ID A0A0Q3BNS0_9RHOB Unreviewed; 768 AA.
AC A0A0Q3BNS0;
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=AN189_04965 {ECO:0000313|EMBL:KQI69729.1};
OS Loktanella sp. 3ANDIMAR09.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Loktanella.
OX NCBI_TaxID=1225657 {ECO:0000313|EMBL:KQI69729.1, ECO:0000313|Proteomes:UP000051463};
RN [1] {ECO:0000313|EMBL:KQI69729.1, ECO:0000313|Proteomes:UP000051463}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3ANDIMAR09 {ECO:0000313|EMBL:KQI69729.1,
RC ECO:0000313|Proteomes:UP000051463};
RA Mas-Llado M., Nogales B., Bosch R.;
RT "Draft genome sequence of Loktanella sp. 3ANDIMAR09.";
RL Submitted (SEP-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:KQI69729.1}.
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DR EMBL; LJAK01000002; KQI69729.1; -; Genomic_DNA.
DR RefSeq; WP_056031890.1; NZ_LJAK01000002.1.
DR AlphaFoldDB; A0A0Q3BNS0; -.
DR STRING; 1225657.AN189_04965; -.
DR PATRIC; fig|1225657.3.peg.1013; -.
DR OrthoDB; 9759743at2; -.
DR Proteomes; UP000051463; 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 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; 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; PS50873; PEROXIDASE_4; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|HAMAP-Rule:MF_01961, ECO:0000256|RuleBase:RU003451};
KW Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324, ECO:0000256|HAMAP-
KW Rule:MF_01961};
KW Iron {ECO:0000256|HAMAP-Rule:MF_01961, ECO:0000256|RuleBase:RU003451};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01961,
KW ECO:0000256|RuleBase:RU003451};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01961,
KW ECO:0000256|RuleBase:RU003451};
KW Peroxidase {ECO:0000256|HAMAP-Rule:MF_01961,
KW ECO:0000256|RuleBase:RU003451};
KW Reference proteome {ECO:0000313|Proteomes:UP000051463}.
FT DOMAIN 152..451
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 101
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
FT BINDING 289
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 97
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
FT CROSSLNK 248..274
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp-
FT 100)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
SQ SEQUENCE 768 AA; 84068 MW; F45422800A86628B CRC64;
MKDHAATQGA CPFRGTRIGG AQGSEPNVNH WWPNRLKVEA LYQDPPQANA LGRDFDYAAA
NAKIDHKALW EDVRAFLHTP VDWWPSDYGH YGPQMNRMSW HSAGTYRIAD GRGGAGEGMQ
RFAPINSWWD NGNTDKSRRL LAPIKAKYGA GLSWADLIAL AGTVALEDMG LPVQGFAYGR
EDAWSADVNT YWGPEGWFGK PPSEQPADPQ LGHPEQMVNR GLRWEGGPKD DHYDLENPLA
ASHQSLIYVD PEGPGGNGDP MDAARDIRET FARMAMNDEE TLALVAGGHA FGKSHGAVPA
SEIGGAPEIA KMSEQGLGWS NPVGSGNAEH TMTNGIEGSW TPNPTQWDND YLTNLFKFEW
EQTKSPAGAL QWTPTDPDAP KTPDAHLPGV MNPLMMMTTD IAFKVDPAYR KIAERFLEDF
DYFTETFSKA WHKLMHRDLG PTSRWLGPDQ GGTFIWQDPV PEVDHPLIDA TQIADLKARA
LDLDVAATDL IAAAWAAAST YRDSDKRGGA NGARVQLAPQ RGWAVNNPAR LDRVLDALTG
LKSDFDAEGA AKVSMADLIV LAGCAGVEAA AKAGGHDVTV PFVPGRTDAT ADMTDDESFE
WLRPVVDGFR NYVDDAVGYN VPPEQIALDK AALLSLSAPE WTALTGGLRV LDQNWDGSDK
GVFTDRPGTL SADFFRELVS TDLDWRPETD AETAFDLVDR ATGQTRWHAT RLDLVFGANA
ELRQISELYA GVDGEGYFVD TFVRAWHKVM MLDRFDAKAE RKAAVSDC
//