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Database: UniProt/TrEMBL
Entry: D3UIF3_HELM1
LinkDB: D3UIF3_HELM1
Original site: D3UIF3_HELM1 
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
//
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