KATG_SALTO
ID KATG_SALTO Reviewed; 758 AA.
AC A4X6K7;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=Strop_2054;
OS Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / CNB-440).
OC Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC Salinispora.
OX NCBI_TaxID=369723;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-916 / DSM 44818 / CNB-440;
RX PubMed=17563368; DOI=10.1073/pnas.0700962104;
RA Udwary D.W., Zeigler L., Asolkar R.N., Singan V., Lapidus A., Fenical W.,
RA Jensen P.R., Moore B.S.;
RT "Genome sequencing reveals complex secondary metabolome in the marine
RT actinomycete Salinispora tropica.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10376-10381(2007).
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; CP000667; ABP54507.1; -; Genomic_DNA.
DR RefSeq; WP_011905937.1; NC_009380.1.
DR AlphaFoldDB; A4X6K7; -.
DR SMR; A4X6K7; -.
DR STRING; 369723.Strop_2054; -.
DR PRIDE; A4X6K7; -.
DR EnsemblBacteria; ABP54507; ABP54507; Strop_2054.
DR KEGG; stp:Strop_2054; -.
DR PATRIC; fig|369723.5.peg.2107; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_11; -.
DR OMA; EEIFWGP; -.
DR Proteomes; UP000000235; 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..758
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354903"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 129
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 291
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 125
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 128..250
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 276)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 250..276
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 128)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 758 AA; 82880 MW; 8806AAC7990C19F3 CRC64;
MSDTQDNAPV SAQGVDQKAA AGCPVAHDSV TAHGSESESP AIDSPSAVGG GRPRTNRDWW
PNQLDLSVLS TNSAKVNPLG EDFSYAKEFA KLDVEALKRD ITEVLTTSQD WWPADFGHYG
GLMIRLSWHA AGTYRIHDGR GGAGDGGQRF APLNSWPDNV NLDKARRLLW PVKQKYGQKI
SWADLLVLAG NVALESMGFK TFGFGFGRED VWEPEEIFWG PEDTWLGDER YVSEKEFSAG
VGATEMGLIY VNPEGPRGNA DPASAAHFIR ETFRRMAMND EETVALIAGG HTFGKTHGAG
VADDHVGPEP EGAPLEAQGL GWMSSHASGV GADTISSGLE VTWTDRPTQW SNRFFEILFG
YEWELTTSPG GAKQWVAKDA EAIIPDAYDS TKKHKPTMLT TDLSLRVDPA YERISRRFLE
NPDEFALAFA KAWYKLLHRD MGPVSRFLGP WVPQTQLWQD PVPAVDHELV GAADIAALKA
KVLESGLTTT QLVSTAWASA ASFRHTDKRG GANGARIRLE PQRSWEVNQP EQLATVLPAL
EEIQREFNAA GGAKISLADL IVLAGSAAVE KAARDAGVEV TVPFRPGRTD ATQEQTDVDS
FRVLEPRADA FRNYLRPGEK TQPEVLLVDR AYLLNLTAPE MTVLIGGLRA LEANAGGSRH
GVLTDRPGVL TNDFFTNLLA SGARWKASES TEHAYEIRDV ATDKVKWTAS AVDLIFGSNS
QLRALAEVYA SEDAREKFVQ DFVAAWTKVM ELDRFDLA
