KATG2_SHEAM
ID KATG2_SHEAM Reviewed; 738 AA.
AC A1S3J7;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=Sama_0745;
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; ABL98953.1; -; Genomic_DNA.
DR RefSeq; WP_011758863.1; NC_008700.1.
DR AlphaFoldDB; A1S3J7; -.
DR SMR; A1S3J7; -.
DR STRING; 326297.Sama_0745; -.
DR PeroxiBase; 3598; SamCP01_SB2B.
DR EnsemblBacteria; ABL98953; ABL98953; Sama_0745.
DR KEGG; saz:Sama_0745; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_6; -.
DR OMA; EEIFWGP; -.
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 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..738
FT /note="Catalase-peroxidase 2"
FT /id="PRO_5000205037"
FT ACT_SITE 105
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 267
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 101
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 104..226
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 252)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 226..252
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 104)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 738 AA; 80792 MW; 16A56208A6DDEC69 CRC64;
MKRTLPTLSA LALSMSLALA AGQTQAAETT TNSYWWPEQL DLSPLRQHGS ESNPYGADYD
YAKAFGSLDL VAVKADIKTV LTTSQDWWPA DYGHYGPFFI RMAWHSAGVY RIFDGRGGAS
GGQQRFEPLN SWPDNVNLDK ARRLLWPIKQ KYGSKISWAD LMVLAGNVSL ESMGFKTFGF
AGGRTDDWEA ERVDWGHEKK WLDNKRHNEK GELAKPLGAT QMGLIYVNPE GPNGVPDPLA
AARDIRETFG RMAMNDEETV ALIAGGHTFG KAHGAHDPAK CVGADPAAAG VEAQGLGWKN
KCGKGHSEDT VTSGLEGAWS VSPTQWTMQY LDNLYGFEWV QSKSPAGHIQ WIPANGAGDN
LVPDAHVAGK RHAPIMFTTD IALKEDPSYR EITSRFRKDP KAFELAFAKA WFKLTHRDMG
PKTRYLGSDV PAEALIWQDP IPALDHAVID TNDIAALKSA ILASGIAVPE LVRTAWASAA
SFRGTDMRGG ANGARLRLEP QRSWEVNNPE ELAKVLPKLE KIQKDFNKSL KGGKKVSLAD
VIVLAGGTAI EQAARSAGYS VTVPFTPGRM DATTAQTDVS SFAVLEPKAD AFRNFFSEES
YLPPAEALVE KATQLTLSVP EMTALVGGLR VLDANSNKAK HGVFTDKPGN LSNDFFVNLL
DMSTRWEKSP REAGLYQGFD RQSGKLRWTA TPVDLIFGSH AELRAVAEVY GANDGKDRFV
EDFIAAWTKV MNLDRFDI
