KATG_PSEU2
ID KATG_PSEU2 Reviewed; 756 AA.
AC Q4ZNN4;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Catalase-peroxidase {ECO:0000255|HAMAP-Rule:MF_01961};
DE Short=CP {ECO:0000255|HAMAP-Rule:MF_01961};
DE EC=1.11.1.21 {ECO:0000255|HAMAP-Rule:MF_01961};
DE AltName: Full=Peroxidase/catalase {ECO:0000255|HAMAP-Rule:MF_01961};
GN Name=katG {ECO:0000255|HAMAP-Rule:MF_01961}; OrderedLocusNames=Psyr_4208;
OS Pseudomonas syringae pv. syringae (strain B728a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=205918;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B728a;
RX PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA Kyrpides N.C., Ivanova N., Lindow S.E.;
RT "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT syringae B728a and pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
CC -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC peroxidase activity. {ECO:0000255|HAMAP-Rule:MF_01961}.
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:0000255|HAMAP-
CC 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:0000255|HAMAP-Rule:MF_01961};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01961};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
CC {ECO:0000255|HAMAP-Rule:MF_01961};
CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01961}.
CC -!- SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01961}.
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DR EMBL; CP000075; AAY39238.1; -; Genomic_DNA.
DR RefSeq; WP_011268890.1; NC_007005.1.
DR RefSeq; YP_237276.1; NC_007005.1.
DR AlphaFoldDB; Q4ZNN4; -.
DR SMR; Q4ZNN4; -.
DR STRING; 205918.Psyr_4208; -.
DR PeroxiBase; 2312; PssCP01_B728a.
DR EnsemblBacteria; AAY39238; AAY39238; Psyr_4208.
DR KEGG; psb:Psyr_4208; -.
DR PATRIC; fig|205918.7.peg.4335; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_6; -.
DR OMA; MILAGNC; -.
DR Proteomes; UP000000426; Chromosome.
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; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase.
FT CHAIN 1..756
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354872"
FT REGION 198..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 92
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 285
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:0000255|HAMAP-Rule:MF_01961"
FT SITE 88
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 91..244
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 270)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 244..270
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 91)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 756 AA; 82451 MW; 1C0B9BFB33DF004D CRC64;
MSTESKCPFN HAAGGGTTNR DWWPKQLNLK ILHQHSTLSD PMGENFDYAK EFKSLDIEAV
KQDLRNVMTQ SQDWWPADFG HYGPLFIRMA WHSAGTYRTG DGRGGAGAGQ QRFAPLNSWP
DNVSLDKARR LIWPVKQKYG RKISWADLIV LTGNVALESM GFKTFGFSGG RADVWEPEED
VYWGSETTWL GGEERYGAQK KMQQPGDGTL VAEPENHANE ESRTASGERN LENPLAAVQM
GLIYVNPEGP EGVPDPVASA RDIRETFGRM AMNDEETVAL IAGGHAFGKT HGAGPADNVG
PEPEAAGLEE QGLGWRNKFG SGKGGDTITS GLEVTWTSTP TKWSNEYLEN LFGFEWELTK
SPAGAHQWTP KNGAGAGKIP DAHDPSKRHA PSMLTSDLAL RFDPAYEQIS RRFLNNPEQL
ADAFARAWFK LTHRDMGPLA RYLGPETPAE ELLWQDPIPS VDHALVDDQD VATLKAKILA
SGLSVSQLVS TAWAAASTFR GSDKRGGANG GRLRLAPQKD WAVNQPEQLA GVLKTLEGIQ
SEFNAAQSGG KKVSIADLIV LAGNAGVEQA AKNAGQHVTV PFAPGRADAS QEQTDVESFS
FLEPIADGFR NYQKGHYKVS AESLLVDKAQ LLTLTAPEMT VLLGGLRVLN INVGQSKHGV
FTDQPGTLTN DFFKNLLDMG VEWKATAGGT DTFEARDRKT GAVKWTGTRV DLVFGSHAQL
RAISEVYGSS DAHEKFVKDF VAVWTKVMNL DRFDLA
