ID A0A3T3GB00_SALET Unreviewed; 726 AA. AC A0A3T3GB00; A0A6C8XK67; DT 08-MAY-2019, integrated into UniProtKB/TrEMBL. DT 08-MAY-2019, sequence version 1. DT 03-AUG-2022, entry version 20. 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:EBV9200547.1}; GN ORFNames=A4W49_17175 {ECO:0000313|EMBL:EDA9403245.1}, A4W57_15605 GN {ECO:0000313|EMBL:EDA9438227.1}, AIK92_15990 GN {ECO:0000313|EMBL:MID46438.1}, ASH82_07930 GN {ECO:0000313|EMBL:EBV9200547.1}, CB395_13360 GN {ECO:0000313|EMBL:EDH6429806.1}, D6J51_16065 GN {ECO:0000313|EMBL:EBY7386024.1}, D6K67_14700 GN {ECO:0000313|EMBL:EBY7627669.1}, DKU10_12110 GN {ECO:0000313|EMBL:EBU6915444.1}, DOJ23_08140 GN {ECO:0000313|EMBL:EBV3761516.1}, DP829_17530 GN {ECO:0000313|EMBL:EBW6733602.1}, DPJ44_15275 GN {ECO:0000313|EMBL:EBW4105466.1}, DPS10_11625 GN {ECO:0000313|EMBL:EBX3355507.1}, DQQ63_16065 GN {ECO:0000313|EMBL:ECT0411527.1}, DY868_18255 GN {ECO:0000313|EMBL:ECU3484604.1}, EUX26_17870 GN {ECO:0000313|EMBL:ECB0525011.1}, F9G64_06830 GN {ECO:0000313|EMBL:EDA0174555.1}, G0D76_21305 GN {ECO:0000313|EMBL:HAC6917684.1}, G3408_004062 GN {ECO:0000313|EMBL:HAE2914880.1}, G4B28_002876 GN {ECO:0000313|EMBL:HAE3940876.1}, G4B35_001986 GN {ECO:0000313|EMBL:HAE4048868.1}, G4I58_003730 GN {ECO:0000313|EMBL:HAE6002075.1}, G4I61_003038 GN {ECO:0000313|EMBL:HAE6032873.1}, G4L02_004140 GN {ECO:0000313|EMBL:HAE6748354.1}, G4Y23_004155 GN {ECO:0000313|EMBL:HAE9563348.1}, G9C15_001071 GN {ECO:0000313|EMBL:HAF0861915.1}, GCZ77_21285 GN {ECO:0000313|EMBL:EDH0980684.1}; OS Salmonella enterica subsp. enterica serovar Braenderup. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=149391 {ECO:0000313|EMBL:EBV9200547.1}; RN [1] {ECO:0000313|EMBL:HAC6917684.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=10-0026 {ECO:0000313|EMBL:HAE6032873.1}, 10-2663 RC {ECO:0000313|EMBL:HAE3940876.1}, 10-2762 RC {ECO:0000313|EMBL:HAE4048868.1}, 11-2318 RC {ECO:0000313|EMBL:HAE2914880.1}, 12-7261 RC {ECO:0000313|EMBL:HAE6002075.1}, 13-0112 RC {ECO:0000313|EMBL:HAF0861915.1}, 13-2733 RC {ECO:0000313|EMBL:HAE9563348.1}, 13-2740 RC {ECO:0000313|EMBL:HAE6748354.1}, and 14-0315 RC {ECO:0000313|EMBL:HAC6917684.1}; RX PubMed=30286803; RA Souvorov A., Agarwala R., Lipman D.J.; RT "SKESA: strategic k-mer extension for scrupulous assemblies."; RL Genome Biol. 19:153-150(2018). RN [2] {ECO:0000313|EMBL:HAC6917684.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=10-0026 {ECO:0000313|EMBL:HAE6032873.1}, 10-2663 RC {ECO:0000313|EMBL:HAE3940876.1}, 10-2762 RC {ECO:0000313|EMBL:HAE4048868.1}, 11-2318 RC {ECO:0000313|EMBL:HAE2914880.1}, 12-7261 RC {ECO:0000313|EMBL:HAE6002075.1}, 13-0112 RC {ECO:0000313|EMBL:HAF0861915.1}, 13-2733 RC {ECO:0000313|EMBL:HAE9563348.1}, 13-2740 RC {ECO:0000313|EMBL:HAE6748354.1}, and 14-0315 RC {ECO:0000313|EMBL:HAC6917684.1}; RG NCBI Pathogen Detection Project; RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:EBV9200547.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FDA00007829 {ECO:0000313|EMBL:MID46438.1, RC ECO:0000313|Proteomes:UP000270594}, FSIS11810940 RC {ECO:0000313|EMBL:ECT0411527.1}, FSIS11812815 RC {ECO:0000313|EMBL:ECU3484604.1}, and NY-N20005 RC {ECO:0000313|EMBL:EBV9200547.1}; RG GenomeTrakr network: Whole genome sequencing for foodborne pathogen traceback; RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:EDA9403245.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=105336 {ECO:0000313|EMBL:EBV3761516.1}, 205626 RC {ECO:0000313|EMBL:EBX3355507.1}, 223495 RC {ECO:0000313|EMBL:EDA9438227.1}, 236276 RC {ECO:0000313|EMBL:EDA9403245.1}, 271067 RC {ECO:0000313|EMBL:EBW6733602.1}, 300664 RC {ECO:0000313|EMBL:EBW4105466.1}, 329132 RC {ECO:0000313|EMBL:EBY7627669.1}, 358409 RC {ECO:0000313|EMBL:EDH6429806.1}, 394884 RC {ECO:0000313|EMBL:EBY7386024.1}, 443566 RC {ECO:0000313|EMBL:EBU6915444.1}, 555488 RC {ECO:0000313|EMBL:ECB0525011.1}, and 810119 RC {ECO:0000313|EMBL:EDA0174555.1}; 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. RN [5] {ECO:0000313|EMBL:EDH0980684.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SAL-19-VL-WA-IL-0012 {ECO:0000313|EMBL:EDH0980684.1}; RG Veterinary Laboratory Investigation and Response Network; RL Submitted (OCT-2019) 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: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:EBV9200547.1}. 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; AAHCWL010000009; EBU6915444.1; -; Genomic_DNA. DR EMBL; AAHFAS010000013; EBV3761516.1; -; Genomic_DNA. DR EMBL; AAHGTQ010000006; EBV9200547.1; -; Genomic_DNA. DR EMBL; AAHIGD010000009; EBW4105466.1; -; Genomic_DNA. DR EMBL; AAHIXO010000012; EBW6733602.1; -; Genomic_DNA. DR EMBL; AAHKXZ010000007; EBX3355507.1; -; Genomic_DNA. DR EMBL; AAHOXC010000012; EBY7386024.1; -; Genomic_DNA. DR EMBL; AAHPAD010000009; EBY7627669.1; -; Genomic_DNA. DR EMBL; AAHWIJ010000012; ECB0525011.1; -; Genomic_DNA. DR EMBL; AAKLND010000020; ECT0411527.1; -; Genomic_DNA. DR EMBL; AAKPQX010000010; ECU3484604.1; -; Genomic_DNA. DR EMBL; AALIQJ010000007; EDA0174555.1; -; Genomic_DNA. DR EMBL; AALLSV010000014; EDA9403245.1; -; Genomic_DNA. DR EMBL; AALLTD010000013; EDA9438227.1; -; Genomic_DNA. DR EMBL; AAMGJL010000012; EDH0980684.1; -; Genomic_DNA. DR EMBL; AAMIHV010000013; EDH6429806.1; -; Genomic_DNA. DR EMBL; DAAMJL010000010; HAC6917684.1; -; Genomic_DNA. DR EMBL; DAARLP010000009; HAE2914880.1; -; Genomic_DNA. DR EMBL; DAARUC010000019; HAE3940876.1; -; Genomic_DNA. DR EMBL; DAARUZ010000010; HAE4048868.1; -; Genomic_DNA. DR EMBL; DAASLG010000010; HAE6002075.1; -; Genomic_DNA. DR EMBL; DAASLQ010000046; HAE6032873.1; -; Genomic_DNA. DR EMBL; DAASRW010000011; HAE6748354.1; -; Genomic_DNA. DR EMBL; DAATPN010000013; HAE9563348.1; -; Genomic_DNA. DR EMBL; DAAUAM010000008; HAF0861915.1; -; Genomic_DNA. DR EMBL; RSGD01000011; MID46438.1; -; Genomic_DNA. DR RefSeq; WP_000108103.1; NZ_QDUC01000013.1. DR Proteomes; UP000270594; Unassembled WGS sequence. 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 BINDING 267 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 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; 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 //