ID D3UIF3_HELM1 Unreviewed; 317 AA.
AC D3UIF3;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 24-JAN-2024, entry version 65.
DE RecName: Full=Catalase-related peroxidase {ECO:0000256|PIRNR:PIRNR000296};
DE EC=1.11.1.- {ECO:0000256|PIRNR:PIRNR000296};
GN OrderedLocusNames=HMU10190 {ECO:0000313|EMBL:CBG40276.1};
OS Helicobacter mustelae (strain ATCC 43772 / LMG 18044 / NCTC 12198 / 12198)
OS (Campylobacter mustelae).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=679897 {ECO:0000313|EMBL:CBG40276.1, ECO:0000313|Proteomes:UP000001522};
RN [1] {ECO:0000313|EMBL:CBG40276.1, ECO:0000313|Proteomes:UP000001522}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43772 / LMG 18044 / NCTC 12198 / 12198
RC {ECO:0000313|Proteomes:UP000001522};
RX PubMed=20219135; DOI=10.1186/1471-2164-11-164;
RA O'Toole P.W., Snelling W.J., Canchaya C., Forde B.M., Hardie K.R.,
RA Josenhans C., Graham R.L.J., McMullan G., Parkhill J., Belda E.,
RA Bentley S.D.;
RT "Comparative genomics and proteomics of Helicobacter mustelae, an
RT ulcerogenic and carcinogenic gastric pathogen.";
RL BMC Genomics 11:164-164(2010).
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; FN555004; CBG40276.1; -; Genomic_DNA.
DR RefSeq; WP_013023348.1; NC_013949.1.
DR AlphaFoldDB; D3UIF3; -.
DR STRING; 679897.HMU10190; -.
DR KEGG; hms:HMU10190; -.
DR eggNOG; COG0753; Bacteria.
DR HOGENOM; CLU_045961_2_0_7; -.
DR OMA; KINHTKG; -.
DR Proteomes; UP000001522; 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 SUPFAM; SSF56634; Heme-dependent catalase-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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 Reference proteome {ECO:0000313|Proteomes:UP000001522};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..317
FT /note="Catalase-related peroxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003051755"
FT DOMAIN 45..310
FT /note="Catalase core"
FT /evidence="ECO:0000259|Pfam:PF00199"
FT ACT_SITE 47
FT /evidence="ECO:0000256|PIRSR:PIRSR000296-1"
FT BINDING 309
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 317 AA; 36013 MW; 38F85C7E36E29805 CRC64;
MKKISLSVCA VLFSCMGFAH AHDVSAEGIA DAFYKLNGKD PKMKINHTKG FCTKGVFLSS
QEARDSLDVP LLNQKEIPAF VRYSLGGVEM DDRSKGRGMA LQLEGKGGTW TMVMTNAEIL
FAKNPEEFIQ FLAMRTPKNG KVDEERVKKL SQEVASYRRF DAYMKNVGIT PSVANTPYYS
VHTFMFKDKK TGKMLPAKWK FVPVDGVRYL SNQDLKEKKS DYLLTAFQEH VKTKPIEYKM
YLVFANKNDA INDTTALWKG KHRELYAGTL KIEQYEGMGC NKDVYFPSDL PTGVRPPNDP
LFQIRNEVYG ITFGRRQ
//