KATG1_LEGPN
ID KATG1_LEGPN Reviewed; 721 AA.
AC Q9ZGM4;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Catalase-peroxidase 1 {ECO:0000255|HAMAP-Rule:MF_01961};
DE Short=CP 1 {ECO:0000255|HAMAP-Rule:MF_01961};
DE EC=1.11.1.21 {ECO:0000255|HAMAP-Rule:MF_01961};
DE AltName: Full=Peroxidase/catalase 1 {ECO:0000255|HAMAP-Rule:MF_01961};
GN Name=katG1 {ECO:0000255|HAMAP-Rule:MF_01961}; Synonyms=katB;
OS Legionella pneumophila.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=446;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC STRAIN=JR32;
RX PubMed=9765568; DOI=10.1128/jb.180.20.5369-5374.1998;
RA Bandyopadhyay P., Steinman H.M.;
RT "Legionella pneumophila catalase-peroxidases: cloning of the katB gene and
RT studies of KatB function.";
RL J. Bacteriol. 180:5369-5374(1998).
RN [2]
RP SUBCELLULAR LOCATION.
RC STRAIN=JR32;
RX PubMed=11073912; DOI=10.1128/jb.182.23.6679-6686.2000;
RA Bandyopadhyay P., Steinman H.M.;
RT "Catalase-peroxidases of Legionella pneumophila: cloning of the katA gene
RT and studies of KatA function.";
RL J. Bacteriol. 182:6679-6686(2000).
CC -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC peroxidase activity. {ECO:0000255|HAMAP-Rule:MF_01961,
CC ECO:0000269|PubMed:9765568}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11073912}.
CC -!- INDUCTION: Induced during exponential growth.
CC {ECO:0000269|PubMed:9765568}.
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; AF078110; AAC64361.1; -; Genomic_DNA.
DR RefSeq; WP_015444101.1; NZ_UGOV01000002.1.
DR AlphaFoldDB; Q9ZGM4; -.
DR SMR; Q9ZGM4; -.
DR STRING; 91892.BIZ52_12025; -.
DR eggNOG; COG0376; Bacteria.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 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; PS00436; PEROXIDASE_2; 1.
DR PROSITE; PS50873; PEROXIDASE_4; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase;
KW Peroxidase.
FT CHAIN 1..721
FT /note="Catalase-peroxidase 1"
FT /id="PRO_0000354815"
FT ACT_SITE 99
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 264
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 95
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 98..223
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 249)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 223..249
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 98)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 721 AA; 80500 MW; D96347BDAD0B719C CRC64;
MDGKVGSTTT GCPVIHGGMT STGTSNTAWW PNALNLDILH QHDTKTNPME KDFNYREEVK
KLDFEALKKD LHALMTDSQA WWPADWGHYG GLMIRMSWHA AGSYRVADGR GGAGTGNQRF
APLNSWPDNV NLDKARRLLW PIKKKYGNKI SWADLIVLAG TIAYESMGLK TFGFGFGRED
IWHPEKDVYW GSEQEWLGAK RYDGKSRESL ENPLAAVQMG LIYVNPEGVN GQPDPLRTAQ
DVRVTFGRMA MNDEETVALT AGGHTVGKCH GNGNAKLLGP NPEAANVEDQ GLGWINKTTR
GIGRNTVSSG IEGAWTTHPT QWDNGYFYLL LNYDWELKKS PAGAWQWEPI HIKEEDKPVD
VEDPAIRHNP IMTDADMAMK MDPVYRKIAE RFYQDPDYFA EVFARAWFKL THRDMGPKTR
YIGPDVPKED LIWQDPVPAG NRAYDIAAAK AKIAASNLTI GEMVSTAWDS ARTFRGSDKR
GGANGARIRL KPQKDWEGNE PQRLTKVLQI LEDIATDTGA SVADVIILAG NVGIEKAAKA
AGFDIIVPFA PGRGDATDDM TDAESFDVLE PLHDGYRNWL KKTYDVRPEE LMLDRTQLMG
LTAHEMTVLV GGLRVLGTNH NNTQYGVFTD RVGALTNDFF VNLTDMANVW IPSKDNLYEI
RDRKAGNIKW TATRVDLVFG SNSILRSYAE VYAQDDNKGK FIQDFVAAWT KVMNADRFDL
A
