KATG2_SHEFN
ID KATG2_SHEFN Reviewed; 757 AA.
AC Q07YF5;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Catalase-peroxidase 2 {ECO:0000255|HAMAP-Rule:MF_01961};
DE Short=CP 2 {ECO:0000255|HAMAP-Rule:MF_01961};
DE EC=1.11.1.21 {ECO:0000255|HAMAP-Rule:MF_01961};
DE AltName: Full=Peroxidase/catalase 2 {ECO:0000255|HAMAP-Rule:MF_01961};
DE Flags: Precursor;
GN Name=katG2 {ECO:0000255|HAMAP-Rule:MF_01961}; OrderedLocusNames=Sfri_3122;
OS Shewanella frigidimarina (strain NCIMB 400).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=318167;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 400;
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 Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H.,
RA Newman D., Tiedje J.M., Zhou J., Romine M.F., Culley D.E., Serres M.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT "Complete sequence of Shewanella frigidimarina NCIMB 400.";
RL Submitted (AUG-2006) 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; CP000447; ABI72959.1; -; Genomic_DNA.
DR RefSeq; WP_011638565.1; NC_008345.1.
DR AlphaFoldDB; Q07YF5; -.
DR SMR; Q07YF5; -.
DR STRING; 318167.Sfri_3122; -.
DR PeroxiBase; 2663; SfrCP02_NCIMB400.
DR PRIDE; Q07YF5; -.
DR EnsemblBacteria; ABI72959; ABI72959; Sfri_3122.
DR KEGG; sfr:Sfri_3122; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_6; -.
DR OMA; EEIFWGP; -.
DR OrthoDB; 49441at2; -.
DR Proteomes; UP000000684; 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; 2.
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..757
FT /note="Catalase-peroxidase 2"
FT /id="PRO_5000130998"
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 757 AA; 83632 MW; B32EA3AA64FB2459 CRC64;
MKHPLFNQKV LAGFVSMLLI SGSAFASNNE KSEMTKPKGA VGTGVALENQ ARTNQFWWPD
QLNLSALRDH DKRSNPYGEN FDYAKAFNSL DLDKVKLDIN ALLTTSQDWW PSDYSNYGPF
FIRMTWHSAG TYRTLDGRGG AGGGQQRFEP LNSWPDNASL DKARRLLWPI KMKYGEAISW
SDLIVLAGNV SLENMGFKTY GFAGGRHDDW EPDMVYWGPE IEMLASDRED NGGKLQRPLG
ATHMGLIYVN PEGPKGVPDP LGSAKNIRVA FERMAMNDEE TLALIAGGHT FGKMHGAHKP
KDCLGAEPAA AGIEEQGLGW KNKCGKGHSE DTITSGLEGA WTQAPTKWTS LYLSNLLTFE
WKQTRSPAGA IQWIPTDESL HKAVPDAHVK GKFHAPVMTT ADLALKYDPE YRKIAERFLA
DPEEYRLAFA KAWYKLTHRD MGPSRNFLGK EVPKESLIWQ DPIDDKTQSN IDADGVQELK
AQILKSNLTV SELVRVAWAS AASYRHSDMR GGANGARIAL SPQKDWSVNN PAETAKVIKT
LKAIQEDYND SLFSKSKVSL ADLIVLGGTA AIEKAAKDAG FTVSVPFNAG RGDATQAMTD
INAFSLLELT SDGFRNYFDA QQSYKSPVDM LVDKADQLNL SVPEMTVLVG GLRALDANYK
GLKHGVLTST PGTLNNDFFV NLLDMSTVWK KSSTDGIYEG FDRQSGHKKW TATSVDLVFG
SNSELRAVSE VYAFDTSKQK FVEDFAAAWT KVMNLDR
