ID A0A6S6M053_9BACT Unreviewed; 711 AA. AC A0A6S6M053; DT 02-DEC-2020, integrated into UniProtKB/TrEMBL. DT 02-DEC-2020, sequence version 1. DT 29-MAY-2024, entry version 13. 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:BCG45566.1}; GN ORFNames=GEOBRER4_03160 {ECO:0000313|EMBL:BCG45566.1}; OS Citrifermentans bremense. OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales; OC Geobacteraceae; Citrifermentans. OX NCBI_TaxID=60035 {ECO:0000313|EMBL:BCG45566.1, ECO:0000313|Proteomes:UP000515472}; RN [1] {ECO:0000313|EMBL:BCG45566.1, ECO:0000313|Proteomes:UP000515472} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R4 {ECO:0000313|EMBL:BCG45566.1, RC ECO:0000313|Proteomes:UP000515472}; RA Meng L., Yoshida N.; RT "Interaction of electrochemicaly active bacteria, Geobacter bremensis R4 on RT different carbon anode."; RL Submitted (JUN-2020) 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; AP023213; BCG45566.1; -; Genomic_DNA. DR AlphaFoldDB; A0A6S6M053; -. DR KEGG; gbn:GEOBRER4_03160; -. DR Proteomes; UP000515472; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. 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:0070301; P:cellular response to hydrogen peroxide; IEA:TreeGrafter. DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW. 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 InterPro; IPR019793; Peroxidases_heam-ligand_BS. 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; 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 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 108..397 FT /note="Plant heme peroxidase family profile" FT /evidence="ECO:0000259|PROSITE:PS50873" FT ACT_SITE 75 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961" FT BINDING 238 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 71 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961" FT CROSSLNK 197..223 FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp- FT 74)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961" SQ SEQUENCE 711 AA; 78508 MW; 5325DC7D37F2F8FE CRC64; MNRDWWPNQL NLKILHQHSP LSNPMGGNFN YSEEFETLDL AAVRQDIFEL MTTSQEWWPA DYGHYGPLFI RMAWHSAGTY RTGDGRGGAR SGSQRFAPLN SWPDNANLDK ARMLLWPIKQ KYGKKISWAD LLIFAGNCAL ESMGFKTFGF GGGREDIWEP GEDIYWGAED TWLGDTRYSG ERLLENPLAA VQMGLIYVNP EGPNGNPDPL AAAKDIRETF ARMAMNDEET VALIAGGHTF GKCHGAGAAT HVGPEPEGAS IIEQGLGWKC SFGTGKGEYT ITSGLEGAWT TNPVKWDNGF FDVLFRYDWA LTKSPAGAHQ WTPTDPAAKG TVPDAHNPTK RHAPMMLTTD LALKLDPIYG PISKRFHEQP DVFADAFARA WFKLTHRDMG PRACYLGPQV PAEDLIWQDP LPARNHELID DKDIAELKGK IITSGLSIPQ LVSTAWASAS TFRSSDRRGG ANGARIRLAP QKDWEVNQPA QLKLVLETLE GIQKQFNSAQ SGGKRVSIAD LIVLGGCAAI ELAARNAGHE VLVPFTPGRT DAKQEQTDVV AFAPLEPTAD GFRNYLKARY SVSAEELLVD RAQLLTLSAP EMTVLIGGMR VLDANANQSR HGVFTKQPGT LTNDFFVNLL DMSTTWSATS EAEDVFEGRD RVTGEMKWTG TRVDLIFGSN SLLRAQAEVY GCKDSQEKFL LDFIAAWCKV MNLDRFDIAK S //