GenomeNet

Database: UniProt
Entry: T0F3Z5_HELPX
LinkDB: T0F3Z5_HELPX
Original site: T0F3Z5_HELPX 
ID   T0F3Z5_HELPX            Unreviewed;       505 AA.
AC   T0F3Z5;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN   ORFNames=N207_08085 {ECO:0000313|EMBL:EPZ92826.1};
OS   Helicobacter pylori UM114.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=1355531 {ECO:0000313|EMBL:EPZ92826.1, ECO:0000313|Proteomes:UP000015605};
RN   [1] {ECO:0000313|EMBL:EPZ92826.1, ECO:0000313|Proteomes:UP000015605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UM114 {ECO:0000313|EMBL:EPZ92826.1,
RC   ECO:0000313|Proteomes:UP000015605};
RX   PubMed=24051312;
RA   Rehvathy V., Tan M.H., Gunaletchumy S.P., Teh X., Wang S., Baybayan P.,
RA   Singh S., Ashby M., Kaakoush N.O., Mitchell H.M., Croft L.J., Goh K.L.,
RA   Loke M.F., Vadivelu J.;
RT   "Multiple genome sequences of Helicobacter pylori strains of diverse
RT   disease and antibiotic resistance backgrounds from malaysia.";
RL   Genome Announc. 1:E00687-E00713(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:EPZ92826.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AUSS01000017; EPZ92826.1; -; Genomic_DNA.
DR   RefSeq; WP_021310146.1; NZ_AUSS01000017.1.
DR   AlphaFoldDB; T0F3Z5; -.
DR   PATRIC; fig|1355531.3.peg.934; -.
DR   Proteomes; UP000015605; 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;  58692 MW;  E0E492805C3363FE CRC64;
     MVNKDVKQTT AFGTPVWDDN NVITAGPRGP VLLQSTWFLE KLAAFDRERI PERVVHAKGS
     GAYGTFTVTK DITKYTKAKI FSKVGKKTEC FFRFSTVAGE RGSADAVRDP RGFAMKYYTE
     EGNWDLVGNN TPVFFIRDAI KFPDFIHTQK RDPQTNLPNH DMVWDFWSNV PESLYQVTWV
     MSDRGIPKSF RHMDGFGSHT FSLINAKGER FWVKFHFHTM QGVKHLTNEE AAEIRKHDPD
     SNQRDLFDAI ARGDFPKWKL SIQVMPEEDA KKYRFHPFDV TKIWYLQDYP LMEVGIVELN
     KNPENYFAEV EQAAFTPANV VPGIGYSPDR MLQGRLFSYG DTHRYRLGVN YPQIPVNKPR
     CPFHSSSRDG YMQNGYYGSL QNYTPSSLPG YKEDKSARDP KFNLAHIEKE FEVWNWDYRA
     DDSDYYTQPG DYYRSLPADE KERLHDTIGE SLAHVTHKEI VDKQLEHFKK ADPKYAEGVK
     KALEKHQKMM KDMHGKDMHH MKKKK
//
DBGET integrated database retrieval system