ID A0A1V0DGL1_9BACT Unreviewed; 746 AA.
AC A0A1V0DGL1;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=AWN76_014060 {ECO:0000313|EMBL:ARA94166.1};
OS Rhodothermaceae bacterium RA.
OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Rhodothermaceae.
OX NCBI_TaxID=1779382 {ECO:0000313|EMBL:ARA94166.1, ECO:0000313|Proteomes:UP000055617};
RN [1] {ECO:0000313|EMBL:ARA94166.1, ECO:0000313|Proteomes:UP000055617}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RA {ECO:0000313|EMBL:ARA94166.1,
RC ECO:0000313|Proteomes:UP000055617};
RA Liew K.J.;
RT "Complete genome of the potential lignocellulosic biomass degrader
RT Rhodothermaceae bacterium RA isolated from the saline hot spring in
RT Malaysia.";
RL Submitted (MAR-2017) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP020382; ARA94166.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V0DGL1; -.
DR STRING; 1779382.AWN76_014060; -.
DR KEGG; rbar:AWN76_014060; -.
DR OrthoDB; 9759743at2; -.
DR Proteomes; UP000055617; 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 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:UP000055617}.
FT DOMAIN 139..436
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT ACT_SITE 106
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
FT BINDING 275
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 102
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
FT CROSSLNK 234..260
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp-
FT 105)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
SQ SEQUENCE 746 AA; 82260 MW; 4204CE58395AF79B CRC64;
MQANGSPSND TATGRCPVVH TAAGQKHHRG TQNADWWPNA LNLAILHQHS PRANPLGETF
DYARAFQSLD LDAVRRDLFA LMTDSQDWWP ADYGHYGPLF IRLAWHSAGT YRVGDGRGGA
SSGTIRFAPL NSWPDNGNLD KARRLLWPIK KKYGRKLSWA DLIILAGNCA LESMGFKTLG
FAGGREDLYE PEIDIYWGSE TTFHGDPNYE YDKRWTENRE LEHPVGAAEM GLIYVNPQGP
DGKPDPVAAA HDIRETFARM AMNDEETVAL IAGGHTFGKM HGNGDPGLVG PEPEAAPITE
MGLGWKNRNG SGIGVDTFTS GLEGAWTPTP TRWDTSYFDT LFGYEWELTK SPAGAWQWIP
ANGAAAEAVP DAHDPSVRHA PVMATTDLAL IKDPAYLEIS RRFHQNPAEL EEAFARAWYK
LTHRDMGPRS RCLGPLVPDE DFLWQDPIPP VDHALVDADD IAALKAEILA SGLPVSDLVY
TAWSSASTFR GSDKRGGANG ARIRLAPQKD WEVNQPGKLA RVLGVLEGIQ QRFNAAQPGD
KRISLADLIV LAGCAAVEKA AREAGFDVEV PFTPGRTDAS QEQTDVDSFA HLEPMADGFR
NYLAHEYTLS PEALLVDRAQ LLTLSAPEMT VLVGGLRVLN ANYQKRPHGV FTDRPETLTN
DFFVNLLDMS TVWSATDESE TVFEGRDRQT GDLRWTATRV DLVFGSNSQL RAIAEVYACD
DAQETFVRDF VAAWDKVMNL DRFDLA
//
