ID A0A1I0SYU1_9SPHI Unreviewed; 759 AA. AC A0A1I0SYU1; DT 22-NOV-2017, integrated into UniProtKB/TrEMBL. DT 22-NOV-2017, sequence version 1. DT 07-OCT-2020, entry version 20. DE RecName: Full=Catalase-peroxidase {ECO:0000256|HAMAP-Rule:MF_01961, ECO:0000256|RuleBase:RU003451}; DE Short=CP {ECO:0000256|HAMAP-Rule:MF_01961}; DE EC=1.11.1.21 {ECO:0000256|HAMAP-Rule:MF_01961, ECO:0000256|RuleBase:RU003451}; DE AltName: Full=Peroxidase/catalase {ECO:0000256|HAMAP-Rule:MF_01961}; GN Name=katG {ECO:0000256|HAMAP-Rule:MF_01961}; GN ORFNames=SAMN04488511_104172 {ECO:0000313|EMBL:SFA44689.1}; OS Pedobacter suwonensis. OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Pedobacter. OX NCBI_TaxID=332999 {ECO:0000313|EMBL:SFA44689.1, ECO:0000313|Proteomes:UP000198836}; RN [1] {ECO:0000313|Proteomes:UP000198836} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18130 {ECO:0000313|Proteomes:UP000198836}; RA Varghese N., Submissions S.; RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum CC peroxidase activity. {ECO:0000256|HAMAP-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:0000256|ARBA:ARBA00001378, ECO:0000256|HAMAP- CC Rule:MF_01961, ECO:0000256|RuleBase:RU003451}; 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:0000256|HAMAP- CC Rule:MF_01961, ECO:0000256|RuleBase:RU003451}; CC -!- COFACTOR: CC Name=heme b; Xref=ChEBI:CHEBI:60344; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01961}; CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer. CC {ECO:0000256|HAMAP-Rule:MF_01961}; CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01961}. CC -!- SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01961, CC ECO:0000256|RuleBase:RU003451}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01961}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; FOJM01000004; SFA44689.1; -; Genomic_DNA. DR Proteomes; UP000198836; Unassembled WGS sequence. 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 {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|HAMAP-Rule:MF_01961, KW ECO:0000256|RuleBase:RU003451}; KW Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324, ECO:0000256|HAMAP- KW Rule:MF_01961, ECO:0000256|RuleBase:RU003451}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01961, KW ECO:0000256|RuleBase:RU003451}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01961, ECO:0000256|RuleBase:RU003451}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_01961, ECO:0000256|RuleBase:RU003451}; KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|HAMAP-Rule:MF_01961, KW ECO:0000256|RuleBase:RU003451, ECO:0000313|EMBL:SFA44689.1}. FT DOMAIN 135..433 FT /note="PEROXIDASE_4" FT /evidence="ECO:0000259|PROSITE:PS50873" FT REGION 1..21 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 102 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961" FT METAL 289 FT /note="Iron (heme axial ligand)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961" FT SITE 98 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961" FT CROSSLNK 248..274 FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp- FT 101)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961" SQ SEQUENCE 759 AA; 82853 MW; 6BD2142B4B76587A CRC64; MEKESNDISK CPFHNGSMKS NVAGGGTRNG DWWPKQLNLS ILRQHSSLSN PMDDGFNYAE AFKSLDLAAL KADLHALMTD SQDWWPADFG HYGGLFIRMA WHSAGTYRVG DGRGGAGAGL QRFAPLNSWP DNVSLDKARR LLWPIKQKYG RKISWADLMI LTGNVALESM GFKTFGFAGG REDVWEADES VYWGSETTWL GGDLRYGHGS DGADKVHGVV VTDDDADGDI HSRNLEKPLA AVQMGLIYVN PEGPDGNPDP ILAAKDIRDT FGRMAMDDEE TVALIAGGHT FGKTHGAASA DHVGKEPEAA DIENQGFGWN NSYGSGKGAD AITSGLEVIW TTTPTQWSNN FFENLFGFEW ELTKSPAGAH QWKAINADAI IPDAFDGSKK HLPTMLTTDL ALRFDPAYEK ISRRFLENPD QFADAFARAW FKLTHRDMGP VARYLGPEVP QEKLLWQDPI PAVDHVLISE SDVAALKAKV LASGLSVSEL VSTAWASAST FRGSDKRGGA NGARIRLAPQ KDWAVNNPPQ LQKVLNVLEG IQNEFNAAQF DGKKVSLADL IVLAGVAAVE KAAADAGHSI LVPFTPGRMD ASQAQTDIES FGYLEPAADG FRNYRKVKSP VPTEEFLIDK AQLLTLTAPE LTVLVGGLRA LDTNFDGSKN GVLTTKPGQL TNDFFINLLD METAWKAIAE DKELYMGSSR STGQPKWTAT RADLVFGSNA ELRAIAEVYA SADAQEKFVK DFVATWNKVM NLDRFDLIN //