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Database: UniProt
Entry: V6L769_HELPX
LinkDB: V6L769_HELPX
Original site: V6L769_HELPX 
ID   V6L769_HELPX            Unreviewed;       505 AA.
AC   V6L769;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN   ORFNames=N871_06090 {ECO:0000313|EMBL:EST40197.1};
OS   Helicobacter pylori X47-2AL.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=1386083 {ECO:0000313|EMBL:EST40197.1, ECO:0000313|Proteomes:UP000017937};
RN   [1] {ECO:0000313|EMBL:EST40197.1, ECO:0000313|Proteomes:UP000017937}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=X47-2AL {ECO:0000313|EMBL:EST40197.1,
RC   ECO:0000313|Proteomes:UP000017937};
RX   PubMed=24356847;
RA   Veyrier F.J., Ecobichon C., Boneca I.G.;
RT   "Draft Genome Sequence of Strain X47-2AL, a Feline Helicobacter pylori
RT   Isolate.";
RL   Genome Announc. 1:e01095-13(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:EST40197.1}.
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DR   EMBL; AWNG01000022; EST40197.1; -; Genomic_DNA.
DR   RefSeq; WP_000247370.1; NZ_AWNG01000022.1.
DR   AlphaFoldDB; V6L769; -.
DR   SMR; V6L769; -.
DR   PATRIC; fig|1386083.3.peg.1226; -.
DR   Proteomes; UP000017937; 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;  58629 MW;  9F029B55B73C26EA CRC64;
     MVNKDVKQTT AFGAPVWDDN NVITAGPRGP VLLQSTWFLE KLAAFDRERI PERVVHAKGS
     GAYGTFTVTK DITKYTKAKI FSKVGKKTEC FFRFSTVAGE RGSADAVRDP RGFAMKYYTE
     EGNWDLVGNN TPVFFIRDAI KFPDFIHTQK RDPQTNLPNH DMVWDFWSNV PESLYQVTWV
     MSDRGIPKSF RHMDGFGSHT FSLINAKGER FWVKFHFHTM QGVKHLTNEE AAEVRKYDPD
     SNQRDLFNAI ARGDFPKWKL SIQVMPEEDA KKYRFHPFDV TKIWYLQDYP LMEVGIVELN
     KNPENYFAEV EQAAFSPANV VPGIGYSPDR MLQGRLFSYG DTHRYRLGVN YPQIPVNKPR
     CPFHSSSRDG YMQNGYYGSL QNYTPSSLPG YKEDKSARDP KFNLAHIEKE FEVWNWDYRA
     DDSDYYTQPG DYYRSLPADE KERLHDTIGE SLAHVTHKEI VDKQLEHFKK ADPKYAEGVK
     KALEKHQKMM KDMHGKDMHH TKKKK
//
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