KATG_BRADU
ID KATG_BRADU Reviewed; 779 AA.
AC Q89WB4;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=blr0778;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
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; BA000040; BAC46043.1; -; Genomic_DNA.
DR RefSeq; NP_767418.1; NC_004463.1.
DR AlphaFoldDB; Q89WB4; -.
DR SMR; Q89WB4; -.
DR STRING; 224911.27349027; -.
DR PeroxiBase; 2347; BjaCP01_USDA110.
DR EnsemblBacteria; BAC46043; BAC46043; BAC46043.
DR KEGG; bja:blr0778; -.
DR PATRIC; fig|224911.5.peg.802; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_5; -.
DR InParanoid; Q89WB4; -.
DR OMA; MILAGNC; -.
DR PhylomeDB; Q89WB4; -.
DR Proteomes; UP000002526; 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..779
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354727"
FT ACT_SITE 149
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 311
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 145
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 148..270
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 296)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 270..296
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 148)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 779 AA; 85664 MW; 7BF99C75572BB055 CRC64;
MAVTRQRVEI PELAHRHVDH QKILSQRSLK STSPDGMRGL EWFYLVKGAS STPPEEVFMD
DTSKCPFSGG KRVPANRDWW PTQLSIEMLH KNSGLSDPMG EEFDYAKEFK TLDLNAVIKD
LTALMTDSQE WWPADFGHYG GLMIRMAWHS AGTYRITDGR GGAGAGQQRF APLNSWPDNA
NLDKARRLLW PIKQKYGRKI SWADLMVLAG NVALESMGFK TFGFAGGRAD VWEPEELYWG
PEGTWLGDER YSGERQLAEP LGAVQMGLIY VNPEGPNGKP DPIAAAKDIR ETFFRMAMND
EETVALIAGG HTFGKTHGAG DPSLVGPEPE AGALEDQGLG WKSKHASGLA GDSITSGLEV
TWTTTPTKWS NNFFENLFKY EWELTKSPGG ANQWTAKGAE AIIPDAFDKS KKHRPTMLTT
DLSLRLDPAY EKISRRFLEN PDQFADAFAR AWFKLTHRDM GPIQRYLGPL VPKETLIWQD
PIPAVNHELV SDQDIAALKT KILASGLSVP ELVSTAWASA STFRGSDKRG GANGARIRLS
PQKDWEVNQP AQLSKVLGKL EAIQKEFNAS AGAKKVSLAD LIVLGGTAAV EKAAKDAGVD
VKVAFTPGRM DASQEQTDAA SFAPLEPRAD GFRNYVGKRQ QFLQQEEALV DRAQLLKLTG
PELTVLVGGL RVLGANANGS KHGVLTAKVG ALSNDFFVNL LDMSTQWAPA ADGTYEARDR
KTNAVKWTGT RADLIFGAHS QLRAYAEVYA TSDSKEQFVK DFAKAWTKVM NLDRFDLAA
