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Protein

Catalase-peroxidase

Gene

katG

Organism
Xylella fastidiosa (strain 9a5c)
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
Sitei122 – 1221Transition state stabilizerUniRule annotation
Active sitei126 – 1261Proton acceptorUniRule annotation
Metal bindingi313 – 3131Iron (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

Protein family/group databases

PeroxiBasei2320. XfCP01_9a5c.

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:XF_2232
OrganismiXylella fastidiosa (strain 9a5c)
Taxonomic identifieri160492 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXylella
Proteomesi
  • UP000000812 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020UniRule annotationAdd
BLAST
Chaini21 – 781761Catalase-peroxidasePRO_0000354959Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki125 ↔ 272Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-298)UniRule annotation
Cross-linki272 ↔ 298Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-125)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

PRIDEiQ9PBB2.

Interactioni

Subunit structurei

Homodimer or homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi160492.XF2232.

Structurei

3D structure databases

ProteinModelPortaliQ9PBB2.
SMRiQ9PBB2. Positions 50-780.
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.
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.

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

Q9PBB2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLYIYYLFKS LFFHTLFVFS IYKDCPYMRA SSPETTSAVK CPFNKTAVEG
60 70 80 90 100
THNKDWWPNQ LRVDLLHQHS NKSNPLGETF DYAKEFQKLD YAALKRDLHA
110 120 130 140 150
LMTDSQDWWP ADFGHYGGLF IRMAWHSAGT YRIGDGRGGA GRGQQRFAPL
160 170 180 190 200
NSWPDNVSLD KARRLLWPIK KKYGQQISWA DLIVLSGNVA LESMGFKTFG
210 220 230 240 250
FAGGRVDTWE PDQDVYWGRE TTWLGGDVRY GAVSEGVHHP DEHRGAKEKA
260 270 280 290 300
AKNSDSRVLE NPLAAVQMGL IYVNPEGPDG RPDPLASARD IRETFARMAM
310 320 330 340 350
NDEETVALIA GGHTFGKTHG AAPADNVGPE PEAGELEQQG LGWHNRFGSG
360 370 380 390 400
KAGDTITSGL EVTWTKTPTQ WSNDFFEHLF GYEWELTKSP AGAYQWVAKN
410 420 430 440 450
AAATIPHAHD PSKKLLPMML TSDLALRFDP IYEKISRHFH AHPDQFADVF
460 470 480 490 500
ARAWFKLMHR DMGPRVRYLG PEVPVEELIW QDPVPKVSHV LVDAQDLLAL
510 520 530 540 550
KQKISASGLG ISQLVSTAWA SASTFRGSDK RGGANGGRLC LAPQSQWEVN
560 570 580 590 600
QPQQLSVVLE TLRRVQTEFN AQAGDKRISL ADLIVLAGGV GVEQAAKRAG
610 620 630 640 650
IVVEVPFVPG RTDALQEQTD VSSFAPLEPF ADGFRNYVKG DEVVPSEHLL
660 670 680 690 700
IDRAQLLTLT APEMTVLIGG LRVLGANVGG VKHGVFTDRL GTLSNDFFIN
710 720 730 740 750
LLDMGTEWAP VSKERHVFEG RDRRTGVLKW TGTRVDLVFG SNALLRALAE
760 770 780
FYAAVDAQEK FVRDFVAAWS KVMHLDRFDL V
Length:781
Mass (Da):86,891
Last modified:October 1, 2000 - v1
Checksum:iFD1E6A97299D6605
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE003849 Genomic DNA. Translation: AAF85031.1.
PIRiF82584.

Genome annotation databases

EnsemblBacteriaiAAF85031; AAF85031; XF_2232.
KEGGixfa:XF2232.
PATRICi24134712. VBIXylFas578_2376.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE003849 Genomic DNA. Translation: AAF85031.1.
PIRiF82584.

3D structure databases

ProteinModelPortaliQ9PBB2.
SMRiQ9PBB2. Positions 50-780.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi160492.XF2232.

Protein family/group databases

PeroxiBasei2320. XfCP01_9a5c.

Proteomic databases

PRIDEiQ9PBB2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAF85031; AAF85031; XF_2232.
KEGGixfa:XF2232.
PATRICi24134712. VBIXylFas578_2376.

Phylogenomic databases

eggNOGiENOG4105C1X. Bacteria.
COG0376. LUCA.
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]
ProtoNetiSearch...

Publicationsi

  1. "The genome sequence of the plant pathogen Xylella fastidiosa."
    Simpson A.J.G., Reinach F.C., Arruda P., Abreu F.A., Acencio M., Alvarenga R., Alves L.M.C., Araya J.E., Baia G.S., Baptista C.S., Barros M.H., Bonaccorsi E.D., Bordin S., Bove J.M., Briones M.R.S., Bueno M.R.P., Camargo A.A., Camargo L.E.A.
    , Carraro D.M., Carrer H., Colauto N.B., Colombo C., Costa F.F., Costa M.C.R., Costa-Neto C.M., Coutinho L.L., Cristofani M., Dias-Neto E., Docena C., El-Dorry H., Facincani A.P., Ferreira A.J.S., Ferreira V.C.A., Ferro J.A., Fraga J.S., Franca S.C., Franco M.C., Frohme M., Furlan L.R., Garnier M., Goldman G.H., Goldman M.H.S., Gomes S.L., Gruber A., Ho P.L., Hoheisel J.D., Junqueira M.L., Kemper E.L., Kitajima J.P., Krieger J.E., Kuramae E.E., Laigret F., Lambais M.R., Leite L.C.C., Lemos E.G.M., Lemos M.V.F., Lopes S.A., Lopes C.R., Machado J.A., Machado M.A., Madeira A.M.B.N., Madeira H.M.F., Marino C.L., Marques M.V., Martins E.A.L., Martins E.M.F., Matsukuma A.Y., Menck C.F.M., Miracca E.C., Miyaki C.Y., Monteiro-Vitorello C.B., Moon D.H., Nagai M.A., Nascimento A.L.T.O., Netto L.E.S., Nhani A. Jr., Nobrega F.G., Nunes L.R., Oliveira M.A., de Oliveira M.C., de Oliveira R.C., Palmieri D.A., Paris A., Peixoto B.R., Pereira G.A.G., Pereira H.A. Jr., Pesquero J.B., Quaggio R.B., Roberto P.G., Rodrigues V., de Rosa A.J.M., de Rosa V.E. Jr., de Sa R.G., Santelli R.V., Sawasaki H.E., da Silva A.C.R., da Silva A.M., da Silva F.R., Silva W.A. Jr., da Silveira J.F., Silvestri M.L.Z., Siqueira W.J., de Souza A.A., de Souza A.P., Terenzi M.F., Truffi D., Tsai S.M., Tsuhako M.H., Vallada H., Van Sluys M.A., Verjovski-Almeida S., Vettore A.L., Zago M.A., Zatz M., Meidanis J., Setubal J.C.
    Nature 406:151-159(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 9a5c.

Entry informationi

Entry nameiKATG_XYLFA
AccessioniPrimary (citable) accession number: Q9PBB2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: October 1, 2000
Last modified: November 11, 2015
This is version 92 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.