAAPIEAQ GLGWMSSYGK
310 320 330 340 350
GKGSDTITSG IEGAWTPTPT QWDMSYFDML FGYDWWLTKS PAGAWQWMAV
360 370 380 390 400
DPNEKDLAPD AEDPSKKVPT MMMTTDLALR FDPEYEKIAR RFHQNPEEFA
410 420 430 440 450
EAFARAWFKL THRDMGPKTR YLGPEVPKED FIWQDPIPEV NYELTEAEIE
460 470 480 490 500
EIKAKILNSG LTVSELVKTA WASASTFRHS DKRGGANGAR IRLAPQNEWE
510 520 530 540 550
VNEPERLAKV LSIYEDIQRE LPKKVSIADL IVLGGSAAVE KAARDAGFDV
560 570 580 590 600
KVPFSPGRGD ATQEQTDVES FAVLEPFADG FRNYQKQEYS VPPEELLVDK
610 620 630 640 650
AQLLGLTAPE MTVLVGGLRV LGANYRDLPH GVFTDRIGVL TNDFFVNLLD
660 670 680 690 700
MDYEWVPTDS GIYEIRNRKT GEVRWTATRV DLIFGSNSIL RSYAEFYAQD
710 720 730
DNQEKFVRDF INAWVKVMNA DRFDLVKKAR ESVTA
Length:735
Mass (Da):82,898
Last modified:May 1, 2007 - v1
Checksum:i6634DA0C89D81145
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000557 Genomic DNA. Translation: ABO66929.1.
RefSeqiWP_008879140.1. NC_009328.1.

Genome annotation databases

EnsemblBacteriaiABO66929; ABO66929; GTNG_1561.
KEGGigtn:GTNG_1561.
PATRICi21979555. VBIGeoThe136879_1655.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000557 Genomic DNA. Translation: ABO66929.1.
RefSeqiWP_008879140.1. NC_009328.1.

3D structure databases

ProteinModelPortaliA4INM5.
SMRiA4INM5. Positions 24-725.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi420246.GTNG_1561.

Protein family/group databases

PeroxiBasei7319. GthCP01.

Proteomic databases

PRIDEiA4INM5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABO66929; ABO66929; GTNG_1561.
KEGGigtn:GTNG_1561.
PATRICi21979555. VBIGeoThe136879_1655.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciGTHE420246:GIXT-1634-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. "Genome and proteome of long-chain alkane degrading Geobacillus thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir."
    Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X., Han W., Peng X., Liu R., Wang L.
    Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: NG80-2.

Entry informationi

Entry nameiKATG_GEOTN
AccessioniPrimary (citable) accession number: A4INM5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: May 1, 2007
Last modified: December 9, 2015
This is version 63 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.