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Database: UniProt
Entry: A0A0Q3BNS0_9RHOB
LinkDB: A0A0Q3BNS0_9RHOB
Original site: A0A0Q3BNS0_9RHOB 
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
//
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