KATG_CROS8
ID KATG_CROS8 Reviewed; 726 AA.
AC A7MJS4;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=ESA_00379;
OS Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=290339;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-894;
RX PubMed=20221447; DOI=10.1371/journal.pone.0009556;
RA Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L.,
RA Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A.,
RA Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K.,
RA McClelland M., Forsythe S.J.;
RT "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic
RT hybridization analysis with other Cronobacter species.";
RL PLoS ONE 5:E9556-E9556(2010).
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; CP000783; ABU75677.1; -; Genomic_DNA.
DR RefSeq; WP_012123821.1; NC_009778.1.
DR AlphaFoldDB; A7MJS4; -.
DR SMR; A7MJS4; -.
DR EnsemblBacteria; ABU75677; ABU75677; ESA_00379.
DR KEGG; esa:ESA_00379; -.
DR PATRIC; fig|290339.8.peg.341; -.
DR HOGENOM; CLU_025424_2_0_6; -.
DR OMA; MILAGNC; -.
DR OrthoDB; 49441at2; -.
DR Proteomes; UP000000260; 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; 2.
PE 3: Inferred from homology;
KW Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase.
FT CHAIN 1..726
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354771"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 106
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 102
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 105..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 105)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 726 AA; 79422 MW; C2A3533904F6C6CE CRC64;
MSTPSDQHNT LSAGKCPFHQ GNSNQTAGGG TSSRDWWPNQ LRVELLAQHS NRTNPLGDDF
NYRKAFSELD YAALKADLKA LLTDSQPWWP ADWGSYTGLF IRMAWHSAGT YRSADGRGGA
GRGQQRFAPL NSWPDNVSLD KARRLLWPVK QKYGQKISWA DLFILAGNVA LENSGFRTFG
FGAGREDVWE PDMDVNWGDE KNWLEHRHPE SLAQAPLGAT EMGLIYVNPE GPNHSGDPAS
AAPAIRATFG NMGMNDEETV ALIAGGHTLG KTHGAAAANH VGVDPEAAPI EAQGLGWHSS
FGSGAGADAI TSGLEVTWTQ TPTQWSNYFF ENLFKYEWVQ TRSPAGAIQF EAVDAPEIIP
DPFDPSKKRK PTMLVTDLTL RFDPEFEKIS RRFLNDPQAF NEAFARAWYK LTHRDMGPKA
RYIGPEVPKE DLIWQDPLPA AIYQPTQADI DSLKAEIASA GLTVSELISV AWASASTFRG
GDKRGGANGA RLALAPQRDW DVNASAARAL ATLEAIQRTA NKASLADIIV LAGVVGVEQA
AKAAGVEITV PFAPGRVDAR QDQTDVALFE FLKPKADGFR NYRGVRSSTP TESLLIDKAQ
QLTLTAPELT VLVGGMRALG ANYDASAHGV FTDRVGVLST DFFVNLLDMR YEWKATDATA
EVFEGRDRES GEVKYTATRA DLVFGSNSVL RSFAEVYASQ DAHEKFVKDF VAAWTKVMNL
DRFDIQ
