KATG_RHIE6
ID KATG_RHIE6 Reviewed; 728 AA.
AC B3Q4F9;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 73.
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};
GN OrderedLocusNames=RHECIAT_PC0000007;
OS Rhizobium etli (strain CIAT 652).
OG Plasmid pC.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=491916;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIAT 652;
RA Gonzalez V., Acosta J.L., Santamaria R.I., Bustos P.,
RA Hernandez-Gonzalez I.L., Fernandez J.L., Diaz R., Flores M., Mora J.,
RA Palacios R., Davila G.;
RT "Genome diversity and DNA divergence of Rhizobium etli.";
RL Submitted (APR-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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ACE94090.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP001077; ACE94090.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041684052.1; NC_010997.1.
DR AlphaFoldDB; B3Q4F9; -.
DR SMR; B3Q4F9; -.
DR EnsemblBacteria; ACE94090; ACE94090; RHECIAT_PC0000007.
DR KEGG; rec:RHECIAT_PC0000007; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_5; -.
DR Proteomes; UP000008817; Plasmid pC.
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.
FT CHAIN 1..728
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354883"
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 728 AA; 79730 MW; 091272AB6A487A44 CRC64;
MDNPTDTAGK CPVAHGNKPR GPSNRDWWPN QLNVQILHHN SGRADPMGKD FDYAEEFKKL
DLDALKKDLT ALMTDSQDWW PADFGHYGGL FIRMAWHSAG TYRITDGRGG AGQGQQRFAP
LNSWPDNANL DKARRLLWPI KQKYGNRISW ADLLILTGNV ALESMGFKTF GFAGGRADVW
EPEELYWGPE GTWLGDERYS GERQLAEPLG AVQMGLIYVN PEGPGGNPDP LASARDIRET
FARMAMNDEE TVALIAGGHT FGKTHGAGDP SFIGAEPEGG AIEDQGLGWK SSFGSGVGKD
AITAGLEVTW SQTPTKWSNY FFENLFAYEW ELTKSPAGAH QWQAKNAEAS IPDAYEAGKK
HLPTMLTSDL ALRFDPIYEK ISRRFLENPD QFADAFARAW FKLTHRDMGP KVRYLGPEVP
AEDLIWQDVI PAVDHPLVGD KDIAELKAKV LATGLSVQEL VSTAWASAST FRGSDKRGGA
NGARIRLAPQ KDWDANQPAQ LAKVLGVLEG LQKDFNAAQT GGKKISLADM IVLAGAAGVE
KAAAAGGTTV SVPFTPGRMD ASEAQTDAHS FAALEPRIDG FRNYVNDKRL QFMKPEEALV
DRAQLLTLTG PEMTVLVGGL RVLKAGQPEH GVFTARPETL TNDFFVNLLD MATQWVPAAG
KDGVYEGRDR KTGAAKWTGT RVDLIFGSHS QLRAFAEVYG QADAKEKFVK DFVAAWNKVM
NADRFDLV
