KATG_XYLFA
ID KATG_XYLFA Reviewed; 781 AA.
AC Q9PBB2;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Catalase-peroxidase {ECO:0000255|HAMAP-Rule:MF_01961};
DE Short=CP {ECO:0000255|HAMAP-Rule:MF_01961};
DE EC=1.11.1.21 {ECO:0000255|HAMAP-Rule:MF_01961};
DE AltName: Full=Peroxidase/catalase {ECO:0000255|HAMAP-Rule:MF_01961};
DE Flags: Precursor;
GN Name=katG {ECO:0000255|HAMAP-Rule:MF_01961}; OrderedLocusNames=XF_2232;
OS Xylella fastidiosa (strain 9a5c).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xylella.
OX NCBI_TaxID=160492;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9a5c;
RX PubMed=10910347; DOI=10.1038/35018003;
RA Simpson A.J.G., Reinach F.C., Arruda P., Abreu F.A., Acencio M.,
RA Alvarenga R., Alves L.M.C., Araya J.E., Baia G.S., Baptista C.S.,
RA Barros M.H., Bonaccorsi E.D., Bordin S., Bove J.M., Briones M.R.S.,
RA Bueno M.R.P., Camargo A.A., Camargo L.E.A., Carraro D.M., Carrer H.,
RA Colauto N.B., Colombo C., Costa F.F., Costa M.C.R., Costa-Neto C.M.,
RA Coutinho L.L., Cristofani M., Dias-Neto E., Docena C., El-Dorry H.,
RA Facincani A.P., Ferreira A.J.S., Ferreira V.C.A., Ferro J.A., Fraga J.S.,
RA Franca S.C., Franco M.C., Frohme M., Furlan L.R., Garnier M., Goldman G.H.,
RA Goldman M.H.S., Gomes S.L., Gruber A., Ho P.L., Hoheisel J.D.,
RA Junqueira M.L., Kemper E.L., Kitajima J.P., Krieger J.E., Kuramae E.E.,
RA Laigret F., Lambais M.R., Leite L.C.C., Lemos E.G.M., Lemos M.V.F.,
RA Lopes S.A., Lopes C.R., Machado J.A., Machado M.A., Madeira A.M.B.N.,
RA Madeira H.M.F., Marino C.L., Marques M.V., Martins E.A.L., Martins E.M.F.,
RA Matsukuma A.Y., Menck C.F.M., Miracca E.C., Miyaki C.Y.,
RA Monteiro-Vitorello C.B., Moon D.H., Nagai M.A., Nascimento A.L.T.O.,
RA Netto L.E.S., Nhani A. Jr., Nobrega F.G., Nunes L.R., Oliveira M.A.,
RA de Oliveira M.C., de Oliveira R.C., Palmieri D.A., Paris A., Peixoto B.R.,
RA Pereira G.A.G., Pereira H.A. Jr., Pesquero J.B., Quaggio R.B.,
RA Roberto P.G., Rodrigues V., de Rosa A.J.M., de Rosa V.E. Jr., de Sa R.G.,
RA Santelli R.V., Sawasaki H.E., da Silva A.C.R., da Silva A.M.,
RA da Silva F.R., Silva W.A. Jr., da Silveira J.F., Silvestri M.L.Z.,
RA Siqueira W.J., de Souza A.A., de Souza A.P., Terenzi M.F., Truffi D.,
RA Tsai S.M., Tsuhako M.H., Vallada H., Van Sluys M.A., Verjovski-Almeida S.,
RA Vettore A.L., Zago M.A., Zatz M., Meidanis J., Setubal J.C.;
RT "The genome sequence of the plant pathogen Xylella fastidiosa.";
RL Nature 406:151-159(2000).
CC -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC peroxidase activity. {ECO:0000255|HAMAP-Rule:MF_01961}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + H2O2 = A + 2 H2O; Xref=Rhea:RHEA:30275,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:17499; EC=1.11.1.21; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01961};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.21;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01961};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01961};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
CC {ECO:0000255|HAMAP-Rule:MF_01961};
CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000255|HAMAP-Rule:MF_01961}.
CC -!- PTM: Formation of the three residue Trp-Tyr-Met cross-link is important
CC for the catalase, but not the peroxidase activity of the enzyme.
CC {ECO:0000255|HAMAP-Rule:MF_01961}.
CC -!- SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01961}.
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DR EMBL; AE003849; AAF85031.1; -; Genomic_DNA.
DR PIR; F82584; F82584.
DR AlphaFoldDB; Q9PBB2; -.
DR SMR; Q9PBB2; -.
DR STRING; 160492.XF_2232; -.
DR PeroxiBase; 2320; XfCP01_9a5c.
DR EnsemblBacteria; AAF85031; AAF85031; XF_2232.
DR KEGG; xfa:XF_2232; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_6; -.
DR OMA; MILAGNC; -.
DR Proteomes; UP000000812; Chromosome.
DR GO; GO:0004096; F:catalase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR HAMAP; MF_01961; Catal_peroxid; 1.
DR InterPro; IPR000763; Catalase_peroxidase.
DR InterPro; IPR002016; Haem_peroxidase.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR019794; Peroxidases_AS.
DR InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR PANTHER; PTHR30555; PTHR30555; 1.
DR Pfam; PF00141; peroxidase; 2.
DR PRINTS; PR00460; BPEROXIDASE.
DR PRINTS; PR00458; PEROXIDASE.
DR SUPFAM; SSF48113; SSF48113; 2.
DR TIGRFAMs; TIGR00198; cat_per_HPI; 1.
DR PROSITE; PS00435; PEROXIDASE_1; 1.
DR PROSITE; PS00436; PEROXIDASE_2; 1.
DR PROSITE; PS50873; PEROXIDASE_4; 1.
PE 3: Inferred from homology;
KW Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW Reference proteome; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CHAIN 21..781
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354959"
FT REGION 237..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 126
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 313
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT SITE 122
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 125..272
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 298)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 272..298
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 125)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 781 AA; 86891 MW; FD1E6A97299D6605 CRC64;
MLYIYYLFKS LFFHTLFVFS IYKDCPYMRA SSPETTSAVK CPFNKTAVEG THNKDWWPNQ
LRVDLLHQHS NKSNPLGETF DYAKEFQKLD YAALKRDLHA LMTDSQDWWP ADFGHYGGLF
IRMAWHSAGT YRIGDGRGGA GRGQQRFAPL NSWPDNVSLD KARRLLWPIK KKYGQQISWA
DLIVLSGNVA LESMGFKTFG FAGGRVDTWE PDQDVYWGRE TTWLGGDVRY GAVSEGVHHP
DEHRGAKEKA AKNSDSRVLE NPLAAVQMGL IYVNPEGPDG RPDPLASARD IRETFARMAM
NDEETVALIA GGHTFGKTHG AAPADNVGPE PEAGELEQQG LGWHNRFGSG KAGDTITSGL
EVTWTKTPTQ WSNDFFEHLF GYEWELTKSP AGAYQWVAKN AAATIPHAHD PSKKLLPMML
TSDLALRFDP IYEKISRHFH AHPDQFADVF ARAWFKLMHR DMGPRVRYLG PEVPVEELIW
QDPVPKVSHV LVDAQDLLAL KQKISASGLG ISQLVSTAWA SASTFRGSDK RGGANGGRLC
LAPQSQWEVN QPQQLSVVLE TLRRVQTEFN AQAGDKRISL ADLIVLAGGV GVEQAAKRAG
IVVEVPFVPG RTDALQEQTD VSSFAPLEPF ADGFRNYVKG DEVVPSEHLL IDRAQLLTLT
APEMTVLIGG LRVLGANVGG VKHGVFTDRL GTLSNDFFIN LLDMGTEWAP VSKERHVFEG
RDRRTGVLKW TGTRVDLVFG SNALLRALAE FYAAVDAQEK FVRDFVAAWS KVMHLDRFDL
V
