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Protein

Catalase-peroxidase

Gene

katG

Organism
Xanthomonas axonopodis pv. citri (strain 306)
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
Sitei89 – 891Transition state stabilizerUniRule annotation
Active sitei93 – 931Proton 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

BioCyciXAXO190486:GH55-1301-MONOMER.

Protein family/group databases

PeroxiBasei2289. XacCP01.

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:XAC1301
OrganismiXanthomonas axonopodis pv. citri (strain 306)
Taxonomic identifieri190486 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas
Proteomesi
  • UP000000576 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 748748Catalase-peroxidasePRO_0000354954Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki92 ↔ 238Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-264)UniRule annotation
Cross-linki238 ↔ 264Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-92)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

PRIDEiQ8PMX4.

Interactioni

Subunit structurei

Homodimer or homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi190486.XAC1301.

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.

Q8PMX4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTEAKCPFN HAVVGTGTTN RDWWPKQLRV DLLSQHSSKS NPLDPSFNYA
60 70 80 90 100
DAFKHLDLQA LKQDLHALMT DSQDWWPADF GHYGPLFVRM AWHSAGTYRI
110 120 130 140 150
GDGRGGGGRG QQRFAPLNSW PDNVSLDKAR RLLWPIKQKY GQAISWADLM
160 170 180 190 200
ILTGNVALES MGLKTFGFAG GREDTWEPDQ DLYWGRETKW LGGDERYSRG
210 220 230 240 250
SPGVDEAHGV LVKDDDSQVP HTRDLENPLA AVQMGLIYVN PEGPDGNPDP
260 270 280 290 300
IASARDIRDT FARMAMNDEE TVALIAGGHT FGKTHGAGPA DYVGAEPEAG
310 320 330 340 350
ELESQGFGWH NRYGSGKGAD TITSGLEVTW TTTPAQWSND YFDHLFGFEW
360 370 380 390 400
ELSKSPAGAH QWVAKNADAI IPDAHDASRK HRPTMLTTDL ALRFDPAYEA
410 420 430 440 450
ISRRFQQHPE QFADAFARAW FKLTHRDMGP RARYLGADVP AEELVWQDPV
460 470 480 490 500
PAVDHALVDA QDAAALKQTI LASGLSVAHL VSTAWASAST FRGSDKRGGA
510 520 530 540 550
NGARIRLAPQ KEWQANQPEQ LAKVLATLER IQADFNAAQS GGKKISLADL
560 570 580 590 600
VVLAGNAAVE HAAQAAGHQV TVPFAPGRTD ASQEQTDVES FAVLEPVADG
610 620 630 640 650
FRNFAKRRYA VPAEALLIDK AQLLTLTAPE LTVLVGGLRV LGANVGDSKH
660 670 680 690 700
GVFTSRPGVL SNDFFANLLD MRTEWKATSE AKEVFEGRDR STGELRWTGT
710 720 730 740
RVDLVFGSNS ILRAVAEVYA SADAQEKFVH DFVAAWTKVM QLDRFDLA
Length:748
Mass (Da):81,991
Last modified:November 25, 2008 - v2
Checksum:iE31B0AF1758D8D27
GO

Sequence cautioni

The sequence AAM36172.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE008923 Genomic DNA. Translation: AAM36172.1. Different initiation.
RefSeqiWP_011050828.1. NC_003919.1.

Genome annotation databases

EnsemblBacteriaiAAM36172; AAM36172; XAC1301.
GeneIDi14852060.
KEGGixac:XAC1301.
PATRICi24054587. VBIXanAxo33670_1374.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE008923 Genomic DNA. Translation: AAM36172.1. Different initiation.
RefSeqiWP_011050828.1. NC_003919.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi190486.XAC1301.

Protein family/group databases

PeroxiBasei2289. XacCP01.

Proteomic databases

PRIDEiQ8PMX4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAM36172; AAM36172; XAC1301.
GeneIDi14852060.
KEGGixac:XAC1301.
PATRICi24054587. VBIXanAxo33670_1374.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciXAXO190486:GH55-1301-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. "Comparison of the genomes of two Xanthomonas pathogens with differing host specificities."
    da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., Ciapina L.P.
    , Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.
    Nature 417:459-463(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 306.

Entry informationi

Entry nameiKATG_XANAC
AccessioniPrimary (citable) accession number: Q8PMX4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: November 25, 2008
Last modified: November 11, 2015
This is version 88 of the entry and version 2 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.