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Database: UniProt
Entry: A0A1G6V214_9BURK
LinkDB: A0A1G6V214_9BURK
Original site: A0A1G6V214_9BURK 
ID   A0A1G6V214_9BURK        Unreviewed;       352 AA.
AC   A0A1G6V214;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=Catalase-related peroxidase {ECO:0000256|PIRNR:PIRNR000296};
DE            EC=1.11.1.- {ECO:0000256|PIRNR:PIRNR000296};
GN   ORFNames=SAMN05421548_12011 {ECO:0000313|EMBL:SDD47572.1};
OS   Paraburkholderia lycopersici.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=416944 {ECO:0000313|EMBL:SDD47572.1, ECO:0000313|Proteomes:UP000198908};
RN   [1] {ECO:0000313|Proteomes:UP000198908}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TNe-862 {ECO:0000313|Proteomes:UP000198908};
RA   Varghese N., Submissions S.;
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Has an organic peroxide-dependent peroxidase activity.
CC       {ECO:0000256|PIRNR:PIRNR000296}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000296};
CC   -!- SIMILARITY: Belongs to the catalase family.
CC       {ECO:0000256|PIRNR:PIRNR000296}.
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DR   EMBL; FMYQ01000020; SDD47572.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G6V214; -.
DR   STRING; 416944.SAMN05421548_12011; -.
DR   OrthoDB; 255727at2; -.
DR   Proteomes; UP000198908; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004096; F:catalase activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd08153; srpA_like; 1.
DR   Gene3D; 1.20.1280.120; -; 1.
DR   Gene3D; 2.40.180.10; Catalase core domain; 1.
DR   InterPro; IPR018028; Catalase.
DR   InterPro; IPR011614; Catalase_core.
DR   InterPro; IPR020835; Catalase_sf.
DR   InterPro; IPR024168; Catalase_SrpA-type_pred.
DR   PANTHER; PTHR11465; CATALASE; 1.
DR   PANTHER; PTHR11465:SF9; CATALASE; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   PIRSF; PIRSF000296; SrpA; 1.
DR   SMART; SM01060; Catalase; 1.
DR   SUPFAM; SSF56634; Heme-dependent catalase-like; 1.
DR   PROSITE; PS51402; CATALASE_3; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|PIRNR:PIRNR000296, ECO:0000256|PIRSR:PIRSR000296-2};
KW   Iron {ECO:0000256|PIRNR:PIRNR000296, ECO:0000256|PIRSR:PIRSR000296-2};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR000296,
KW   ECO:0000256|PIRSR:PIRSR000296-2};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000296};
KW   Peroxidase {ECO:0000256|PIRNR:PIRNR000296};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          14..352
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   ACT_SITE        61
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000296-1"
FT   BINDING         329
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000296-2"
SQ   SEQUENCE   352 AA;  37860 MW;  251DA304C720815D CRC64;
     MNRPSICVPC RLAAIAAVMG CATAAFAWTA GWLTPKRLSA PHIIDTFESN YGVHTGYRRN
     HAKGLCVEGT FESNGNGARV SRAAVFAPGT TPVIGRFAIP GSNPSAPDAS TPVRSMALLF
     QLQDGEQWRT GMNSTPVFIV RTPNQFFSQL TASKPDPATG KPDPAKLDAF FQANPETQPF
     RDWVKAHAPS SSFANTAFYG INAFIATDAA GNKRAIRWQT VPETAYAPET PAQKADPNFL
     ADDFDARLAA GPLRWRLVLT VAAPGDPTND ATRQWPADRE QIDAGTLVLT RAEPQSDGMC
     RDVNYDPTIL PNGLKPSDDP LLAARSAAYS VSFNRRTREE AGFAQSHGGA QP
//
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