ID S5N333_SALBN Unreviewed; 726 AA. AC S5N333; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 28-FEB-2018, entry version 32. DE RecName: Full=Catalase-peroxidase {ECO:0000256|RuleBase:RU003451}; DE EC=1.11.1.21 {ECO:0000256|RuleBase:RU003451}; 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 RT isolate."; RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Bifunctional enzyme with both catalase and broad- CC spectrum peroxidase activity. {ECO:0000256|HAMAP-Rule:MF_01961, CC ECO:0000256|SAAS:SAAS00704213}. CC -!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O. CC {ECO:0000256|RuleBase:RU003451, ECO:0000256|SAAS:SAAS00704184}. CC -!- CATALYTIC ACTIVITY: Donor + H(2)O(2) = oxidized donor + 2 H(2)O. CC {ECO:0000256|RuleBase:RU003451, ECO:0000256|SAAS:SAAS00704189}. CC -!- COFACTOR: CC Name=heme b; Xref=ChEBI:CHEBI:60344; CC Evidence={ECO:0000256|RuleBase:RU003451}; CC -!- PTM: Formation of the three residue Trp-Tyr-Met cross-link is CC important for the catalase, but not the peroxidase activity of the CC enzyme. {ECO:0000256|HAMAP-Rule:MF_01961}. CC -!- SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase CC subfamily. {ECO:0000256|RuleBase:RU003451, CC ECO:0000256|SAAS:SAAS00704215}. 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 EnsemblBacteria; AGR61319; AGR61319; A464_4136. DR KEGG; sbz:A464_4136; -. DR PATRIC; fig|1197719.3.peg.4128; -. DR KO; K03782; -. DR OrthoDB; POG091H05R1; -. DR BioCyc; SBON1197719:G1HJ0-4149-MONOMER; -. 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; IPR010255; Haem_peroxidase. DR InterPro; IPR002016; Haem_peroxidase_pln/fun/bac. 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 Complete proteome {ECO:0000313|Proteomes:UP000015042}; KW Heme {ECO:0000256|RuleBase:RU003451, ECO:0000256|SAAS:SAAS00706545}; KW Hydrogen peroxide {ECO:0000256|RuleBase:RU003451, KW ECO:0000256|SAAS:SAAS00704205}; KW Iron {ECO:0000256|RuleBase:RU003451, ECO:0000256|SAAS:SAAS00706540}; KW Metal-binding {ECO:0000256|RuleBase:RU003451, KW ECO:0000256|SAAS:SAAS00706538}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003451, KW ECO:0000256|SAAS:SAAS00706525}; KW Peroxidase {ECO:0000256|RuleBase:RU003451, KW ECO:0000256|SAAS:SAAS00706532, ECO:0000313|EMBL:AGR61319.1}. FT DOMAIN 139 424 PEROXIDASE_4. {ECO:0000259|PROSITE: FT PS50873}. FT ACT_SITE 106 106 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_01961}. FT METAL 267 267 Iron (heme axial ligand). FT {ECO:0000256|HAMAP-Rule:MF_01961}. FT SITE 102 102 Transition state stabilizer. FT {ECO:0000256|HAMAP-Rule:MF_01961}. FT CROSSLNK 105 226 Tryptophyl-tyrosyl-methioninium (Trp-Tyr) FT (with Met-252). {ECO:0000256|HAMAP-Rule: FT MF_01961}. FT CROSSLNK 226 252 Tryptophyl-tyrosyl-methioninium (Tyr-Met) FT (with Trp-105). {ECO:0000256|HAMAP-Rule: FT 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 //