KATG1_SHEAM
ID KATG1_SHEAM Reviewed; 718 AA.
AC A1SAR6;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
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};
GN Name=katG1 {ECO:0000255|HAMAP-Rule:MF_01961}; OrderedLocusNames=Sama_3270;
OS Shewanella amazonensis (strain ATCC BAA-1098 / SB2B).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=326297;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1098 / SB2B;
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 Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Fredrickson J.,
RA Richardson P.;
RT "Complete sequence of Shewanella amazonensis SB2B.";
RL Submitted (DEC-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; CP000507; ABM01473.1; -; Genomic_DNA.
DR RefSeq; WP_011761377.1; NC_008700.1.
DR AlphaFoldDB; A1SAR6; -.
DR SMR; A1SAR6; -.
DR STRING; 326297.Sama_3270; -.
DR PeroxiBase; 3656; SamCP02_SB2B.
DR PRIDE; A1SAR6; -.
DR EnsemblBacteria; ABM01473; ABM01473; Sama_3270.
DR KEGG; saz:Sama_3270; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_6; -.
DR OMA; MILAGNC; -.
DR OrthoDB; 49441at2; -.
DR Proteomes; UP000009175; 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.
FT CHAIN 1..718
FT /note="Catalase-peroxidase 1"
FT /id="PRO_0000354913"
FT ACT_SITE 94
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 262
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 90
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 93..221
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 247)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 221..247
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 93)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 718 AA; 79499 MW; 4F39F7F993749E34 CRC64;
MSNEGKCPVM HGGATSATQA DNHWWPKALN LDILHQHDSK TNPMAPGFNY REALKGLDVE
ALKQDLKALM TDSQAWWPAD WGHYGGLMIR MAWHSAGTYR IADGRGGGGH GAQRFAPLNS
WPDNGNLDKA RRLLWPIKQK YGNKVSWADL MILAGNMAYE SMGLKTFGFA FGREDIWHPE
KDTYWGAEKE WLAPSGGANS RYSGVRDLQN PLAAVMMGLI YVNPEGVDGN PDPLKTAQDM
RVTFARMAMN DEETVALTAG GHTVGKAHGN GNAANLGPEP EAAPLEEQGF GWMNHQSRGI
GRNTVTSGIE GAWTTHPTRW DNGYFHLLFS YDWALTKSPA GAWQWEPVNI REEDKPVDVE
DPNIRSNPMM TDADMALKMD PDYRRIAERF FHDPDYFADT FARAWFKLTH RDMGPKSRYF
GPDVPAEDLI WQDPVPKGNS QYDPEAVKAR IAGTGLGAAE LVATAWDSAR TYRNSDKRGG
ANGARIRLLP QKDWVANEPA RLARVLELLT PIASDMGVSI ADTLVLGGNL GVELAAKAAG
FNIKVPFIPG RGDASQAQTD IDSFEVLEPL ADGFRNWQKQ DFVVTPEEML LDRAQLMGLS
APEMTVLIGG MRAMAVNHGG TTHGVLTDNP GSLSNDFFVN LTDMSYRWKP VANNLYEICD
RASGQKKWTA TRVDLVFGSN SVLRAYAEYY AQDDNKETFV KDFVTAWCKV MNADRFDA
