KATG_RHIL3
ID KATG_RHIL3 Reviewed; 726 AA.
AC Q1M498;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
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};
DE Flags: Precursor;
GN Name=katG {ECO:0000255|HAMAP-Rule:MF_01961}; OrderedLocusNames=pRL120362;
OS Rhizobium leguminosarum bv. viciae (strain 3841).
OG Plasmid pRL12.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=216596;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3841;
RX PubMed=16640791; DOI=10.1186/gb-2006-7-4-r34;
RA Young J.P.W., Crossman L.C., Johnston A.W.B., Thomson N.R., Ghazoui Z.F.,
RA Hull K.H., Wexler M., Curson A.R.J., Todd J.D., Poole P.S., Mauchline T.H.,
RA East A.K., Quail M.A., Churcher C., Arrowsmith C., Cherevach I.,
RA Chillingworth T., Clarke K., Cronin A., Davis P., Fraser A., Hance Z.,
RA Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA Rabbinowitsch E., Sanders M., Simmonds M., Whitehead S., Parkhill J.;
RT "The genome of Rhizobium leguminosarum has recognizable core and accessory
RT components.";
RL Genome Biol. 7:R34.1-R34.20(2006).
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; AM236086; CAK12074.1; -; Genomic_DNA.
DR RefSeq; WP_011649134.1; NC_008378.1.
DR AlphaFoldDB; Q1M498; -.
DR SMR; Q1M498; -.
DR STRING; 216596.pRL120362; -.
DR EnsemblBacteria; CAK12074; CAK12074; pRL120362.
DR KEGG; rle:pRL120362; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_5; -.
DR OMA; MILAGNC; -.
DR OrthoDB; 49441at2; -.
DR Proteomes; UP000006575; Plasmid pRL12.
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 Plasmid; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CHAIN 17..726
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354885"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 97
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 259
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 93
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 96..218
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 244)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 218..244
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 96)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 726 AA; 79667 MW; 8FE32360D1A334A8 CRC64;
MDNPTDSAGK CPVAHGNTPR SRSNRDWWPD QLNVQILHQN SGRADPLGQA FDYAEEFKKL
DLDGLKKDLH ALMTDSQDWW PADFGHYGGL FIRMAWHSAG TYRITDGRGG AGAGQQRFAP
LNSWPDNVNL DKARRLLWPI KQKYGNRISW ADLLILTGNV ALESMGFKTF GFAGGRADVW
EPEELYWGPE GTWLGDERYS GERGLAEPLG AVQMGLIYVN PEGPNGTPDP LASARDIRET
FARMAMNDEE TVALIAGGHT FGKTHGAGDP SFVGVDPEGG ELEAQGLGWT SKFNTGVGRD
AIGSGLEVTW TQTPTQWSNY FFENLFAFEW ELTKSPGGAH QWQAKNADAS IPDAYDASKR
HLPTMLTSDL ALRFDPVYEK ISRRFLENPD QFADAFARAW FKLTHRDMGP KVRYLGPEVP
AEDLIWQDVI PAVDHPLVDD KDIADLKEKV LATGLTVQEL VSTAWASAST FRGSDKRGGA
NGARIRLAPQ KDWEVNQPAQ LAKVLGVLEG IQKNFNAAQT GAKKISLADL IVLGGAAGVE
KAAAAGGHAV SVPFTPGRMD ASEAQTDAHS FAALKPRADG FRNYIGGRQF MKPEEALVDR
AQLLTLTGPE MTVLVGGLRV LKAGAPEHGV FTSRPETLTN DFFVNLLDMG TQWSPAAGRD
GVYEGRDRKT NDVKWTGTRV DLIFGSHSQL RAFAEVYGQA DTKEKFVRDF VAAWTKVMNA
DRFDLV
