KATG_SALAI
ID KATG_SALAI Reviewed; 758 AA.
AC A8M0L5;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=Sare_2160;
OS Salinispora arenicola (strain CNS-205).
OC Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC Salinispora.
OX NCBI_TaxID=391037;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNS-205;
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., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Jensen P.R., Moore B.S., Penn K., Jenkins C.,
RA Udwary D., Xiang L., Gontang E., Richardson P.;
RT "Complete sequence of Salinispora arenicola CNS-205.";
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; CP000850; ABV98025.1; -; Genomic_DNA.
DR RefSeq; WP_012182327.1; NC_009953.1.
DR AlphaFoldDB; A8M0L5; -.
DR SMR; A8M0L5; -.
DR STRING; 391037.Sare_2160; -.
DR EnsemblBacteria; ABV98025; ABV98025; Sare_2160.
DR GeneID; 5705616; -.
DR KEGG; saq:Sare_2160; -.
DR PATRIC; fig|391037.6.peg.2185; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_11; -.
DR OMA; EEIFWGP; -.
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..758
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354902"
FT REGION 1..59
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; 82846 MW; E98A606AA35F0D41 CRC64;
MSDTQDNAPA SAQGVDQKAA AGCPVAHDSV TAHGSESESP AIDSPTPHSG GRPRTNRDWW
PNQLDLSVLS TNSAKVNPLG EDFAYAKEFA KLDVEALKRD IVEVLTTSQD WWPADFGHYG
GLMIRLSWHA AGTYRIDDGR GGAGDGGQRF APLNSWPDNV NLDKARRLLW PVKQKYGQKI
SWADLLVLAG NVALESMGFK TFGFGFGRED VWEPEEIFWG SEDTWVGDER YVSEKEFVAG
VGATEMGLIY VNPEGPRGNA DPAAAAHFIR ETFRRMAMDD EETVALIAGG HTFGKTHGAG
IADDHVGPEP EAAPLEAQGL GWMSSYASGA GADAISSGLE VTWTDRPTQW SNRFFEILFA
YEWELTTSPG GAKQWVAKDA EAIIPDAYDA AKKHKPTMLT TDLSLRVDPA YERISRRFLE
NPDEFALAFA KAWYKLLHRD MGPVSRFLGP WVPEPQLWQD PVPAVDHALV GDADIAALKA
KVLQSGLTTA QLVSTAWASA ASFRHTDRRG GANGARVRLE PQRGWEVNQP EQLATVLTTL
EGIQREFNAA GGTKISLADL IVLAGSAAVE KAARDAGFEV TVPFHPGRTD ATQEQTDVES
FQVLEPRADG FRNYLRPGEK AQPEVLLVDR AYMLNLTAPE MTVLIGGLRA LEANVGGSRH
GVLTDRPGVL TNDFFTNLLA LGTRWKASES TEHVYEIRDL ATDTVKWTAS AVDLIFGSNS
QLRALAEVYA SEDAREKFVT DFVAAWTKVM ELDRFDLA
