ID I0EH19_HELPX Unreviewed; 314 AA.
AC I0EH19;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Catalase-related peroxidase {ECO:0000256|PIRNR:PIRNR000296};
DE EC=1.11.1.- {ECO:0000256|PIRNR:PIRNR000296};
GN ORFNames=HPPC18_02305 {ECO:0000313|EMBL:AFI02238.1};
OS Helicobacter pylori PeCan18.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1163742 {ECO:0000313|EMBL:AFI02238.1, ECO:0000313|Proteomes:UP000005006};
RN [1] {ECO:0000313|EMBL:AFI02238.1, ECO:0000313|Proteomes:UP000005006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PeCan18 {ECO:0000313|EMBL:AFI02238.1,
RC ECO:0000313|Proteomes:UP000005006};
RA Kersulyte D., Ramirez Ramos A., Recarvarren S., Barua R.L., Watanabe J.,
RA Gilman R.H., Berg D.E.;
RL Submitted (APR-2012) 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; CP003475; AFI02238.1; -; Genomic_DNA.
DR RefSeq; WP_000719585.1; NC_017742.1.
DR AlphaFoldDB; I0EH19; -.
DR KEGG; hca:HPPC18_02305; -.
DR PATRIC; fig|1163742.3.peg.475; -.
DR HOGENOM; CLU_045961_2_0_7; -.
DR Proteomes; UP000005006; Chromosome.
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.
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 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..314
FT /note="Catalase-related peroxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003625459"
FT DOMAIN 20..314
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT ACT_SITE 45
FT /evidence="ECO:0000256|PIRSR:PIRSR000296-1"
FT BINDING 306
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 314 AA; 35934 MW; 8B285EDA2B280F67 CRC64;
MKKIGLSLCL VLSLGFLKAH EVSAEEIADI FYKLNAKEPK MKINHTKGFC AKGVFLPNLQ
ARENLEVPLL NEKEIPASVR YSLGGVAMDD KSKVRGMALK LENQNASWTM VMLNTEINFA
KNPKEFAQFF EMRLPKNGKV DEARIKKLYE EVPSYRNFAA YMKTIGISSS VANTPYYSVH
AFKFKDKEEK LLPARWKFVP KDGVKYLNSQ ELKQKDSNYL LSSFQQHLKT KPIEYQMYLV
FANKNDATND TTALWKGKHK ELLVGTLKVE KYEGMGCNKD VYFPADLPKG VEAPTDPLFQ
IRNEVYGITF SRRQ
//