KATG_GEOSE
ID KATG_GEOSE Reviewed; 735 AA.
AC P14412;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 107.
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}; Synonyms=cat, perA;
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=ATCC 8005 / IAM11001;
RX PubMed=2670897; DOI=10.1128/jb.171.9.4871-4875.1989;
RA Loprasert S., Negoro S., Okada H.;
RT "Cloning, nucleotide sequence, and expression in Escherichia coli of the
RT Bacillus stearothermophilus peroxidase gene (perA).";
RL J. Bacteriol. 171:4871-4875(1989).
RN [2]
RP SEQUENCE REVISION.
RA Trakulnaleamsai S., Aihara S., Miyai K., Suga Y., Yomo T., Negoro S.,
RA Urabe I.;
RL Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9920270; DOI=10.1038/5232;
RA Matsuura T., Miyai K., Trakulnaleaamsai S., Yomo T., Shima Y., Miki S.,
RA Yamamoto K., Urabe I.;
RT "Evolutionary molecular engineering by random elongation mutagenesis.";
RL Nat. Biotechnol. 17:58-61(1999).
RN [4]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18178143; DOI=10.1016/j.abb.2007.12.008;
RA Singh R., Wiseman B., Deemagarn T., Jha V., Switala J., Loewen P.C.;
RT "Comparative study of catalase-peroxidases (KatGs).";
RL Arch. Biochem. Biophys. 471:207-214(2008).
CC -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC peroxidase activity. Also displays NADH oxidase, INH lyase and
CC isonicotinoyl-NAD synthase activities.
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 Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=90 mM for H(2)O(2) for the catalase reaction (at pH 5.5-6.0)
CC {ECO:0000269|PubMed:18178143};
CC KM=3.7 mM for H(2)O(2) for the catalase reaction (at pH 7.0)
CC {ECO:0000269|PubMed:18178143};
CC KM=210 mM for H(2)O(2) for the peroxidase reaction
CC {ECO:0000269|PubMed:18178143};
CC KM=31 mM for ABTS for the peroxidase reaction
CC {ECO:0000269|PubMed:18178143};
CC Vmax=5670 umol/min/mg enzyme for H(2)O(2) for the catalase reaction
CC (at pH 5.5-6.0) {ECO:0000269|PubMed:18178143};
CC Vmax=3410 umol/min/mg enzyme for H(2)O(2) for the catalase reaction
CC (at pH 7.0) {ECO:0000269|PubMed:18178143};
CC Vmax=8 umol/min/mg enzyme for ABTS for the peroxidase reaction
CC {ECO:0000269|PubMed:18178143};
CC pH dependence:
CC Optimum pH is 4.0 for the peroxidase reaction.
CC {ECO:0000269|PubMed:18178143};
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; M29876; AAA22655.1; -; mRNA.
DR EMBL; AB020234; BAA37114.1; -; Genomic_DNA.
DR PIR; JS0520; JS0520.
DR AlphaFoldDB; P14412; -.
DR SMR; P14412; -.
DR PeroxiBase; 2437; GstCP01.
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 1: Evidence at protein level;
KW Direct protein sequencing; Heme; Hydrogen peroxide; Iron; Metal-binding;
KW Oxidoreductase; Peroxidase.
FT CHAIN 1..735
FT /note="Catalase-peroxidase"
FT /id="PRO_0000055567"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 101
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 97
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 100..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 100)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 735 AA; 82989 MW; 7131204A4BFABEF1 CRC64;
MENQNRQNAA QCPFHGSVTN QSSNRTTNKD WWPNQLNLSI LHQHDRKTNP HDEEFNYAEE
FQKLDYWALK EDLRKLMTES QDWWPADYGH YGPLFIRMAW HSAGTYRIGD GRGGASTGTQ
RFAPLNSWPD NANLDKARRL LWPIKKKYGN KISWADLFIL AGNVAIESMG GKTIGFGGGR
VDVWHPEEDV YWGSEKEWLA SERYSGDREL ENPLAAVQMG LIYVNPEGPD GKPDPKAAAR
DIRETFRRMG MNDEETVALI AGGHTFGKAH GAGPATHVGP EPEAAPIEAQ GLGWISSYGK
GKGSDTITSG IEGAWTPTPT QWDTSYFDML FGYDWWLTKS PAGAWQWMAV DPDEKDLAPD
AEDPSKKVPT MMMTTDLALR FDPEYEKIAR RFHQNPEEFA EAFARAWFKL THRDMGPKTR
YLGPEVPKED FIWQDPIPEV DYELTEAEIE EIKAKILNSG LTVSELVKTA WASASTFRNS
DKRGGANGAR IRLAPQKDWE VNEPERLAKV LSVYEDIQRE LPKKVSIADL IVLGGSAAVE
KAARDAGFDV KVPFFPGRGD ATQEQTDVES FAVLEPFADG FRNYQKQEYS VPPEELLVDK
AQLLGLTAPE MTVLVGGLRV LGANYRDLPH GVFTDRIGVL TNDFFVNLLD MNYEWVPTDS
GIYEIRDRKT GEVRWTATRV DLIFGSNSIL RSYAEFYAQD DNQEKFVRDF INAWVKVMNA
DRFDLVKKAR ESVTA
