ID   A0A0S2TCN0_9GAMM        Unreviewed;       484 AA.
AC   A0A0S2TCN0;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00014132, ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN   ORFNames=Tel_06700 {ECO:0000313|EMBL:ALP52868.1};
OS   Candidatus Tenderia electrophaga.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Tenderia.
OX   NCBI_TaxID=1748243 {ECO:0000313|EMBL:ALP52868.1, ECO:0000313|Proteomes:UP000055136};
RN   [1] {ECO:0000313|EMBL:ALP52868.1, ECO:0000313|Proteomes:UP000055136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRL1 {ECO:0000313|EMBL:ALP52868.1};
RA   Eddie B.J., Malanoski A.P., Wang Z., Hall R.J., Oh S.D., Heiner C., Lin B.,
RA   Strycharz-Glaven S.M.;
RT   "Description of Candidatus Tenderia electrophaga gen. nov, sp. nov., an
RT   Uncultivated Electroautotroph from a Biocathode Enrichment.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00001971,
CC         ECO:0000256|PIRSR:PIRSR038928-2};
CC   -!- SIMILARITY: Belongs to the catalase family.
CC       {ECO:0000256|ARBA:ARBA00005329, ECO:0000256|RuleBase:RU000498}.
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DR   EMBL; CP013099; ALP52868.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S2TCN0; -.
DR   STRING; 1748243.Tel_06700; -.
DR   KEGG; tee:Tel_06700; -.
DR   Proteomes; UP000055136; Chromosome.
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:SF9; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000055136}.
FT   DOMAIN          10..391
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        57
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   484 AA;  55506 MW;  F4F0BD03571445A3 CRC64;
     MKKDDRTPTT NDAGIPVPSD EYSLTVGPDG PLLLQDHYLI EQMANFNRER IPERQPHAKG
     SGAFGHFEVT QDVSEYTKAA VFQPGTKTDT LIRFSTVAGE RGSPDTWRDP RGFALKFYTR
     QGNYDMVGNN TPVFFIRDPM KFQHFIRSQK RRADSGLRDH DMQWDFWTLS PESAHQVTWL
     MGDRGIPKSY RHMNGYSSHT YMWVNAKGQR FWVKYHFKTD QGIDFLTQAD ADRIAGEDSD
     YHRRDLFDAI QRGDHPSWTL KVQIMPFDDA KDYRFNPFDL TKVWPHSDYP TMEVGRLTLT
     RNPTDFHTEI EQAAFEPNNL VPGIGVSPDK MLLARVFSYA DAHRARLGVN YKQIPVNSPQ
     VPVHSYSKDG AMRVQNVSDP VYAPNSKGGP QADPERYPYV EKWEASGEFM HAAYTPHEDD
     DDFVQPGTLV REVMDAAARD RLVSNVVGHL KDGVTQAVLE RAFEYWRKVD RDVGDRIAKA
     FKDK
//