KATG1_CUPPJ
ID KATG1_CUPPJ Reviewed; 751 AA.
AC Q471D2;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
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}; OrderedLocusNames=Reut_A1635;
OS Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS (strain JMP 134)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=264198;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMP134 / LMG 1197;
RX PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA Kyrpides N.C.;
RT "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT versatile pollutant degrader.";
RL PLoS ONE 5:E9729-E9729(2010).
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; CP000090; AAZ61001.1; -; Genomic_DNA.
DR RefSeq; WP_011297799.1; NC_007347.1.
DR AlphaFoldDB; Q471D2; -.
DR SMR; Q471D2; -.
DR STRING; 264198.Reut_A1635; -.
DR PeroxiBase; 2661; ReCP02_JMP134.
DR PRIDE; Q471D2; -.
DR EnsemblBacteria; AAZ61001; AAZ61001; Reut_A1635.
DR KEGG; reu:Reut_A1635; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_4; -.
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..751
FT /note="Catalase-peroxidase 1"
FT /id="PRO_0000354876"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 104
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 266
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 100
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 103..225
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 251)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 225..251
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 103)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 751 AA; 83059 MW; 927BEE598B274E08 CRC64;
MTDKQHTRSV SESENPAIPS PTPKVSRPRR NKDWWPNQLD LSVLHTHSHL SCPLEEEFDY
ADQFKGLDVD ALKQDLIQLM TTSQDWWPAD YGHYGPLFIR MSWHAAGTYR IADGRGGGGE
GQQRFAPLNS WPDNANLDKA RRLLWPLKKK YGQKVSWADL LIFAGNVAYE SMGFKTFGFG
FGRPDVWEPE DIFWGPEDTW LGDERYSGDR ELAKPLANVQ MGLIYVNPEG PGGNPDPLAA
ARDIRETFAR MAMNDEETVA LIVGGHTVGK THGAAPAAGN VGLEPEGAPI EEQGLGWKNK
FGSGKGSDAI TSGLEGAWTN NPTKWDNGFL ENLFKYEWEL TTSPAGAKQW KPKNPEANDT
VPDAHGASRR HSPTMLTTDL SLRMDPIYGP IAKRFHDNPD QLEDAFAKAW FKLLHRDMGP
RSRYLGPWIP EAQLWQDPIP PVDHELVSEQ DIDALKRTIL GSGLSVPELI STAWGAAASF
RGTDKRGGAN GARIRLAPQK DWESNEPSRL AKVLTALERI QNDFNGSQSG GKKVSLADLI
VLGGCAAVEE AARKAGFNIS VPFAPGRTDA SQEQTDESIF DVLEPIGDAF RNYFRAEDPL
SPETRLLDRA NLLKLTAPQM TVLVGGMRML DANHGQSRHG VFTDKPGTLS NEFFVNLLDI
GTAWRPSVAD KSVYEGIDRT SGKTRWTATA ADLVFGAHSQ LRALAEVYAC DDGKERFVRD
FVAAWNKVMN LDRYDLLGTR NGRRAVTSKP V
