KATG_SHEHH
ID KATG_SHEHH Reviewed; 718 AA.
AC B0TRN5;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Catalase-peroxidase {ECO:0000255|HAMAP-Rule:MF_01961};
DE Short=CP {ECO:0000255|HAMAP-Rule:MF_01961};
DE EC=1.11.1.21 {ECO:0000255|HAMAP-Rule:MF_01961};
DE AltName: Full=Peroxidase/catalase {ECO:0000255|HAMAP-Rule:MF_01961};
GN Name=katG {ECO:0000255|HAMAP-Rule:MF_01961}; OrderedLocusNames=Shal_1888;
OS Shewanella halifaxensis (strain HAW-EB4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=458817;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HAW-EB4;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Kim E., Zhao J.-S., Richardson P.;
RT "Complete sequence of Shewanella halifaxensis HAW-EB4.";
RL Submitted (JAN-2008) 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; CP000931; ABZ76453.1; -; Genomic_DNA.
DR RefSeq; WP_012276985.1; NC_010334.1.
DR AlphaFoldDB; B0TRN5; -.
DR SMR; B0TRN5; -.
DR STRING; 458817.Shal_1888; -.
DR EnsemblBacteria; ABZ76453; ABZ76453; Shal_1888.
DR KEGG; shl:Shal_1888; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_6; -.
DR OMA; MILAGNC; -.
DR OrthoDB; 49441at2; -.
DR Proteomes; UP000001317; 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.
FT CHAIN 1..718
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354919"
FT ACT_SITE 93
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 261
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 89
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 92..220
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 246)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 220..246
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 92)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 718 AA; 80069 MW; 1537EFDAD42FE9E6 CRC64;
MANKKCPVMH GGATEISMSN MEWWPKALNL DILHQHDSKT NPMGAGFNYR EQVKLLDVEA
LKKDLHALMT DSQPWWPADW GHYGGLMIRL SWHAAGTYRT ADGRGGAGRG NQRFAPLNSW
PDNVNLDKAR RLLWPLKKKY GNKLSWADLI AYAGTIAYES MGLKTFGFAF GREDIWHPEK
DIYWGAEKEW LAPSGSEGSR YSGERDLENP LASVMMGLIY VNPEGVDGHP DPLKTANDVR
VTFERMAMND EETVALTAGG HTVGKCHGNG DAELLGPVPE GADVEDQGLG WINKSQRGIG
RDTVSSGLEG AWTTHPTQWD NGYFTLLLNH EWQLNKSPAG AWQWEPINIK EEDKPVDVED
LTQRYNPIMT DADMAMKLDP DYQIISARFD KDPEYFSDVF ARTWFKLTHR DMGPKTRYIG
PDVPAVDLLW QDPVPKGRSD YDVEAVKAQI AASSLSVSDM VTTAWDSART FRGSDLRGGA
NGARIRLAPQ RDWQANEPER LNRVLAVLEP IAAKSGVSVA DVIVLAGNLA VEQAAKAAGF
AIKVPFSPGR GDATADMTDV ESFHVLEPLH DGYRNWLKKD YAVSAEELML DQTQLLGLTA
QEMTVLLGGM RVLGTNYNGE SHGAFTEHQG ALTNDFFVNL TDMNNTWQPV SNNLYEISDR
ETAKLKWTAT RVDLVFGSNS ILRAYAEVYA QDDNQQKFVE DFVTTWAKVM NSDRFDLD
