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Database: UniProt
Entry: A0A0U1Q3W1_9BURK
LinkDB: A0A0U1Q3W1_9BURK
Original site: A0A0U1Q3W1_9BURK 
ID   A0A0U1Q3W1_9BURK        Unreviewed;       488 AA.
AC   A0A0U1Q3W1;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-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=AAV94_00080 {ECO:0000313|EMBL:KKW69325.1};
OS   Lampropedia cohaerens.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Lampropedia.
OX   NCBI_TaxID=1610491 {ECO:0000313|EMBL:KKW69325.1, ECO:0000313|Proteomes:UP000050580};
RN   [1] {ECO:0000313|EMBL:KKW69325.1, ECO:0000313|Proteomes:UP000050580}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT6 {ECO:0000313|EMBL:KKW69325.1,
RC   ECO:0000313|Proteomes:UP000050580};
RA   Tripathi C., Rani P., Mahato N.K., Lal R.;
RT   "Draft genome sequence of Lampropedia sp. CT6, isolated from the microbial
RT   mat of a hot water spring, located at Manikaran, India.";
RL   Submitted (MAY-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|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:KKW69325.1}.
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DR   EMBL; LBNQ01000005; KKW69325.1; -; Genomic_DNA.
DR   RefSeq; WP_046740293.1; NZ_LBNQ01000005.1.
DR   AlphaFoldDB; A0A0U1Q3W1; -.
DR   STRING; 1610491.AAV94_00080; -.
DR   PATRIC; fig|1610491.3.peg.16; -.
DR   OrthoDB; 9761719at2; -.
DR   Proteomes; UP000050580; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050580}.
FT   DOMAIN          14..398
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        61
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   ACT_SITE        134
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   BINDING         344
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   488 AA;  56177 MW;  4E1414A5D1453917 CRC64;
     MSDPTKDLKP TYLTTDFGAP VPDNQNSLTA GPRGPLLAQD VWLHEKLGNF VREVIPERRM
     HAKGSGAFGT FTVTHDITRY TRAKIFSEVG KKTEMFARFT TVAGERGAAD AERDIRGFAL
     KFYTEEGNWD MVGNNTPVFF IRDPRKFPDL NKAVKRCPRT NLRSPTYNWD WWTLLPEALH
     QVTIVMSDRG IPASYRHMHG FGSHTYSFWN EQGERFWVKF HFRTQQGIKN LTDAEAEALI
     GKDRESHQRD LYNAIERGEF PKWTMYIQVM PEEEAEKVPY HPFDLTKVWP KKDYPLIEVG
     EFELNRNPEN FFADVEQSAF APSNLVPGIS VSPDKMLQAR LFNYADAQRY RLGTNYQQIP
     VNAARCPVHS NHRDGIGRVD GNYGSLPHYE PNSFHQWQEQ PQFREPPLKI KGDVADWFNF
     REDDADYYQQ PGDLFRLMTP EQQQALFDNT ARAMNGVPDF IRQRHIANCT KADPAYGAGV
     AEALKRLG
//
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