KATG_SYNC1
ID KATG_SYNC1 Reviewed; 739 AA.
AC Q3A5D3;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=Pcar_1175;
OS Syntrophotalea carbinolica (strain DSM 2380 / NBRC 103641 / GraBd1)
OS (Pelobacter carbinolicus).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Syntrophotaleaceae; Syntrophotalea.
OX NCBI_TaxID=338963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2380 / NBRC 103641 / GraBd1;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chertkov O., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Pelobacter carbinolicus DSM 2380.";
RL Submitted (OCT-2005) 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}.
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DR EMBL; CP000142; ABA88424.1; -; Genomic_DNA.
DR RefSeq; WP_011340898.1; NC_007498.2.
DR AlphaFoldDB; Q3A5D3; -.
DR SMR; Q3A5D3; -.
DR STRING; 338963.Pcar_1175; -.
DR PeroxiBase; 2668; PcaCP01.
DR EnsemblBacteria; ABA88424; ABA88424; Pcar_1175.
DR KEGG; pca:Pcar_1175; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_7; -.
DR OMA; MILAGNC; -.
DR OrthoDB; 49441at2; -.
DR Proteomes; UP000002534; 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 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;
KW Reference proteome.
FT CHAIN 1..739
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354855"
FT ACT_SITE 100
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 268
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 96
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 99..227
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 253)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 227..253
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 99)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 739 AA; 81032 MW; 23581357C49713CE CRC64;
MSEDSKCPVT GKTAKTAIPM TGRGTTNQDW WPNQLKLNIL HQHSSKSNPM GGDFNYAEEF
KKLDLAAVKQ DLYAMMTDSR EWWPADWGHY GGLLIRMAWH SAGTYRMGDG RGGAGSGSQR
LAPLNSWPDN VNLDKARRLL WPIKQKYGRK ISWADLMVLA GNCALESMGF KTFGFAGGRE
DAWEPEQDIY WGAEEEWLAT SDKPKSRYSG DRDLENPLAA VQMGLIYVNP EGPDGNPDPV
ASGRDVRETF ARMAMNDEET VALVAGGHTF GKCHGAGPAT HVGPEPEAAP IEEQGLGWKS
SFGSGKGGDT ISSGIEGAWK PNPTKWDMGY LKVLFKYEWE KVKSPAGAWQ WLAKDVDEED
MIVGAHDPSK KFRPMMTTAD LSLRFDPIYE PIARRYLENP EEFADAFARA WFKLTHRDMG
PRSRYLGSEV PAEELIWQDP VPAVDHELID AADIADLKVK ILASGLSIPQ LVSTAWASAS
TFRGSDKRGG ANGARIRLAP QKDWEVNQPA QLKTVLQTLE GIQQAFNGAQ AGGKKVSLAD
LIVLGGCAAV EQAAGNAGHD VTVPFTPGRT DATSEQTDVA SFSVLEPVAD GFRNYQKAKF
AVRAEELLVD RAQLLTLTAP EMTVLVGGMR VLNTNHGGTP HGVFTDRPET LTNDFFVNLL
DMGTTWQPTA EDADIFEGCD RATGELKWTG TRIDLVFGSN SQLRAIAEVY GCADSGEKFV
NDFVAVWSKI MNLDRFDLA
