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   29-SEP-2021, entry version 17.
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}, DRR55_16885
GN   {ECO:0000313|EMBL:ECU2153094.1}, 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:ECU2153094.1, ECO:0000313|Proteomes:UP000413511}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSIS11810639 {ECO:0000313|EMBL:ECU2153094.1,
RC   ECO:0000313|Proteomes:UP000413511};
RG   NARMS: The National Antimicrobial Resistance Monitoring System;
RL   Submitted (JUN-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: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   [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.
RN   [6] {ECO:0000313|EMBL:EDA0174555.1}
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 (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}.
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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; AAKPGS010000017; ECU2153094.1; -; 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   Proteomes; UP000413511; 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   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;  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
//