KATG_BORA1
ID KATG_BORA1 Reviewed; 748 AA.
AC Q2KTI4;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 89.
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};
GN Name=katG {ECO:0000255|HAMAP-Rule:MF_01961}; OrderedLocusNames=BAV3417;
OS Bordetella avium (strain 197N).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=360910;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=197N;
RX PubMed=16885469; DOI=10.1128/jb.01927-05;
RA Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA Parkhill J., Temple L.M.;
RT "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT extensive diversity in surface structures associated with host
RT interaction.";
RL J. Bacteriol. 188:6002-6015(2006).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAJ51027.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AM167904; CAJ51027.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_039051346.1; NC_010645.1.
DR AlphaFoldDB; Q2KTI4; -.
DR SMR; Q2KTI4; -.
DR STRING; 360910.BAV3417; -.
DR PeroxiBase; 3418; BavCP01.
DR EnsemblBacteria; CAJ51027; CAJ51027; BAV3417.
DR GeneID; 41395249; -.
DR KEGG; bav:BAV3417; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_4; -.
DR OrthoDB; 49441at2; -.
DR Proteomes; UP000001977; 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.
FT CHAIN 1..748
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354726"
FT REGION 201..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..220
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 92
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 277
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 88
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 91..236
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 262)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 236..262
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 91)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 748 AA; 82411 MW; 13D42B441D82CDB5 CRC64;
MSNEAKCPFN HTAGSGTTNQ DWWPKRLRLE LLSQHSAKTN PLDPDFDYAK AFNSLDLAAV
KQDLAKLMTD SQDWWPADFG HYGPLFIRMA WHSAGTYRVG DGRGGAGRGQ QRFAPLNSWP
DNVSLDKARR LLWPIKKKYG NKISWADLFI LTGNVALETM GFKTFGFGGG REDTWEPDQD
VYWGDEKTWL GGDLRYGKNE AQPVADKAGH GKEHGRTDGG RNLENPLAAV QMGLIYVNPE
GPDGNPDPQA SAHDIRETFA RMAMNDEETV ALIAGGHTFG KTHGAGPADN VGPEPEAAEL
ENQGLGWKNS FGTGKGSDTI TSGLEVTWTS TPTKWSNNFF WNLFGYEWEL TKSPAGAHQW
IPKHGAGAGS VPDAHDPSKR HVPSMLTSDI ALRVDPAYEK IARRFFENPD EFADAFARAW
FKLTHRDMGP RVRYLGPEVP AEDLIWQDPI PKVNHPLVDD QDVAALKQKV LASGLSVSEL
VSTAWASAST FRGSDKRGGA NGARIRLAPQ KDWAVNQPEQ LAKVLKVLEG IQADFNGKQS
GGKKVSLADL IVLAGCAAIE QAAGQAGHKV TVPFTAGRMD ASQEQTDVAS FAPLEPVHDG
FRNFLKSRYD VPAEHLLIDR AQLLTLTAPE MTVLIGGLRV LDVHTDKEKH GVFTDRPGVL
TNDFFRNLID MGTEWKPSSP ARESFTGHDR KTGKQKWTAS RVDLVFGSNS QLRALSEVYA
SDDAQDKFVR DFIAAWTKVM NLDRFDLK
