ID A0A2S4YC62_9ACTN Unreviewed; 738 AA.
AC A0A2S4YC62;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Catalase-peroxidase {ECO:0000256|HAMAP-Rule:MF_01961, ECO:0000256|RuleBase:RU003451};
DE Short=CP {ECO:0000256|HAMAP-Rule:MF_01961};
DE EC=1.11.1.21 {ECO:0000256|HAMAP-Rule:MF_01961, ECO:0000256|RuleBase:RU003451};
DE AltName: Full=Peroxidase/catalase {ECO:0000256|HAMAP-Rule:MF_01961};
GN Name=katG {ECO:0000256|HAMAP-Rule:MF_01961,
GN ECO:0000313|EMBL:POX46472.1};
GN ORFNames=C3489_31750 {ECO:0000313|EMBL:POX46472.1};
OS Streptomyces sp. Ru71.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2080746 {ECO:0000313|EMBL:POX46472.1, ECO:0000313|Proteomes:UP000237414};
RN [1] {ECO:0000313|EMBL:POX46472.1, ECO:0000313|Proteomes:UP000237414}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ru71 {ECO:0000313|EMBL:POX46472.1,
RC ECO:0000313|Proteomes:UP000237414};
RA Suneja G., Sharma R.;
RT "Genome sequencing of cellulose degrading bacteria.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC peroxidase activity. {ECO:0000256|HAMAP-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:0000256|ARBA:ARBA00001378, ECO:0000256|HAMAP-
CC Rule:MF_01961, ECO:0000256|RuleBase:RU003451};
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:0000256|HAMAP-
CC Rule:MF_01961, ECO:0000256|RuleBase:RU003451};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01961};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
CC {ECO:0000256|HAMAP-Rule:MF_01961};
CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01961}.
CC -!- SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01961,
CC ECO:0000256|RuleBase:RU003451}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01961}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:POX46472.1}.
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DR EMBL; PQSS01000081; POX46472.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S4YC62; -.
DR OrthoDB; 9759743at2; -.
DR Proteomes; UP000237414; Unassembled WGS sequence.
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 CDD; cd00649; catalase_peroxidase_1; 1.
DR CDD; cd08200; catalase_peroxidase_2; 1.
DR Gene3D; 1.10.520.10; -; 2.
DR Gene3D; 1.10.420.10; Peroxidase, domain 2; 2.
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 NCBIfam; TIGR00198; cat_per_HPI; 1.
DR PANTHER; PTHR30555:SF0; CATALASE-PEROXIDASE; 1.
DR PANTHER; PTHR30555; HYDROPEROXIDASE I, BIFUNCTIONAL CATALASE-PEROXIDASE; 1.
DR Pfam; PF00141; peroxidase; 2.
DR PRINTS; PR00460; BPEROXIDASE.
DR PRINTS; PR00458; PEROXIDASE.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 2.
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 {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|HAMAP-Rule:MF_01961};
KW Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324, ECO:0000256|HAMAP-
KW Rule:MF_01961};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01961};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01961};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01961};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|HAMAP-
KW Rule:MF_01961}; Reference proteome {ECO:0000313|Proteomes:UP000237414}.
FT DOMAIN 142..429
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 109
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
FT BINDING 272
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:0000256|HAMAP-Rule:MF_01961"
FT SITE 105
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
FT CROSSLNK 231..257
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp-
FT 108)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
SQ SEQUENCE 738 AA; 80721 MW; 6A9EBC1BEFF27157 CRC64;
MSENPDAIVT DPKTEGAGGC PVAHGRAPHP TQGGGNRQWW PERLNLKILA KNPAVANPMG
EDFDYAEAFQ SLDLPAVKRD IAEVLTTSQD WWPADFGHYG PLIIRMAWHS AGTYRISDGR
GGAGAGQQRF APLNSWPDNA NLDKARRLLW PVKKKYGKSL SWADLMILAG NVALESMGFE
TFGFGGGRAD VWEPEEDVYW GPETTWLGDE RYSGDRELEN PLGAVQMGLI YVNPEGPNGN
PDPLAAARDI RETFRRMAMN DEETVALIAG GHTFGKTHGA GPADHVGNDP EAASLEEQGL
GWKSTYGTGK GADTITSGLE VTWTTTPTQW SNGFFKNLFE YEYELTESPA GAKQWVAKDA
PEIVPDAHDP SKKHRPTMLT TDLSLRFDPI YEPISRRFYE NPQEFADAFA RAWYKLTHRD
MGPKSLYLGP EVPEETLIWQ DPLPEAEGEP IGAADIAALK AKLLDSGLTV SQLVSTAWAS
ASTFRGSDKR GGANGARIRL APQRGWEVND PDQRALVLRT LEGIQQEFNT GARKVSLADL
IVLGGCAAVE KAAKDAGFDI EVPFTPGRVD ATEEHTDVES FEALEPTADG FRNYLGKGNR
LPAEYLLLDR ANLLTLSAPE MTVLVGGLRV LGANHQQSQL GVFTKTPGAL TNDFFVNLLD
LGTTWKSTSE DQTTFEGRDA ATGELKWAGS RADLVFGSNS ELRALAEVYA SDDAKEKFVK
DFVAAWDKVM NLDRFDLV
//
