KATG_CHLPB
ID KATG_CHLPB Reviewed; 732 AA.
AC B3EKE9;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=Cphamn1_0152;
OS Chlorobium phaeobacteroides (strain BS1).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=331678;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BS1;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Ovchinnikova G., Li T., Liu Z., Zhao F.,
RA Overmann J., Bryant D.A., Richardson P.;
RT "Complete sequence of Chlorobium phaeobacteroides BS1.";
RL Submitted (JUN-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 ---------------------------------------------------------------------------
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; CP001101; ACE03127.1; -; Genomic_DNA.
DR RefSeq; WP_012473618.1; NC_010831.1.
DR AlphaFoldDB; B3EKE9; -.
DR SMR; B3EKE9; -.
DR STRING; 331678.Cphamn1_0152; -.
DR PeroxiBase; 3650; CphCP01_BS1.
DR KEGG; cpb:Cphamn1_0152; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_10; -.
DR OMA; MILAGNC; -.
DR OrthoDB; 49441at2; -.
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.
FT CHAIN 1..732
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354759"
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; 81607 MW; D4CBAA5E831DD9E9 CRC64;
MSEHSRCPVT GRTAGNPVAG GGIANRDWWP NQLHLDMLHQ HSSLSNPMEE AFKYKEEFGK
LDLKAVKKDL YTLMTDSQEW WPADYGHYGG LFIRMTWHSA GTYRTGDGRG GGGTGNQRFA
PLNSWPDNAN LDKARRLLWP IKQKYGKKLS WADLMILAGN YALESMGFKT FGFGGGRVDI
WEPEEDIYWG KEVEWLDNKR YSGERDLENP LAAVQMGLIY VNPEGPDGKP DPVAAGKDIR
ETFGRMAMND EETVALVAGG HTFGKCHGVG DPKLVGPEPE AADIEEQGLG WKSGYGSGKG
DETMTSGLEG AWTPDPIHWD MGYLGMLFKY EWELTKSPAG AWQWKPTDVA EEDLAPAAHD
PSKRVPTMMT TADLAMRMDP IYGPISRRYY EHPDQFADAF ARAWFKLTHR DMGPKSRYLG
TEVPEEDLIW QDPVPAVDHE LIGDREIAEL KKRLLASGLS IPELVSTAWA SASTFRGSDK
RGGANGARIR LAPQKDWEVN QPEQLKIVLQ KLEEIRQEFN DAQSGGKRVS LADLIVLGGC
AGVEEAARKA GTDVTIPFTP GRTDASQEQT DTESFAVLEP LADGFRNYMK KKYSVSAEEM
LVDRSQLLTL TAPEMTVLVG GLRVLNVNFG QSPHGVFTTL PETLTNDFFV NLLDMGTEWK
PLSKEHDTFE GRDRKTGEPR WTATRVDLIF GSNSRLRAIA EVYGSDNAQE KFVHDFVAAW
NKVMNLDRFE LG
