ID A0A1G7BIU0_9PROT Unreviewed; 745 AA.
AC A0A1G7BIU0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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};
DE Flags: Precursor;
GN Name=katG {ECO:0000256|HAMAP-Rule:MF_01961};
GN ORFNames=SAMN04488071_2537 {ECO:0000313|EMBL:SDE26969.1};
OS Kordiimonas lacus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Kordiimonadales;
OC Kordiimonadaceae; Kordiimonas.
OX NCBI_TaxID=637679 {ECO:0000313|EMBL:SDE26969.1, ECO:0000313|Proteomes:UP000183685};
RN [1] {ECO:0000313|EMBL:SDE26969.1, ECO:0000313|Proteomes:UP000183685}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.9109 {ECO:0000313|EMBL:SDE26969.1,
RC ECO:0000313|Proteomes:UP000183685};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNAK01000005; SDE26969.1; -; Genomic_DNA.
DR RefSeq; WP_068307745.1; NZ_LRUA01000007.1.
DR AlphaFoldDB; A0A1G7BIU0; -.
DR STRING; 637679.GCA_001550055_03702; -.
DR OrthoDB; 9759743at2; -.
DR Proteomes; UP000183685; 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:UP000183685};
KW Signal {ECO:0000256|HAMAP-Rule:MF_01961, ECO:0000256|RuleBase:RU003451}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961,
FT ECO:0000256|RuleBase:RU003451"
FT CHAIN 20..745
FT /note="Catalase-peroxidase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961,
FT ECO:0000256|RuleBase:RU003451"
FT /id="PRO_5009999737"
FT DOMAIN 122..438
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT REGION 362..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 115
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
FT BINDING 278
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 111
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
FT CROSSLNK 237..263
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp-
FT 114)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
SQ SEQUENCE 745 AA; 81590 MW; EB034D6AA702476C CRC64;
MLKRKLPMIV ILAMGTALAT APQAAAEHHE PMETHMQSAP TNDYWWPNRL NLEPLRLNLP
DANPLGADFN YAEAFKDVDL DELRADMEKL MTTSQDWWPA DYGHYGPFFI RLSWHSAGTY
RMIDGRGGAD GGMHRFAPLN SWPDNTNLDK AQRLLWPIKQ KYGNKISWSD LIVLAGTIGM
EHMGFKTAGF AFGREDAWMP EEVNWGPEGE WLGRAESRHK DGKLTGSLSA ARMGLIYVNP
EGPNGVPDPL LAAQEIRDTF GRMAMNDEET VALIAGGHTF GKAHGASKGS NLGAEPEGAS
LEEQGLGWKN KYGSGKGADT ITSGLEGAWT VSPAEWTHNY LQNLFMFDWV QTKSPAGAIQ
WEPSDDSTSE MVPDAHDPDK RHKPIMFTTD LALKEDPAYR KVSERFLENP EEFEQAFARA
WFKLTHRDMG PTSRYLGDWA PDETYIWQDP VPAVDHKLVS KSDADKLKKV ILESGLSHAD
LVRTAWASAS SFRGTDMRGG ANGARVRLAP QKDWAANDPA ELDRVLGVLA GIQADFNKKA
SGGKKISLAD LIVLGGAAAI EDAAAKAGHK VSVPFKPGRT DATAEMTDAD SFSVLEPTAD
GFRNYFADGN DRSPAEMLVE KAALLKLSVP EMTVLVGGLR ALDANTGGAK HGVFTNTPGV
LTNDFFTGLL DMGTEWKKAD TAGIYEGFDR VSGEKKWSAT PVDLIFGSNS ELRAVAEVYA
TDGSEAKFVE DFIGAWTKVM NLDRF
//
