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Database: UniProt
Entry: T2SFL7_HELPX
LinkDB: T2SFL7_HELPX
Original site: T2SFL7_HELPX 
ID   T2SFL7_HELPX            Unreviewed;       505 AA.
AC   T2SFL7;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN   ORFNames=L935_03295 {ECO:0000313|EMBL:EQD91387.1};
OS   Helicobacter pylori PZ5086.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=1337395 {ECO:0000313|EMBL:EQD91387.1, ECO:0000313|Proteomes:UP000015855};
RN   [1] {ECO:0000313|EMBL:EQD91387.1, ECO:0000313|Proteomes:UP000015855}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PZ5086 {ECO:0000313|EMBL:EQD91387.1,
RC   ECO:0000313|Proteomes:UP000015855};
RX   PubMed=24051318;
RA   Sheh A., Piazuelo M.B., Wilson K.T., Correa P., Fox J.G.;
RT   "Draft Genome Sequences of Helicobacter pylori Strains Isolated from
RT   Regions of Low and High Gastric Cancer Risk in Colombia.";
RL   Genome Announc. 1:e00736-13(2013).
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=1.11.1.6;
CC         Evidence={ECO:0000256|ARBA:ARBA00000720,
CC         ECO:0000256|RuleBase:RU000498};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|PIRSR:PIRSR038928-2};
CC   -!- SIMILARITY: Belongs to the catalase family.
CC       {ECO:0000256|ARBA:ARBA00005329, ECO:0000256|RuleBase:RU000498}.
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:EQD91387.1}.
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DR   EMBL; ASYW01000199; EQD91387.1; -; Genomic_DNA.
DR   AlphaFoldDB; T2SFL7; -.
DR   PATRIC; fig|1337395.3.peg.1151; -.
DR   Proteomes; UP000015855; Unassembled WGS sequence.
DR   GO; GO:0004096; F:catalase activity; IEA:UniProtKB-EC.
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   CDD; cd08156; catalase_clade_3; 1.
DR   Gene3D; 2.40.180.10; Catalase core domain; 1.
DR   InterPro; IPR018028; Catalase.
DR   InterPro; IPR040333; Catalase_3.
DR   InterPro; IPR024708; Catalase_AS.
DR   InterPro; IPR024711; Catalase_clade1/3.
DR   InterPro; IPR011614; Catalase_core.
DR   InterPro; IPR002226; Catalase_haem_BS.
DR   InterPro; IPR010582; Catalase_immune_responsive.
DR   InterPro; IPR020835; Catalase_sf.
DR   PANTHER; PTHR11465; CATALASE; 1.
DR   PANTHER; PTHR11465:SF61; CATALASE; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   Pfam; PF06628; Catalase-rel; 1.
DR   PIRSF; PIRSF038928; Catalase_clade1-3; 1.
DR   PRINTS; PR00067; CATALASE.
DR   SMART; SM01060; Catalase; 1.
DR   SUPFAM; SSF56634; Heme-dependent catalase-like; 1.
DR   PROSITE; PS00437; CATALASE_1; 1.
DR   PROSITE; PS00438; CATALASE_2; 1.
DR   PROSITE; PS51402; CATALASE_3; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR038928-2};
KW   Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324,
KW   ECO:0000256|RuleBase:RU000498};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR038928-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR038928-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000498};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU000498}.
FT   DOMAIN          9..392
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   ACT_SITE        56
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   ACT_SITE        129
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   BINDING         339
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:PIRSR038928-2"
SQ   SEQUENCE   505 AA;  58631 MW;  46956B5D2EDD8C9D CRC64;
     MVNKDVKQTT AFGAPVWDDN NVITAGPRGP VLLQSTWFLE KLAAFDRERI PERVVHAKGS
     GAYGTFTVTK DITKYTKAKI FSKVGKKTEC FFRFSTVAGE RGSADAVRDP RGFAMKYYTE
     EGNWDLVGNN TPVFFIRDAI KFPDFIHTQK RDPQTNLPNH DMVWDFWSNV PESLYQVTWV
     MSDRGIPKSF RHMDGFGSHT FSLINAKGER FWVKFHFHTM QGVKHLTNEE AAEIRKHDPD
     SNQRDLFNAI ARGDFPKWKL SIQVMPEEDA KKYRFHPFDV TKIWYLQDYP LMEVGIVELN
     KNPENYFAEV EQAAFSPANV VPGIGYSPDR MLQGRLFSYG DTHRYRLGVN YPQIPVNKPR
     CPFHSSSRDG YMQNGYYGSL QNYTPSSLPG YKEDKSARDP KFNLAHIEKE FEVWNWDYRA
     EDSDYYTQPG DYYRSLPADE KERLHDTIGE SLAHVTHKEI VDKQLEHFKK ADPKYAEGVK
     KALEKHQKMM KDMHGKDMHH TKKKK
//
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