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}.
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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
//