KATG_SINFN
ID KATG_SINFN Reviewed; 718 AA.
AC Q6W102; C3KPU1;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 3.
DT 03-AUG-2022, entry version 119.
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=NGR_b06410;
GN ORFNames=RNGR00441;
OS Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OG Plasmid sym pNGR234b.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=394;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101917 / NGR234;
RX PubMed=14702322; DOI=10.1128/jb.186.2.535-542.2004;
RA Streit W.R., Schmitz R.A., Perret X., Staehelin C., Deakin W.J., Raasch C.,
RA Liesegang H., Broughton W.J.;
RT "An evolutionary hot spot: the pNGR234b replicon of Rhizobium sp. strain
RT NGR234.";
RL J. Bacteriol. 186:535-542(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101917 / NGR234;
RX PubMed=19376903; DOI=10.1128/aem.00515-09;
RA Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT systems.";
RL Appl. Environ. Microbiol. 75:4035-4045(2009).
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=AAQ87566.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAQ87566.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=ACP22099.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY316747; AAQ87566.1; ALT_FRAME; Genomic_DNA.
DR EMBL; CP000874; ACP22099.1; ALT_FRAME; Genomic_DNA.
DR RefSeq; YP_002822852.1; NC_012586.1.
DR AlphaFoldDB; Q6W102; -.
DR SMR; Q6W102; -.
DR PeroxiBase; 3569; RHspCP01_NGR234.
DR EnsemblBacteria; ACP22099; ACP22099; NGR_b06410.
DR KEGG; rhi:NGR_b06410; -.
DR PATRIC; fig|394.7.peg.1090; -.
DR HOGENOM; CLU_025424_2_0_5; -.
DR OrthoDB; 49441at2; -.
DR Proteomes; UP000001054; Plasmid sym pNGR234b.
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; Reference proteome.
FT CHAIN 1..718
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354888"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 96
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 258
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 92
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 95..217
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 243)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 217..243
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 95)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 718 AA; 79396 MW; 7FE0DE1975427F41 CRC64;
MDQKSDNAGK CPVAHTVPKG RSNRDWWPDQ LDVQVLHQHS GLSDPMGKAF NYAEEFKKLD
LEELKKDLHA LMTESQDWWP ADFGHYGGLF IRMAWHSAGT YRITDGRGGA GQGQQRFAPL
NSWPDNANLD KARRLLWPIK QKYGNRISWA DLMILTGNVA LESMGFQTFG FAGGRADVWE
PQELFWGPEG TWLGDERYSG ERQLDEPLAA VQMGLIYVNP EGPNGNPDPV AAAREIRETF
ARMAMNDEET VALIAGGHTF GKTHGAGDPS FIGPDPEGGA IEDQGLGWKS TFGTGVGKDA
ITGGPEVTWS QTPTRWSNYF FENLFNYEWE LTKSPAGAHQ WKAKNADASI PDAFDASKKH
VPTMLTTDLS LRFDPIYEKI SRRFLENPDQ FADAFARAWF KLTHRDMGPK VRYLGPEVPA
EDLIWQDVIP AVDHKLVDEN DVADLKGKVL ASGLSVQELV STAWASASTF RGSDKRGGAN
GARIRLAPQK DWEVNQPAQL ARVLSVLEGI QKDFNTAHTG GKKISLADLI VLAGAAGVEK
AAKAGGHDIT VPFTPGRADA SEAQTDAASF AALEPRADGF RNYVSRRRRQ FMKPEEALVD
RAQLLTLTAP ELTVLVGGLR VVFTSRPEVL TNDFFVNLLD MGTQWSPMAE KEGVYEGRDR
KTHEVKWTGT RVDLIFGSHS QLRALAEVYA SSDAKEKFVG DFVAAWTKVM NADRFDLV
