GenomeNet

Database: UniProt/TrEMBL
Entry: A0LWQ6_ACIC1
LinkDB: A0LWQ6_ACIC1
Original site: A0LWQ6_ACIC1 
ID   A0LWQ6_ACIC1            Unreviewed;       482 AA.
AC   A0LWQ6;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   24-JAN-2024, entry version 95.
DE   RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN   OrderedLocusNames=Acel_2094 {ECO:0000313|EMBL:ABK53866.1};
OS   Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B).
OC   Bacteria; Actinomycetota; Actinomycetes; Acidothermales; Acidothermaceae;
OC   Acidothermus.
OX   NCBI_TaxID=351607 {ECO:0000313|EMBL:ABK53866.1, ECO:0000313|Proteomes:UP000008221};
RN   [1] {ECO:0000313|EMBL:ABK53866.1, ECO:0000313|Proteomes:UP000008221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43068 / DSM 8971 / 11B
RC   {ECO:0000313|Proteomes:UP000008221};
RX   PubMed=19270083; DOI=10.1101/gr.084848.108;
RA   Barabote R.D., Xie G., Leu D.H., Normand P., Necsulea A., Daubin V.,
RA   Medigue C., Adney W.S., Xu X.C., Lapidus A., Parales R.E., Detter C.,
RA   Pujic P., Bruce D., Lavire C., Challacombe J.F., Brettin T.S., Berry A.M.;
RT   "Complete genome of the cellulolytic thermophile Acidothermus
RT   cellulolyticus 11B provides insights into its ecophysiological and
RT   evolutionary adaptations.";
RL   Genome Res. 19:1033-1043(2009).
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   ---------------------------------------------------------------------------
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; CP000481; ABK53866.1; -; Genomic_DNA.
DR   RefSeq; WP_011720929.1; NC_008578.1.
DR   AlphaFoldDB; A0LWQ6; -.
DR   STRING; 351607.Acel_2094; -.
DR   KEGG; ace:Acel_2094; -.
DR   eggNOG; COG0753; Bacteria.
DR   HOGENOM; CLU_010645_2_0_11; -.
DR   InParanoid; A0LWQ6; -.
DR   OMA; NPSWTCY; -.
DR   OrthoDB; 3169619at2; -.
DR   Proteomes; UP000008221; 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:UP000008221}.
FT   DOMAIN          10..391
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
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   482 AA;  55356 MW;  A928D024A07D49F4 CRC64;
     MTETTRPVTT TDAGIPAASD EYSLTVGAGG PILLQDHYLI QKMAQFNRER VPERVVHAKG
     GGAFGFFETT EDVSQFTKAD LFQPGRRCEV LVRFSTVAGE QGSPDTWRDP RGFAVKFYTQ
     QGNYDLVGNN TPIFFIRDPQ KFQDFIHSQK RRADSGLRDH NMQWDFWTLS PESAHQVTWL
     MGDRGIPKTW RHMNGYGSHT FLWQNAGGER FWIKYHFKTD QGIDFLTQDE ADRIAGEDAD
     FHRRDLYEAI RRGEHPSWTL YVQVMPFHEA ADYRFNPFDL TKVWPHGDYP LIKVGRMVLN
     RNPDNFFAQI EQAAFEPANM VPGIGPSPDR MLLGRLFSYP DTHRYRIGTN YLQLPVNRPK
     VPVHSYNRDG AMRYENPGDP VYAPNSYGGP QADPSYELPS WFVEGGEIVR TAYVKHRDDD
     DFVQAGTLYR KVLDDAARDR LVDNITRHLK QGVSTPVLER AFEYWRSVDP DLGARVAKNF
     GR
//
DBGET integrated database retrieval system