ID A0A3T3GB00_SALET Unreviewed; 726 AA. AC A0A3T3GB00; DT 08-MAY-2019, integrated into UniProtKB/TrEMBL. DT 08-MAY-2019, sequence version 1. DT 31-JUL-2019, entry version 4. 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:EAA0622572.1}; GN ORFNames=ABL22_13575 {ECO:0000313|EMBL:EAB6112811.1}, AF673_17905 GN {ECO:0000313|EMBL:EAA8872764.1}, AIM14_20165 GN {ECO:0000313|EMBL:EAA8190682.1}, DKT81_17520 GN {ECO:0000313|EMBL:EAA0622572.1}, OT45_22045 GN {ECO:0000313|EMBL:EAA7148002.1}, PW90_20890 GN {ECO:0000313|EMBL:EAA7358209.1}; OS Salmonella enterica subsp. enterica serovar Braenderup. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=149391 {ECO:0000313|EMBL:EAA0622572.1}; RN [1] {ECO:0000313|EMBL:EAA0622572.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CFSAN030817 {ECO:0000313|EMBL:EAA8190682.1}, FDA00013002 RC {ECO:0000313|EMBL:EAA0622572.1}, and VA-WGS-00568 RC {ECO:0000313|EMBL:EAA8872764.1}; RG GenomeTrakr network: Whole genome sequencing for foodborne pathogen traceback; RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EAA7148002.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=9277 {ECO:0000313|EMBL:EAB6112811.1}, H123760513 RC {ECO:0000313|EMBL:EAA7148002.1}, and H124860457 RC {ECO:0000313|EMBL:EAA7358209.1}; RA Ashton P.M., Dallman T., Nair S., De Pinna E., Peters T., Grant K.; RL Submitted (JUL-2018) 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:SAAS00699576}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; CC EC=1.11.1.21; Evidence={ECO:0000256|HAMAP-Rule:MF_01961, CC ECO:0000256|RuleBase:RU003451, ECO:0000256|SAAS:SAAS01122822}; 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 ECO:0000256|SAAS:SAAS01122785}; CC -!- COFACTOR: CC Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000256|HAMAP- CC 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- CC Rule:MF_01961}. 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|HAMAP-Rule:MF_01961, CC ECO:0000256|RuleBase:RU003451, ECO:0000256|SAAS:SAAS00699595}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAA0622572.1}. 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; AAAAHW010000011; EAA0622572.1; -; Genomic_DNA. DR EMBL; AAACJP010000011; EAA7148002.1; -; Genomic_DNA. DR EMBL; AAACKR010000012; EAA7358209.1; -; Genomic_DNA. DR EMBL; AAACRW010000019; EAA8190682.1; -; Genomic_DNA. DR EMBL; AAACWT010000008; EAA8872764.1; -; Genomic_DNA. DR EMBL; AAAFGK010000012; EAB6112811.1; -; Genomic_DNA. DR RefSeq; WP_000108103.1; NZ_UFRJ01000001.1. DR EnsemblBacteria; AKH09720; AKH09720; SE14_04347. DR EnsemblBacteria; OCS97910; OCS97910; A7B05_03960. DR EnsemblBacteria; OCT00988; OCT00988; A7B04_06490. 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|HAMAP-Rule:MF_01961, ECO:0000256|RuleBase:RU003451, KW ECO:0000256|SAAS:SAAS01096127}; KW Hydrogen peroxide {ECO:0000256|HAMAP-Rule:MF_01961, KW ECO:0000256|RuleBase:RU003451, ECO:0000256|SAAS:SAAS00699625}; KW Iron {ECO:0000256|HAMAP-Rule:MF_01961, ECO:0000256|RuleBase:RU003451, KW ECO:0000256|SAAS:SAAS01096128}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01961, KW ECO:0000256|RuleBase:RU003451, ECO:0000256|SAAS:SAAS01096116}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01961, KW ECO:0000256|RuleBase:RU003451, ECO:0000256|SAAS:SAAS01096123}; KW Peroxidase {ECO:0000256|HAMAP-Rule:MF_01961, KW ECO:0000256|RuleBase:RU003451, ECO:0000256|SAAS:SAAS01096119, KW ECO:0000313|EMBL:EAA0622572.1}. FT DOMAIN 139 424 PEROXIDASE_4. {ECO:0000259|PROSITE: FT PS50873}. FT REGION 1 33 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT COMPBIAS 1 16 Polar. {ECO:0000256|SAM:MobiDB-lite}. 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; 79656 MW; 7C4BA44439E9FFAB 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 EAVDAPDIIP DPFDPSKKRK PTMLVTDLTL RFDPEFEKIS RRFLNDPQAF NEAFARAWFK LTHRDMGPKA RYIGPEVPKE DLIWQDPLPQ PLYQPTQEDI INLKAAIAAS GLSISEMVSV AWASASTFRG GDKRGGANGA RLALAPQRDW DVNAVAARVL PVLEEIQKTT NKASLADIIV LAGVVGIEQA AAAAGVSISV PFAPGRVDAR QDQTDIEMFS LLEPIADGFR NYRARLDVST TESLLIDKAQ QLTLTAPEMT VLVGGMRVLG TNFDGSQNGV FTDRPGVLST DFFANLLDMR YEWKPTDDAN ELFEGRDRLT GEVKYTATRA DLVFGSNSVL RALAEVYACS DAHEKFVKDF VAAWVKVMNL DRFDLQ //