ID S5N333_SALBN Unreviewed; 726 AA. AC S5N333; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 02-JUN-2021, entry version 45. 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=A464_4136 {ECO:0000313|EMBL:AGR61319.1}; OS Salmonella bongori N268-08. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=1197719 {ECO:0000313|EMBL:AGR61319.1, ECO:0000313|Proteomes:UP000015042}; RN [1] {ECO:0000313|EMBL:AGR61319.1, ECO:0000313|Proteomes:UP000015042} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=N268-08 {ECO:0000313|EMBL:AGR61319.1, RC ECO:0000313|Proteomes:UP000015042}; RA Marti R., Hagens S., Loessner M.J., Klumpp J.; RT "Genome sequence of Salmonella bongori N268-08 - a rare clinical isolate."; RL Submitted (JUL-2013) 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|ARBA:ARBA00001970, CC 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 --------------------------------------------------------------------------- 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; CP006608; AGR61319.1; -; Genomic_DNA. DR RefSeq; WP_020845759.1; NC_021870.1. DR STRING; 1197719.A464_4136; -. DR EnsemblBacteria; AGR61319; AGR61319; A464_4136. DR KEGG; sbz:A464_4136; -. DR PATRIC; fig|1197719.3.peg.4128; -. DR eggNOG; COG0376; Bacteria. DR HOGENOM; CLU_025424_2_0_6; -. DR Proteomes; UP000015042; 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; 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 139..424 FT /note="PEROXIDASE_4" FT /evidence="ECO:0000259|PROSITE:PS50873" FT REGION 1..33 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..16 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 106 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961" FT METAL 267 FT /note="Iron (heme axial ligand)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961" FT SITE 102 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961" FT CROSSLNK 105..226 FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with Met- FT 252)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961" FT CROSSLNK 226..252 FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp- FT 105)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961" SQ SEQUENCE 726 AA; 79686 MW; 455081851DA998E5 CRC64; MSTTDDTHNT LSTGKCPFHQ GGHDRSAGAG TASRDWWPNQ LRVDLLNQHS NRSNPLGEDF DYRKEFSKLD YSALKGDLKA LLTDSQPWWP ADWGSYVGLF IRMAWHGAGT YRSIDGRGGA GRGQQRFAPL NSWPDNVSLD KARRLLWPIK QKYGQKISWA DLFILAGNVA LENSGFRTFG FGAGREDVWE PDLDVNWGDE KAWLTHRHPE ALAKAPLGAT EMGLIYVNPE GPDHSGEPLS AAAAIRATFG NMGMNDEETV ALIAGGHTLG KTHGAAAASH VGADPEAAPI EAQGLGWASS YGSGVGADAI TSGLEVVWTQ TPTQWSNYFF ENLFKYEWVQ TRSPAGAIQF EAVDAPESIP DPFDPSKKRK PTMLVTDLTL RFDPEFEKIS RRFLNDPQAF NEAFARAWFK LTHRDMGPKA RYIGPEVPKE DLIWQDPLPQ PLYQPTQEDI INLKAAIAAS GLSISEMVSV AWASASTFRG GDKRGGANGA RLALAPQRDW DVNAVAARVL PVLEELQKKT NKASLADIIV LAGVVGIEQA AAAAGVSISV PFAPGRVDAR QDQTDIEMFS LLEPIADGFR NYRARLDVST TESLLIDKAQ QLTLTAPEMT VLVGGMRVLG TNFDGSQNGV FTDRPGVLST DFFANLLDMR YEWKPTDESN ELFEGRDRLT GEVKYTATRA DLVFGSNSVL RALAEVYACS DAHEKFVKDF VAAWVKVMNL DRFDLL //