KATG_ACIBY
ID KATG_ACIBY Reviewed; 718 AA.
AC B0V4K1;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=ABAYE3366;
OS Acinetobacter baumannii (strain AYE).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=509173;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AYE;
RX PubMed=18350144; DOI=10.1371/journal.pone.0001805;
RA Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E.,
RA Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J.,
RA Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C.,
RA Weissenbach J., Cruveiller S.;
RT "Comparative analysis of Acinetobacters: three genomes for three
RT lifestyles.";
RL PLoS ONE 3:E1805-E1805(2008).
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; CU459141; CAM88162.1; -; Genomic_DNA.
DR RefSeq; WP_000064284.1; NC_010410.1.
DR AlphaFoldDB; B0V4K1; -.
DR SMR; B0V4K1; -.
DR EnsemblBacteria; CAM88162; CAM88162; ABAYE3366.
DR KEGG; aby:ABAYE3366; -.
DR HOGENOM; CLU_025424_2_0_6; -.
DR OMA; KWTATRM; -.
DR Proteomes; UP000002446; 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 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 3: Inferred from homology;
KW Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase.
FT CHAIN 1..718
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354713"
FT ACT_SITE 99
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 260
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..219
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 245)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 219..245
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 98)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 718 AA; 78629 MW; ADDE8973C4C0D0BA CRC64;
MSNESKCPFS GHNSKPQVTV GGGTANLHWW PNQLRVDLLN QHSERSNPLG KDFNYRQEFK
KLDYYALKAD IKNVLTDSQD WWPADWGNYT GLFIRLAWHA AGTYRMGDGR GGAGRGQQRF
APLNSWPDNA SLDKARRLLW PVKQKYGQKI SWADLFILAG NIALESSGFR TFGFGAGRED
VWEPDNDVNW GDEKEWLAHR NSEALAGSNL AATEMGLIYV NPEGPQASGD PRSAAPFIRA
TFGNMAMDDE EIVALIAGGH TLGKTHGAAP ADHVQADPEG APIEQMGFGW ANSYGTGVGK
DAITSGLEVI WSQTPTQWSN YFFENLFKYE WVQERSPAGA IQWVAADAEA IIPDPFDPSI
KRKPTMLTTD LTLRFDPEFE KISRRFLNDP QAFANAFARA WFKLTHRDMG PKARYLGPEV
PTEDLIWQDP LPAASATPSS ASIADAKAKI VALGLPAGEL VSLAWASAST FRGGDKRGGA
NGARIALSPQ REWEVNKKAV ETLTKIEELK ASTQLSLADL IVLAGNVGVE QAAQAAGFNI
TVPFAPGRVD ALQSQTDVES FQLLLGLADG FRNWKKQGVN TPAEVLLIDK AQQLTLTAPE
LTALIGGLRV LGTNWDGSQH GVFTQQVGVL STDFFTNLLD MSNVWAPVDS TSEVFEGKDR
KSGTVKFTAT RNDLVFGSNS ILRALAEVYA QADGKEKFVQ DFVAAWTKVM NLDRFDLA
