KATG_SHELP
ID KATG_SHELP Reviewed; 756 AA.
AC A3QAT3;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 99.
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};
DE Flags: Precursor;
GN Name=katG {ECO:0000255|HAMAP-Rule:MF_01961}; OrderedLocusNames=Shew_0709;
OS Shewanella loihica (strain ATCC BAA-1088 / PV-4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=323850;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1088 / PV-4;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Serres G.,
RA Fredrickson J., Tiedje J., Richardson P.;
RT "Complete sequence of Shewanella loihica PV-4.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000606; ABO22581.1; -; Genomic_DNA.
DR RefSeq; WP_011864515.1; NC_009092.1.
DR AlphaFoldDB; A3QAT3; -.
DR SMR; A3QAT3; -.
DR STRING; 323850.Shew_0709; -.
DR PeroxiBase; 3562; SHspCP01_PV-4.
DR EnsemblBacteria; ABO22581; ABO22581; Shew_0709.
DR KEGG; slo:Shew_0709; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_6; -.
DR OMA; EEIFWGP; -.
DR OrthoDB; 49441at2; -.
DR Proteomes; UP000001558; 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;
KW Reference proteome; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CHAIN 27..756
FT /note="Catalase-peroxidase"
FT /id="PRO_5000228926"
FT ACT_SITE 127
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 289
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 123
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 126..248
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 274)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 248..274
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 126)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 756 AA; 83204 MW; 447D42CFC535AE7D CRC64;
MKGKTVNKQT LAALVSALLV FNPAVADEQE SAQMTKPKGA AATGTAKAFQ PKSKQFWWPD
QLDLSPLRDH DSRSNPYGES FDYAKAFNSL DLDQVKADID QLLTQSQDWW PADYGNYGPF
FIRMTWHSAG TYRTLDGRGG AGGGQQRFEP LNSWPDNASL DKARRLLWPV KQKYGEALSW
SDLIVLAGNV ALENMGFKTF GFAGGRNDDW EPDMVYWGPE VEMLASDRED RDGKLQRPLG
ATHMGLIYVN PEGPKGVPDP LGSAKNIRTA FSRMAMNDEE TLALIAGGHT FGKMHGAHKP
KDCLGAEPAA AGIEAQGLGW HNKCGKGHSE DTITSGLEGA WTQAPTKWTS LYLSNLLTYD
WQQTRSPAGA IQWIPTDESV HKAVPDAHVK GKFHAPVMTT ADLALKYDPE YRKIAERFLA
DPEEYRLAFA KAWYKLTHRD MGPARNFLGK EVPQGNFIWQ DPIDDKTQSR LSAGDIKQLK
KAISKSGLSV AERVRLAWAS AASYRQSDMR GGANGARIAL APQKDWTVNN PAETAKVLKT
LEAIRADFNK GAGKRQVSLA DLIVLAGASA LEQAAKQAGF EVAVPFTPGR GDATQAQTDE
NSFSLLELHA DGFRNYFDVN HSYKSPTEML VDKADQLDLT VPEMTVLVGG LRALDANYQG
AKHGVLTQRP GTLNNDFFVN LLDMSTLWQK SDVDGIYQGL DRSSGKPKWT ATSVDLIFGS
NSELRAVAEV YAFDTSKQKF VDDFVAAWVK VMNLDR
