KATG1_SHEFN
ID KATG1_SHEFN Reviewed; 728 AA.
AC Q082Q2;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 77.
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}; OrderedLocusNames=Sfri_1917;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABI71763.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000447; ABI71763.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041412930.1; NC_008345.1.
DR AlphaFoldDB; Q082Q2; -.
DR SMR; Q082Q2; -.
DR STRING; 318167.Sfri_1917; -.
DR PeroxiBase; 2662; SfrCP01_NCIMB400.
DR PRIDE; Q082Q2; -.
DR EnsemblBacteria; ABI71763; ABI71763; Sfri_1917.
DR KEGG; sfr:Sfri_1917; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_6; -.
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 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 Reference proteome; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CHAIN 17..728
FT /note="Catalase-peroxidase 1"
FT /id="PRO_0000354918"
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; 81314 MW; 8CDEEEF3A613CB6C CRC64;
MDKAQHTQGK CPVAHGGNTT VASDVMEWWP NALNLDILHQ HDNKTNPMDP NFDYREAFKS
LDLSAVKQDL RALMTDSKDW WPADWGHYGG LMIRMAWHSA GTYRMADGRG GAGTGNQRFA
PLNSWPDNAN LDKARRLLWP IKKKYGNKLS WADLIILAGT IAYESMGLKT FGFAGGRADI
WHPEKDIYWG SEKQWLAASD AENSRYSGQR DLENPLAAVM MGLIYVNPEG VDGQPDPLKT
AQDIRVTFER MAMNDEETVA LTAGGHTVGK CHGNGRAENL EAAPEGAELE DQGLGWLNKT
SRGIGRDTVT SGIEGAWTTH PTQWDNGYFE LLLNYDWELK KSPAGAWQWQ PINIKEEHKP
VDVEDPSIRL SPIMTDADMA MKMDPEYRKI SDRFYQDPAY FSEVFARAWF KLTHRDLGPK
SRYLGTDVPA EELIWQDPIP QVDYSLTEQE VTDIKAKILA SGLSIAQLVA TAWDSARTFR
GSDFRGGANG ARIRLAPQKD WQGNEPARLQ KVLAVLATIQ AGLTKSVSIA DLIVLGGTAA
VEKAAHAAGV HVKVPFAAGR GDSTLAQTDV ESFDVLEPLH DAFRNWQKKD YVVQPEEMML
DRTQLMGLTA HEMTVLVGGM RVLGANYDNS KHGVFTDNVG VLSNDFFVNL TDMSYNWKPA
GKNLYHIVDR STDKVKWTAT RVDLVFGSNS ILRSYAEIYA QDDAKEKFVN DFVKTWTKVM
NADRFDLM
