KATG_PSELT
ID KATG_PSELT Reviewed; 726 AA.
AC A8F6I7;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=Tlet_1209;
OS Pseudothermotoga lettingae (strain ATCC BAA-301 / DSM 14385 / NBRC 107922 /
OS TMO) (Thermotoga lettingae).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Pseudothermotoga.
OX NCBI_TaxID=416591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-301 / DSM 14385 / NBRC 107922 / TMO;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Foster B., Bruce D., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K.,
RA Richardson P.;
RT "Complete sequence of Thermotoga lettingae TMO.";
RL Submitted (AUG-2007) 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; CP000812; ABV33771.1; -; Genomic_DNA.
DR RefSeq; WP_012003252.1; NC_009828.1.
DR AlphaFoldDB; A8F6I7; -.
DR SMR; A8F6I7; -.
DR STRING; 416591.Tlet_1209; -.
DR EnsemblBacteria; ABV33771; ABV33771; Tlet_1209.
DR KEGG; tle:Tlet_1209; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_0; -.
DR OMA; MILAGNC; -.
DR OrthoDB; 49441at2; -.
DR Proteomes; UP000002016; 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..726
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354946"
FT ACT_SITE 86
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 249
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 82
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 85..208
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 234)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 208..234
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 85)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 726 AA; 83440 MW; 6D14BB04AD33F5FF CRC64;
MKSKERKSRK RWITDWWPNR LNLKILRQNC SDSNPYGSDY DYLKEVKTLD VDAVIEDLKK
LMKTSQDWWP ADFGHYGPLF IRLSWHSAGS YRIHDGRGGA KNGSIRFPAR INWPDNINLD
KAIRLLWPIK KKYGKKLSWA DLIILAGTVA LQDMGVKILG FSLGREDVFE ADESPDWGAE
QEMLSGKERF KEGELEKPFA ATEMGLIYVN PEGPMGNPDP SGSAKEIRLA FTRMGMNDEE
TVALIAGGHS FGKCHGAGPS KDLGPDPSSS PIEQMGLGWK YTYKTGKASD TYTSGFEVIW
SSKPTKFGIQ YLKFLLEFEW ELEKSPDGKN QWVAKNAPEM IPDPFDPNKK HKPRMLTADL
ALKFDPIYSK IAKKFLENPE EFEKAFAWAW FKLTHRDMGP KSCYIGPYVP REEFIWQDPL
PKRDYELIDE EDIEYLKKQI LNSGINISQL VYTAWSSAST YRDSDRRGGA NGARIRLRPM
NLWEVNHPDD LIKIIKVYEK IQKNFNEEQK NNKKVSIADL IVLGGCAAIE SAAKKAGFDI
RVPFIPGRVD ALQDQVEEEF YREIEPFADG FRNYFKDPYK IDESDISTTP EYFLIDKAQL
LKLTVPELVV IVGGLRVLGA VYSYKNYGVL THTVGTLTND FFVNLLDMNI EWKQIDEHRY
LFEGFNRKTK EPEFKATRVD LIFAHHDELR AVAEVYASDD EKEKFVSDFI KTWDKVMTLD
RFDLKV
