KATG_DESOH
ID KATG_DESOH Reviewed; 732 AA.
AC A9A0F0;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=Dole_1646;
OS Desulfococcus oleovorans (strain DSM 6200 / JCM 39069 / Hxd3).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC Desulfosudaceae; Desulfosudis.
OX NCBI_TaxID=96561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6200 / JCM 39069 / Hxd3;
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., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Wawrik B.,
RA Richardson P.;
RT "Complete sequence of Desulfococcus oleovorans Hxd3.";
RL Submitted (OCT-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; CP000859; ABW67450.1; -; Genomic_DNA.
DR RefSeq; WP_012175066.1; NC_009943.1.
DR AlphaFoldDB; A9A0F0; -.
DR SMR; A9A0F0; -.
DR STRING; 96561.Dole_1646; -.
DR EnsemblBacteria; ABW67450; ABW67450; Dole_1646.
DR KEGG; dol:Dole_1646; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_7; -.
DR OMA; MILAGNC; -.
DR OrthoDB; 49441at2; -.
DR Proteomes; UP000008561; 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..732
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354768"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 93
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 261
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 89
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 92..220
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 246)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 220..246
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 92)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 732 AA; 80818 MW; 7E7AFB4F8E5A2558 CRC64;
MDKDSKRPVV GSTVRGGMSN RDWWPNQLNL SILHQQSNKS NPMGEDFDYA KEFKKLNLAA
VKKDLYALMT DSQEWWPADY GHYGGLFIRM AWHSAGTYRM GDGRGGAGSG SQRLAPLNSW
PDNANLDKAR RLLWPIKKKY GKRISWADLM VLAGNCALES MGFKTFGFAG GREDVWEPET
DIYWGAEEEW LATSDKPKSR YSGDRDLENP LAAVQMGLIY VNPEGPDGNP DPVAAGYDVI
ETFARMAMDP EETVALVAGG HTFGKCHGAG PASHVGPEPE AAPIEAQGLG WKSSFGTGKG
GDTITSGIEG AWKPYPTRWD MGYLKVLFKY EWELVKSPAG AYQWLAMDVD EEDMVIDAHD
PSKKHRPMMT TADLSLRFDP VLGPIAKRFS KNPKAFADAF ARAWFKLTHR DMGPRSRYLG
PEVPKKELIW QDPVPAVNHK LIGARDIAAL KREILASGLS VSQLVYTAWS SAVTFRGSDK
RGGANGARIR LAPQKEWEVN QPAQLKKVLA KLEKIRRAFN SAQSDGKKVS LADLIVLGGC
AAIEQAARNA GYKGTVPFKP GRMDATQKQT DAASFAVLEP LADGFRNYLK AKFTVSAEEL
LIDKARLLTL TAPEMTVLIG GMRVLNANYG QSPHGVFTKR PETLTNDFFV NLLDMGTVWN
PAKADDCVFE GRDRQTGALR WTGTRVDLLF GSNSQLRAIA EVYACKDAGE KFVNDFVAVW
NKVMNADRFD LA
