KATG1_SHESA
ID KATG1_SHESA Reviewed; 728 AA.
AC A0KRY0;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Catalase-peroxidase 1 {ECO:0000255|HAMAP-Rule:MF_01961};
DE Short=CP 1 {ECO:0000255|HAMAP-Rule:MF_01961};
DE EC=1.11.1.21 {ECO:0000255|HAMAP-Rule:MF_01961};
DE AltName: Full=Peroxidase/catalase 1 {ECO:0000255|HAMAP-Rule:MF_01961};
DE Flags: Precursor;
GN Name=katG1 {ECO:0000255|HAMAP-Rule:MF_01961};
GN OrderedLocusNames=Shewana3_0306;
OS Shewanella sp. (strain ANA-3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=94122;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANA-3;
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 Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Newman D.,
RA Salticov C., Konstantinidis K., Klappenback J., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Shewanella sp. ANA-3.";
RL Submitted (SEP-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; CP000469; ABK46549.1; -; Genomic_DNA.
DR RefSeq; WP_011715540.1; NC_008577.1.
DR AlphaFoldDB; A0KRY0; -.
DR SMR; A0KRY0; -.
DR STRING; 94122.Shewana3_0306; -.
DR PeroxiBase; 3616; SHspCP01_ANA-3.
DR EnsemblBacteria; ABK46549; ABK46549; Shewana3_0306.
DR KEGG; shn:Shewana3_0306; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_6; -.
DR OMA; MILAGNC; -.
DR OrthoDB; 49441at2; -.
DR Proteomes; UP000002589; 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 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; 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 Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CHAIN 23..728
FT /note="Catalase-peroxidase 1"
FT /id="PRO_0000354923"
FT ACT_SITE 98
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 266
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 94
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 97..225
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 251)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 225..251
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 97)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 728 AA; 81113 MW; 285760B6474BB5B4 CRC64;
MDKTQSSQGK CPVMHGANSA VASNNMDWWP KALNLDILHQ HDKKTDPMDP KFNYRDAFNS
LDLAAVKRDL NALMTDSQDW WPADWGHYGG LMIRMAWHSA GTYRVADGRG GAGTGNQRFA
PLNSWPDNAN LDKARRLLWP IKKKYGNKLS WADLMILAGN VAYESMGLKT YGFAGGREDI
WHPEKDIYWG SEKQWLAPTE NPNSRYSGER DLENPLAAVM MGLIYVNPEG VDGKPDPLRT
AQDVRVTFAR MAMNDEETVA LTAGGHTVGK CHGNGKAQDL GPEPEGEELE AQGLGWLNKK
GPGTGANAVT SGLEGAWTTH PTQWDNGYFH LLLNYDWELK KSPAGASQWE PINIKEEDKV
VSVGDPNRKF NPIMTDADMA MKMDPEYRKI SEKFYQDPAY FSEVFARAWF KLTHRDLGPK
SRYLGPEVPN EDLLWQDPIP SVDYRLDASE IVELKAKLLA SGLSVSDLVA TAWDSARTFR
GSDFRGGANG ARIRLAPQKD WQANEPERLQ KVLKVLIELQ ASLSKKVSIA DLIVLGGAAA
IEKAAHAAGV KITVPFIPGR GDATQEMTDV ESFAVLEPLH DAYRNWQKKD YVVQPEEMML
DRTQLMGLTA HEMTVLIGGM RVLGTNYGGT RHGVFTDKVG VLTNDFFVNL TDMAYNWKPA
GSNLYEIVER KTGAVKWTAT RVDLVFGSNS ILRSYAEVYA QDDAKEKFVH DFVAAWTKVM
NADRFDLA
