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Database: UniProt/TrEMBL
Entry: N6UDL6_DENPD
LinkDB: N6UDL6_DENPD
Original site: N6UDL6_DENPD 
ID   N6UDL6_DENPD            Unreviewed;       508 AA.
AC   N6UDL6;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
DE   Flags: Fragment;
GN   Name=109538109 {ECO:0000313|EnsemblMetazoa:ENN76752};
GN   ORFNames=D910_07741 {ECO:0000313|EMBL:ERL90392.1}, YQE_06817
GN   {ECO:0000313|EMBL:ENN76752.1};
OS   Dendroctonus ponderosae (Mountain pine beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Curculionidae; Scolytinae; Dendroctonus.
OX   NCBI_TaxID=77166 {ECO:0000313|EMBL:ENN76752.1};
RN   [1] {ECO:0000313|Proteomes:UP000019118, ECO:0000313|Proteomes:UP000030742}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23537049; DOI=10.1186/gb-2013-14-3-r27;
RA   Keeling C.I., Yuen M.M., Liao N.Y., Roderick Docking T., Chan S.K.,
RA   Taylor G.A., Palmquist D.L., Jackman S.D., Nguyen A., Li M., Henderson H.,
RA   Janes J.K., Zhao Y., Pandoh P., Moore R., Sperling F.A., W Huber D.P.,
RA   Birol I., Jones S.J., Bohlmann J.;
RT   "Draft genome of the mountain pine beetle, Dendroctonus ponderosae Hopkins,
RT   a major forest pest.";
RL   Genome Biol. 14:R27-R27(2013).
RN   [2] {ECO:0000313|EnsemblMetazoa:ENN76752}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JAN-2017) to UniProtKB.
CC   -!- FUNCTION: Occurs in almost all aerobically respiring organisms and
CC       serves to protect cells from the toxic effects of hydrogen peroxide.
CC       {ECO:0000256|RuleBase:RU004142}.
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; APGK01039325; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KB740969; ENN76752.1; -; Genomic_DNA.
DR   EMBL; KB632230; ERL90392.1; -; Genomic_DNA.
DR   RefSeq; XP_019760743.1; XM_019905184.1.
DR   RefSeq; XP_019760745.1; XM_019905186.1.
DR   AlphaFoldDB; N6UDL6; -.
DR   STRING; 77166.N6UDL6; -.
DR   EnsemblMetazoa; ENN76752; ENN76752; YQE_06817.
DR   GeneID; 109538109; -.
DR   KEGG; dpa:109538109; -.
DR   HOGENOM; CLU_010645_2_0_1; -.
DR   OMA; KFRWNVF; -.
DR   OrthoDB; 3198922at2759; -.
DR   Proteomes; UP000019118; Unassembled WGS sequence.
DR   Proteomes; UP000030742; 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: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:UP000030742}.
FT   DOMAIN          29..411
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   ACT_SITE        76
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   ACT_SITE        149
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   BINDING         359
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"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ENN76752.1"
SQ   SEQUENCE   508 AA;  57554 MW;  29DC436301C85ECC CRC64;
     MASEDKASRQ ILDWKPKERA SCAESIYART AFGAPIVVKD ASETVGPKGP ILLQDAHFIE
     DMAHFNRERI PERVVHAKGA GAFGYFKVTH DITEYCAAKV FEGIGKTTPI AVRFSTVGGE
     AGSADTARDP RGFAVKFYTE DGNWDLVGNN TPVFFIKDPI LFSSFIHTQK RNPQTHLKDP
     NMMWDFHTLR PESIHQWMFL FGDRGTPDGY RHMNGYGSHT FKLVNRDGKY HYCKFHYKTD
     QGVKNLPVEK ADELAGSDPD YAIRDLYNAI ANKNYPSYSM YIQIMTPEQA QTSKFNPFDL
     TKIWPHSDYP LIPVGKLVLD RNPENYFAEV EQIAFNPAHM VPGILPSPDR MLQGRLFTYG
     DTHRYRLGPN YLQLPVNCPY KVKNYQRDGN MAISNQGNAP NYHPNSFSGP KVDPNVKVLY
     PPYTITGDVN RYDEPMKDED FEQPAALWLR VLDEDAKTRL VNNLAGSLKS TADFIQERAV
     KLYSRVHPTL GSRLEKALNL AARAKANL
//
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