ID A0A0Q6VEW1_9ACTN Unreviewed; 760 AA.
AC A0A0Q6VEW1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 37.
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 ORFNames=ASC64_00050 {ECO:0000313|EMBL:KQV77291.1};
OS Nocardioides sp. Root122.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736431 {ECO:0000313|EMBL:KQV77291.1, ECO:0000313|Proteomes:UP000051395};
RN [1] {ECO:0000313|EMBL:KQV77291.1, ECO:0000313|Proteomes:UP000051395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root122 {ECO:0000313|EMBL:KQV77291.1,
RC ECO:0000313|Proteomes:UP000051395};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQV77291.1, ECO:0000313|Proteomes:UP000051395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root122 {ECO:0000313|EMBL:KQV77291.1,
RC ECO:0000313|Proteomes:UP000051395};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQV77291.1}.
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DR EMBL; LMDE01000001; KQV77291.1; -; Genomic_DNA.
DR RefSeq; WP_056905491.1; NZ_LMDE01000001.1.
DR AlphaFoldDB; A0A0Q6VEW1; -.
DR STRING; 1736431.ASC64_00050; -.
DR OrthoDB; 9759743at2; -.
DR Proteomes; UP000051395; 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:UP000051395}.
FT DOMAIN 163..479
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 130
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
FT BINDING 292
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 126
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
FT CROSSLNK 251..277
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp-
FT 129)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
SQ SEQUENCE 760 AA; 83558 MW; 5512123F4F184127 CRC64;
MTDNQDSSAP ESPQGVDRKA ESGCPVMHDS ATAQGSESEN PAIDSPEPKT GGRPHGLKDW
WPNMLDLSVL HAHSPKGNPL GADFDYAKAF EGLDVEALKR DLVEVMHTSQ DWWPADFGHY
GGLFVRMSWH AAGTYRIYDG RGGAGDGGQR FAPLNSWPDN ANLDKARRLL WPVKQKYGQK
ISWADLLVLA GTVAMEDMGF ENFGFAFGRQ DVWEPEEIFW GPEDTWLGDE RYTDERTLEE
SLGAVQMGLI YVNPEGPNGN PDPVASARDI RDTFARMAMN DEETVALIAG GHTFGKTHGA
GDADLVGPEP EGAPLENQGL GWKSEYGSGK AGDTITSGLE VTWTYHPTRW DNEFFHILYA
YDWELMESPA GAHQWRPKNG AGSDMVPGAH EGDPRREPRM LTSDLALRFD PEYDKISRRF
KENPEEFRLA FAKAWYKLLH RDMGPVSRYL GPWVPEAQLW QDPVPAVEGE LVSDADVATL
KDAVLGSGLS VADLVSTAWA SAATFRTTDK RGGANGARIR LEPQRGWAVN QPEQLERVLA
ALESVRDDFN GRGGAQVSLA DLIVLGGSAA IEKAARDAGV EVTVPFHPGR TDATQEQTDV
DSFRVLEPRA DGFRNYVRPG EKLQPEKLLV DRAYMLGLSA PQMTALVGGL RAIGTNHGGT
AHGVLTDRPG VLSNDFFVNL LSPGTQWKVS QQEENVYEIQ DLDGTVKWTA TPVDLVFGSN
SQLRALAEVY ASDDATEKFV HDFVAAWTHV MDNDRFDLHA
//
