ID   KATG_HERSS              Reviewed;         748 AA.
AC   D8INT8;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Catalase-peroxidase;
DE            Short=CP;
DE            EC=1.11.1.21;
DE   AltName: Full=Peroxidase/catalase;
GN   Name=katG; OrderedLocusNames=Hsero_1242;
OS   Herbaspirillum seropedicae (strain SmR1).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Herbaspirillum.
OX   NCBI_TaxID=757424;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SmR1;
RA   Pedrosa F.O., Monteiro R.A., Wassem R., Cruz L.M., Ayub R.A., Colauto N.B.,
RA   Fernandez M.A., Fungaro M.H.P., Grisard E.C., Hungria M., Madeira H.M.F.,
RA   Nodari R.O., Osaku C.A., Petzl-Erler M.L., Terenzi H., Vieira L.G.E.,
RA   Almeida M.I.M., Alves L.R., Arantes O.M.N., Balsanelli E., Barcellos F.G.,
RA   Baura V.A., Binde D.R., Campo R.J., Chubatsu L.S., Chueire L.M.O.,
RA   Ciferri R.R., Correa L.C., da Conceicao Silva J.L., Dabul A.N.G.,
RA   Dambros B.P., Faoro H., Favetti A., Friedermann G., Furlaneto M.C.,
RA   Gasques L.S., Gimenes C.C.T., Gioppo N.M.R., Glienke-Blanco C., Godoy L.P.,
RA   Guerra M.P., Karp S., Kava-Cordeiro V., Margarido V.P., Mathioni S.M.,
RA   Menck-Soares M.A., Murace N.K., Nicolas M.F., Oliveira C.E.C.,
RA   Pagnan N.A.B., Pamphile J.A., Patussi E.V., Pereira L.F.P.,
RA   Pereira-Ferrari L., Pinto F.G.S., Precoma C., Prioli A.J., Prioli S.M.A.P.,
RA   Raittz R.T., Ramos H.J.O., Ribeiro E.M.S.F., Rigo L.U., Rocha C.L.M.S.C.,
RA   Rocha S.N., Santos K., Satori D., Silva A.G., Simao R.C.G., Soares M.A.M.,
RA   Souza E.M., Steffens M.B.R., Steindel M., Tadra-Sfeir M.Z., Takahashi E.K.,
RA   Torres R.A., Valle J.S., Vernal J.I., Vilas-Boas L.A., Watanabe M.A.E.,
RA   Weiss V.A., Yates M.A., Souza E.M.;
RT   "The genome of Herbaspirillum seropedicae SmR1, an endophytic, nitrogen-
RT   fixing, plant-growth promoting beta-Proteobacteria.";
RL   Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=17853511; DOI=10.1002/pmic.200600859;
RA   Chaves D.F.S., Ferrer P.P., de Souza E.M., Gruz L.M., Monteiro R.A.,
RA   de Oliveira Pedrosa F.;
RT   "A two-dimensional proteome reference map of Herbaspirillum seropedicae
RT   proteins.";
RL   Proteomics 7:3759-3763(2007).
CC   -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC       peroxidase activity. {ECO:0000250}.
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;
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   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250};
CC       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
CC       {ECO:0000250};
CC   -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000250}.
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:0000250}.
CC   -!- SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CP002039; ADJ62758.1; -; Genomic_DNA.
DR   RefSeq; WP_013233264.1; NC_014323.1.
DR   AlphaFoldDB; D8INT8; -.
DR   SMR; D8INT8; -.
DR   STRING; 757424.Hsero_1242; -.
DR   EnsemblBacteria; ADJ62758; ADJ62758; Hsero_1242.
DR   KEGG; hse:Hsero_1242; -.
DR   eggNOG; COG0376; Bacteria.
DR   HOGENOM; CLU_025424_2_0_4; -.
DR   OMA; MILAGNC; -.
DR   OrthoDB; 49441at2; -.
DR   BioCyc; HSER757424:HSERO_RS06245-MON; -.
DR   Proteomes; UP000000329; 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; 2.
PE   1: Evidence at protein level;
KW   Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW   Reference proteome.
FT   CHAIN           1..748
FT                   /note="Catalase-peroxidase"
FT                   /id="PRO_0000400097"
FT   REGION          194..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          288..310
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        289..307
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        92
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         283
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:0000250"
FT   SITE            88
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        91..242
FT                   /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT                   268)"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        242..268
FT                   /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT                   91)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   748 AA;  81181 MW;  72B8D9B4CA803A63 CRC64;
     MSNEAKCPFN HTAGSGTSNR DWWPKQLRVD LLAQHSSKSN PMGEDFDYAE AFKSLDLAAV
     KADLAKVMTD SQDWWPADFG HYGPLFVRMA WHSAGTYRIG DGRGGAGRGQ QRFAPLNSWP
     DNVNLDKARR LLWPVKQKYG NKISWADLLI LTGNVALETM GFKTFGFAGG RADVWEPDLD
     VYWGTESTWL GGDDRYGKGK GSSSQGEIPA DAHRHGQEQA RTAPAGRNLE NPLAAVQMGL
     IYVNPEGPEG NPDPLAAAHD IRETFARMAM DDEETVALIA GGHTFGKTHG AGDAKHVGRE
     PEGEDMDSQG LGWKSSFGSG VGGDTISSGL EVTWTQTPAQ WSNYFFENLF KYEWELTKSP
     AGAHQWVAKG ADAVIPHAHG GAPLLPTMLT TDLSLRFDPA YEKISRRFLE HPEQFADAFA
     RAWFKLTHRD LGPRSRYLGP EVPAEELIWQ DPLPQAEGAQ IDAADVAALK AKVLGSGLSV
     PELVATAWAS ASTFRGGDMR GGANGARIRL APQKDWAANQ PAQLAKVLKT LEGIQSAFNQ
     GGKKVSLADL IVLAGSAAVE KAAQDAGVAV AVPFRAGRVD ASQEQTDAAS FAPLEPIVDG
     FRNFQKQRYA VRGEDMLIDK AQQLTLSAPE MTVLVGGLRV LGNNVGGSTK GMFTDRVGVL
     SNDFFVNLLD MATEWKSTSP AQEEFEGRDR KTGAVKWAGT RVDLVFGSNA VLRALAEVYA
     SADAKEKFVK DFVAAWVKVM ELDRFDLK