KATG2_CELJU
ID KATG2_CELJU Reviewed; 740 AA.
AC B3PEP6;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=CJA_0025;
OS Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp.
OS cellulosa).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=498211;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ueda107;
RX PubMed=18556790; DOI=10.1128/jb.01701-07;
RA DeBoy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H.,
RA Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J.,
RA Nelson K.E.;
RT "Insights into plant cell wall degradation from the genome sequence of the
RT soil bacterium Cellvibrio japonicus.";
RL J. Bacteriol. 190:5455-5463(2008).
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; CP000934; ACE85973.1; -; Genomic_DNA.
DR RefSeq; WP_012485709.1; NC_010995.1.
DR AlphaFoldDB; B3PEP6; -.
DR SMR; B3PEP6; -.
DR STRING; 498211.CJA_0025; -.
DR PRIDE; B3PEP6; -.
DR EnsemblBacteria; ACE85973; ACE85973; CJA_0025.
DR KEGG; cja:CJA_0025; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_6; -.
DR OMA; EEIFWGP; -.
DR OrthoDB; 49441at2; -.
DR Proteomes; UP000001036; 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..27
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CHAIN 28..740
FT /note="Catalase-peroxidase 2"
FT /id="PRO_0000354756"
FT ACT_SITE 107
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 269
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 103
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 106..228
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 254)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 228..254
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 106)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 740 AA; 81550 MW; 2FD3F6FC1791C1DC CRC64;
MFKKTKPRIS ILALTISCAI YSGAALAQDA ANSNKFWWPE QLNLSPLRQH GVESNPMGST
FNYAQAFKKL DLNAVKADIK ALMTQSQDWW PADYGHYGPF FIRMAWHSAG TYRIYDGRGG
AGGGQQRFEP LNSWPDNVNL DRARRLLWPI KQKYGSSISW ADLMVLTGNV ALESMGFKTF
GFAGGRQDDW EADTVYWGPE KKWLDDKRYS GDRTLEKPLA AVQMGLIYVN PEGPNGVPDP
LLAAKDIRDT FGRMAMNDEE TVALIAGGHT FGKAHGAHKP ETCLGKEPAA AGIEEQGLGW
TNKCGKGNAE DTITSGLEGA WSVNPIAWTT QYLDNLFAFE WVQVRSPAGA VQWIPKDGQA
ANLVPDAHDK TKRHAPIMFT TDLALKEDPE YRKISLRFKE NPKEFELAFA KAWFKLTHRD
MGPRVRYLGN EVPGEILLWQ DPVPEVDHPL IDAADITKLK SSLLSSGLSS AELVRTAWAA
AASFRGTDLR GGANGARIRL APQNTWAVNN PRELNRALTR LEKVQGDFNK ASTGGKKVSL
ADVIVLGGVA AVEQAAKKAG YAVEVPFIPG RTDASQAQTD VTSFAVLEPT ADGFRNYYAK
DNTLPPTDML VERANLLTLT VPEMTVLVGG LRVLGANSDA AKNGIFTDKP GTLSNDFFIN
LLDMSTQWRK SAKTGGLYEG LDRKTGKLKW TATPVDLIFG SHSELRAVAE VYAANDGQEK
FVNDFVKAWH KVMMLDRFDW
