ID A0AA49Q4L1_9BACT Unreviewed; 736 AA. AC A0AA49Q4L1; DT 24-JAN-2024, integrated into UniProtKB/TrEMBL. DT 24-JAN-2024, sequence version 1. DT 27-MAR-2024, entry version 2. 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 ECO:0000313|EMBL:WKW11864.1}; GN ORFNames=Strain138_001132 {ECO:0000313|EMBL:WKW11864.1}; OS Gemmatimonadaceae bacterium 'strain 138'. OC Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales; OC Gemmatimonadaceae. OX NCBI_TaxID=3062593 {ECO:0000313|EMBL:WKW11864.1}; RN [1] {ECO:0000313|EMBL:WKW11864.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Strain 138 {ECO:0000313|EMBL:WKW11864.1}; RA Haufschild T., Kallscheuer N., Hammer J., Kohn T., Kabuu M., Jogler M., RA Wohfarth N., Heuer A., Rohde M., van Teeseling M.C.F., Jogler C.; RL Submitted (JUL-2023) 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; CP130612; WKW11864.1; -; Genomic_DNA. DR CDD; cd00649; catalase_peroxidase_1; 1. DR CDD; cd08200; catalase_peroxidase_2; 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 NCBIfam; TIGR00198; cat_per_HPI; 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; PS00436; PEROXIDASE_2; 1. DR PROSITE; PS50873; PEROXIDASE_4; 2. PE 3: Inferred from homology; KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|HAMAP-Rule:MF_01961}; KW Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324, ECO:0000256|HAMAP- KW Rule:MF_01961}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01961}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01961}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_01961}; KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|HAMAP- KW Rule:MF_01961}. FT DOMAIN 134..425 FT /note="Plant heme peroxidase family profile" FT /evidence="ECO:0000259|PROSITE:PS50873" FT DOMAIN 479..736 FT /note="Plant heme peroxidase family profile" FT /evidence="ECO:0000259|PROSITE:PS50873" FT REGION 1..27 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 101 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961" FT BINDING 264 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:0000256|HAMAP-Rule:MF_01961" FT SITE 97 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961" FT CROSSLNK 223..249 FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp- FT 100)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961" SQ SEQUENCE 736 AA; 80659 MW; 93011261F53D91AA CRC64; MSDSAKSGGK CPVMHGSPSA VKAGGRSNRD WWPNQLNIGI LHQNPPAGDP MGAAFDYAKE FATLDLDAVV ADLKALMTDS QDWWPADYGH YGPLMIRMAW HSAGTYRTAD GRGGAGNGTQ RFAPLNSWPD NGNLDKARRL LWPIKQKYGK KLSWADLMIL AGNVALESMG FKTFGFAGGR ADVWEPEQDI YWGPEADMLG DKRYSGDREL ENPLAAVQMG LIYVNPEGPN GKPDPLASAR DIRETFRRMA MNDEETVALT AGGHTFGKMH GAGDPALVGK EPEGASMEEQ GLGWKNALGT GKGEFTTTSG LEGAWTPTPT QWDNSYFETL FKWEWELVKS PAGAWIWEPK DKEAARTVPD AHVKGKFVLP AMSTADMAMR EDPAYRKISE RFHKHPEQLA DAFARAWFKL THRDMGPRAR YLGKLVPSEV LSWQDPVPAV DHPLVDAKDI AALKATLLKS GLSISELVST AWASASTFRG SDKRGGANGA RIRLAPQKDW EVNEPRQLTR VLAVLEKIQA EFNAAQKGGK KVSLADLIVL GGVAAIEEAA RKGGLNITVP FTPGRSDATQ EQTDVESFAW LEPQADGFRN WQKTRFSVSA EEMLLDKAQL LTLTAPEMTA LVGGLRVLGA NHGGSKHGVL TTRPETLTND FFVNLLDMGV EWKSVSEAQE LFEARDRKTG AVKWTGTRND LVFGSHSQLR ALAEAFAESD AQERFAKTFV AAWTKVMDAD RFDLAK //