ID   A0A1I0SYU1_9SPHI        Unreviewed;       759 AA.
AC   A0A1I0SYU1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   16-JAN-2019, entry version 13.
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   ORFNames=SAMN04488511_104172 {ECO:0000313|EMBL:SFA44689.1};
OS   Pedobacter suwonensis.
OC   Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=332999 {ECO:0000313|EMBL:SFA44689.1, ECO:0000313|Proteomes:UP000198836};
RN   [1] {ECO:0000313|EMBL:SFA44689.1, ECO:0000313|Proteomes:UP000198836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18130 {ECO:0000313|EMBL:SFA44689.1,
RC   ECO:0000313|Proteomes:UP000198836};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01961}.
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DR   EMBL; FOJM01000004; SFA44689.1; -; Genomic_DNA.
DR   Proteomes; UP000198836; 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   Complete proteome {ECO:0000313|Proteomes:UP000198836};
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:SFA44689.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198836}.
FT   DOMAIN      135    433       PEROXIDASE_4. {ECO:0000259|PROSITE:
FT                                PS50873}.
FT   ACT_SITE    102    102       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01961}.
FT   METAL       289    289       Iron (heme axial ligand).
FT                                {ECO:0000256|HAMAP-Rule:MF_01961}.
FT   SITE         98     98       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_01961}.
FT   CROSSLNK    248    274       Tryptophyl-tyrosyl-methioninium (Tyr-Met)
FT                                (with Trp-101). {ECO:0000256|HAMAP-Rule:
FT                                MF_01961}.
SQ   SEQUENCE   759 AA;  82853 MW;  6BD2142B4B76587A CRC64;
     MEKESNDISK CPFHNGSMKS NVAGGGTRNG DWWPKQLNLS ILRQHSSLSN PMDDGFNYAE
     AFKSLDLAAL KADLHALMTD SQDWWPADFG HYGGLFIRMA WHSAGTYRVG DGRGGAGAGL
     QRFAPLNSWP DNVSLDKARR LLWPIKQKYG RKISWADLMI LTGNVALESM GFKTFGFAGG
     REDVWEADES VYWGSETTWL GGDLRYGHGS DGADKVHGVV VTDDDADGDI HSRNLEKPLA
     AVQMGLIYVN PEGPDGNPDP ILAAKDIRDT FGRMAMDDEE TVALIAGGHT FGKTHGAASA
     DHVGKEPEAA DIENQGFGWN NSYGSGKGAD AITSGLEVIW TTTPTQWSNN FFENLFGFEW
     ELTKSPAGAH QWKAINADAI IPDAFDGSKK HLPTMLTTDL ALRFDPAYEK ISRRFLENPD
     QFADAFARAW FKLTHRDMGP VARYLGPEVP QEKLLWQDPI PAVDHVLISE SDVAALKAKV
     LASGLSVSEL VSTAWASAST FRGSDKRGGA NGARIRLAPQ KDWAVNNPPQ LQKVLNVLEG
     IQNEFNAAQF DGKKVSLADL IVLAGVAAVE KAAADAGHSI LVPFTPGRMD ASQAQTDIES
     FGYLEPAADG FRNYRKVKSP VPTEEFLIDK AQLLTLTAPE LTVLVGGLRA LDTNFDGSKN
     GVLTTKPGQL TNDFFINLLD METAWKAIAE DKELYMGSSR STGQPKWTAT RADLVFGSNA
     ELRAIAEVYA SADAQEKFVK DFVATWNKVM NLDRFDLIN
//