KATG_CHLPD
ID KATG_CHLPD Reviewed; 732 AA.
AC A1BEI1;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=Cpha266_0755;
OS Chlorobium phaeobacteroides (strain DSM 266).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=290317;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 266;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.,
RA Schmutz J., Larimer F., Land M., Hauser L., Mikhailova N., Li T.,
RA Overmann J., Bryant D.A., Richardson P.;
RT "Complete sequence of Chlorobium phaeobacteroides DSM 266.";
RL Submitted (DEC-2006) 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}.
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DR EMBL; CP000492; ABL64808.1; -; Genomic_DNA.
DR RefSeq; WP_011744637.1; NC_008639.1.
DR AlphaFoldDB; A1BEI1; -.
DR SMR; A1BEI1; -.
DR STRING; 290317.Cpha266_0755; -.
DR PeroxiBase; 2369; CphCP01_DSM266.
DR EnsemblBacteria; ABL64808; ABL64808; Cpha266_0755.
DR KEGG; cph:Cpha266_0755; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_10; -.
DR OMA; MILAGNC; -.
DR OrthoDB; 49441at2; -.
DR Proteomes; UP000008701; Chromosome.
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 Reference proteome.
FT CHAIN 1..732
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354760"
FT ACT_SITE 98
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 261
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 94
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 97..220
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 246)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 220..246
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 97)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 732 AA; 81551 MW; C5EF26974D8212EF CRC64;
MSEQSKCPVT GRTAGNPVAG GSMLNRDWWP NQLHLDMLHQ HSSLVNPMGD EFRYKEEFRK
LDLGAVKKDL YALMTDSQEW WPADYGHYGG LFIRMAWHSA GTYRTSDGRG GGGRGNQRFA
PLNSWPDNAN LDKARRLLWP IKQKYGKMLS WADLMILAGN CALESMGFKT FGFGGGRVDI
WEPEEDIYWG KEVEWLGNNR YSGERDLENP LAAVQMGLIY VNPEGPDGNP DPVAAGRDIR
ETFARMAMND EETVALVAGG HTFGKCHGVG DPNLIGPEPE AAGIEEQGLG WKSGYGSGKG
DETMTSGLEG AWTPDPIHWD MGYLGMLFKY EWELTKSPAG AWQWKPKDVA EEDLAPAAHD
PSKRVPTMMT TADLAMRMDP VYGPISRRYY EHPDQFADAF ARAWFKLTHR DMGPKSRYLG
AEVPAEDLIW QDPVPAVDHE LIGEGEIAEL KKRLLASGLP IPELVSTTWA SASTFRGSDK
RGGANGSRIR LAPQKDWEVN QPEQLQRVLE KLEEIRHAFN GEQSGGKRVS LADLIVLGGC
AAVEEAARRA GNDVTIPFAP GRTDASQAET DVESFAVLEP LADGFRNYAR QKYSVTPEEM
LVDRSQLLTL TATEMTVLLG GLRVLGANFR QSPHGVFTKR HETLTNDFFV NLLDMGTEWK
PVSKEHDTFE GRDRKTGEPR WSATRVDLIF GSNARLRAIA EVYGSDDAQE KFVQDFVAAW
NKVMNLDRFE IS
