ID   KATG_SOLUE              Reviewed;         743 AA.
AC   Q02A20;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   02-SEP-2026, entry version 103.
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};
GN   OrderedLocusNames=Acid_1112;
OS   Solibacter usitatus (strain Ellin6076).
OC   Bacteria; Pseudomonadati; Acidobacteriota; Terriglobia; Bryobacterales;
OC   Solibacteraceae; Candidatus Solibacter.
OX   NCBI_TaxID=234267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ellin6076;
RX   PubMed=19201974; DOI=10.1128/aem.02294-08;
RA   Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M.,
RA   Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B.,
RA   Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C.,
RA   Davidsen T.M., DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S.,
RA   Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P.,
RA   Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q.,
RA   Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R.,
RA   Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.;
RT   "Three genomes from the phylum Acidobacteria provide insight into the
RT   lifestyles of these microorganisms in soils.";
RL   Appl. Environ. Microbiol. 75:2046-2056(2009).
CC   -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC       peroxidase activity. {ECO:0000255|HAMAP-Rule:MF_01961}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O2 + AH2 = 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 = O2 + 2 H2O; 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; Evidence={ECO:0000255|HAMAP-
CC         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; CP000473; ABJ82106.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q02A20; -.
DR   SMR; Q02A20; -.
DR   FunCoup; Q02A20; 258.
DR   STRING; 234267.Acid_1112; -.
DR   KEGG; sus:Acid_1112; -.
DR   eggNOG; COG0376; Bacteria.
DR   HOGENOM; CLU_025424_2_0_0; -.
DR   InParanoid; Q02A20; -.
DR   OrthoDB; 9759743at2; -.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-ARBA.
DR   GO; GO:0004096; F:catalase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:TreeGrafter.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:TreeGrafter.
DR   CDD; cd00649; catalase_peroxidase_1; 1.
DR   CDD; cd08200; catalase_peroxidase_2; 1.
DR   FunFam; 1.10.420.10:FF:000002; Catalase-peroxidase; 1.
DR   FunFam; 1.10.420.10:FF:000004; Catalase-peroxidase; 1.
DR   FunFam; 1.10.520.10:FF:000002; Catalase-peroxidase; 1.
DR   Gene3D; 1.10.520.10; -; 2.
DR   Gene3D; 1.10.420.10; Peroxidase, domain 2; 2.
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   NCBIfam; TIGR00198; cat_per_HPI; 1.
DR   NCBIfam; NF011635; PRK15061.1; 1.
DR   PANTHER; PTHR30555:SF0; CATALASE-PEROXIDASE; 1.
DR   PANTHER; PTHR30555; HYDROPEROXIDASE I, BIFUNCTIONAL CATALASE-PEROXIDASE; 1.
DR   Pfam; PF00141; peroxidase; 2.
DR   PRINTS; PR00460; BPEROXIDASE.
DR   PRINTS; PR00458; PEROXIDASE.
DR   SUPFAM; SSF48113; Heme-dependent peroxidases; 2.
DR   PROSITE; PS00435; PEROXIDASE_1; 1.
DR   PROSITE; PS00436; PEROXIDASE_2; 1.
DR   PROSITE; PS50873; PEROXIDASE_4; 2.
PE   3: Inferred from homology;
KW   Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase.
FT   CHAIN           1..743
FT                   /note="Catalase-peroxidase"
FT                   /id="PRO_0000354936"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        106
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   BINDING         268
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            102
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   CROSSLNK        105..227
FT                   /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT                   253)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   CROSSLNK        227..253
FT                   /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT                   105)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ   SEQUENCE   743 AA;  81479 MW;  15497A51D56B3C8B CRC64;
     MEKQSNDAAV AGAPNDHGAA KCPVAHTAHG RRNRDWWPDA LDISTLHRNS SLSDPMGSGF
     DYAMEFESLD LQAVIKDLHA LMTDSQDWWP ADFGHYGGLM IRMAWHSAGT YRITDGRGGA
     GAGQQRFAPL NSWPDNANLD KARRLLWPVK QKYGDKISWA DLMVLAGNVA LESMGFKTFG
     FAGGRSDVWE PEELYWGPEG TWLGDERYSG ERQLSEPLGA VQMGLIYVNP EGPNGNPDPV
     AAAKDIRETF FRMAMNDEET VALIAGGHTF GKTHGAGDPS LVGPDPESGA LEDQGLGWKS
     KFGTGFGADA ITGGPEVTWS QTPTQWSNSF FKNLFENEWE LTNSPAGAKQ WRAKNGQATI
     PDPFDKSKKR VPTMLTTDLS LRFDPAYEKI SRRFYENPDQ FADAFARAWF KLTHRDMGPI
     ARYLGPLVPK ETLLWQDPIP PVDHPLIDEN DASALKAKIL ASGLSTSDLV STAWASASTF
     RGSDKRGGAN GARIRLAPQK DWEVNQPKQL AKVLEKLETI GKEFGKKVSL ADLIVLGGDA
     AIEKAAKDAG VEVKIPFTPG RMDASQEQTD VASFAPLEPK ADGFRNYIGR KTQFLQPEEA
     LVDRAQLLRL TGPEMTVLVG GLRVLGANTA GSKHGVFTAT PGVLTNDFFV NLLDMRTHWQ
     PAGGEEGVYE GRDRKTNALK WTGTRVDLIF GSHSQLRAFA EVYAWAGSKE KFVKDFAAAW
     NKVMNLDRYD VARTGETKKA AVV
//