KATG_RHOBA
ID KATG_RHOBA Reviewed; 857 AA.
AC Q7UUW9;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=RB3010;
OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=243090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA Reinhardt R.;
RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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 -!- CAUTION: Differs from other KatG proteins because it has a much longer
CC N-terminus. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX294138; CAD72958.1; -; Genomic_DNA.
DR RefSeq; NP_865274.1; NC_005027.1.
DR RefSeq; WP_011119144.1; NC_005027.1.
DR AlphaFoldDB; Q7UUW9; -.
DR SMR; Q7UUW9; -.
DR STRING; 243090.RB3010; -.
DR PeroxiBase; 2389; RbaCP01_SH1.
DR PRIDE; Q7UUW9; -.
DR EnsemblBacteria; CAD72958; CAD72958; RB3010.
DR KEGG; rba:RB3010; -.
DR PATRIC; fig|243090.15.peg.1394; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_0; -.
DR InParanoid; Q7UUW9; -.
DR OMA; MILAGNC; -.
DR OrthoDB; 49441at2; -.
DR Proteomes; UP000001025; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004096; F:catalase activity; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IBA:GO_Central.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
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.
FT CHAIN 1..857
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354891"
FT ACT_SITE 208
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 371
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 204
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 207..330
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 356)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 330..356
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 207)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 857 AA; 93632 MW; F28CF3153C2D7330 CRC64;
MRLVHGKDAV NALDVSWLSP ILVRDPTSPS ESAWDLFATF MRTRTMKSTA TNMNQHPTTA
QICRRFATRL FRGTVSIRPL TLTLGCLAAS ASASLVAQET ATNAAASQAD AISKCPVMGN
PAGPNRHTVS GAMGNGDWWP NQLNLDMLHQ NSVKSNPMGE DFDYAAAFNS LDLAAVKADI
KELMNTSQDW WPSDYGHYGP LFIRMAWHSA GTYRVSDGRG GASDGTQRFA PLNSWPDNAN
LDKARRLLWP IKQKYGSKIS WADLMVLTGN CALEDMGFET FGFAGGREDV WEPQKDVYWG
PETEWLGDKR YSGDRDLQNP LAAVQMGLIY VNPEGPNGKP DPIAAAKDIR ETFGRMAMND
EETVALIAGG HTFGKAHGAA SPDGNMGVEP EGEGLAAQGL GWINTHGTGN AGDTITSGLE
GAWTSTPAEW SHGYFENLFG YEWKLVKSPA GAWQWTPTDE NAKGTVPDAH DASKSHAPMM
FTTDLALRMD PEYGKISRRF HDNPEQFEKA FAKAWYKLTH RDMGPVSRLL GDSVPEPQLW
QDPIPEATFD VIGSKEIEQL KQKILATNLT SSQLVSTAWA SASTFRNSDM RGGANGARIR
LAPQKDWEVN EPAELASVLT TLEGVQKEFN ASRKDGKQVS MADLIVLGGC AGVEAAAMKA
GHAIQVPFTP GRTDATQEMT DVESFEPLKP IADGFRNYQG HNADRPAEEM LVDKANLLSL
TAPEMTVLVG GMRALDTNAG AGPLADLGKL TKRPGALTND FFVNLLDMNT VWKQSPMCEH
FFEGRDRESG NLKWTASRVD LVFGSNSQLR GIAEVYASED AKEKFVKDFV NAWTKVMNLD
RFDVNDSEST ETQVAAK
