ID A0A2X4TNM5_SALER Unreviewed; 668 AA.
AC A0A2X4TNM5;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Catalase-peroxidase {ECO:0000256|RuleBase:RU003451};
DE EC=1.11.1.21 {ECO:0000256|RuleBase:RU003451};
GN Name=katG {ECO:0000313|EMBL:SQI27959.1};
GN ORFNames=NCTC7307_05392 {ECO:0000313|EMBL:SQI27959.1};
OS Salmonella enterica subsp. arizonae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=59203 {ECO:0000313|EMBL:SQI27959.1, ECO:0000313|Proteomes:UP000248731};
RN [1] {ECO:0000313|EMBL:SQI27959.1, ECO:0000313|Proteomes:UP000248731}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC7307 {ECO:0000313|EMBL:SQI27959.1,
RC ECO:0000313|Proteomes:UP000248731};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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,
CC 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;
CC Evidence={ECO:0000256|RuleBase:RU003451};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|ARBA:ARBA00001970,
CC ECO:0000256|RuleBase:RU003451};
CC -!- SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase
CC subfamily. {ECO:0000256|RuleBase:RU003451}.
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DR EMBL; LS483466; SQI27959.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2X4TNM5; -.
DR Proteomes; UP000248731; Chromosome 1.
DR GO; GO:0004096; F:catalase activity; IEA:InterPro.
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 Gene3D; 1.10.520.10; -; 2.
DR Gene3D; 1.10.420.10; Peroxidase, domain 2; 2.
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 NCBIfam; TIGR00198; cat_per_HPI; 1.
DR PANTHER; PTHR30555:SF6; CATALASE-PEROXIDASE; 1.
DR PANTHER; PTHR30555; HYDROPEROXIDASE I, BIFUNCTIONAL CATALASE-PEROXIDASE; 1.
DR Pfam; PF00141; peroxidase; 2.
DR PRINTS; PR00460; BPEROXIDASE.
DR PRINTS; PR00458; PEROXIDASE.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 2.
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|RuleBase:RU003451};
KW Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324,
KW ECO:0000256|RuleBase:RU003451};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU003451};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU003451};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003451};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU003451};
KW Reference proteome {ECO:0000313|Proteomes:UP000248731}.
FT DOMAIN 139..424
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 668 AA; 72487 MW; B7DE22AC3798ACF5 CRC64;
MSTTDDTHNT LSAGKCPFHQ 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 GLSVSEMVSV AWASASTFRG
GDKRGGANGA RLALAPQRDW DVNAVAARVL PVLEELQKTT NKASLADIIV LAGVVGIEQA
AAAAGVSISV PFAPGRVDAR QDQTDIEMFS LLEPIADGFR NYRARLDVST TESLLIDKAQ
QLTLTAPEMT VLVGGMRVLG TNFDGSQNGV FTDRPACSAL TSSLICWICV TSGSPPTTLM
SCSKAGIV
//
