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Database: UniProt
Entry: A0A1X7VNW3_AMPQE
LinkDB: A0A1X7VNW3_AMPQE
Original site: A0A1X7VNW3_AMPQE 
ID   A0A1X7VNW3_AMPQE        Unreviewed;       498 AA.
AC   A0A1X7VNW3;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN   Name=100631516 {ECO:0000313|EnsemblMetazoa:Aqu2.1.41530_001};
OS   Amphimedon queenslandica (Sponge).
OC   Eukaryota; Metazoa; Porifera; Demospongiae; Heteroscleromorpha;
OC   Haplosclerida; Niphatidae; Amphimedon.
OX   NCBI_TaxID=400682 {ECO:0000313|EnsemblMetazoa:Aqu2.1.41530_001, ECO:0000313|Proteomes:UP000007879};
RN   [1] {ECO:0000313|Proteomes:UP000007879}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20686567; DOI=10.1038/nature09201;
RA   Srivastava M., Simakov O., Chapman J., Fahey B., Gauthier M.E., Mitros T.,
RA   Richards G.S., Conaco C., Dacre M., Hellsten U., Larroux C., Putnam N.H.,
RA   Stanke M., Adamska M., Darling A., Degnan S.M., Oakley T.H.,
RA   Plachetzki D.C., Zhai Y., Adamski M., Calcino A., Cummins S.F.,
RA   Goodstein D.M., Harris C., Jackson D.J., Leys S.P., Shu S., Woodcroft B.J.,
RA   Vervoort M., Kosik K.S., Manning G., Degnan B.M., Rokhsar D.S.;
RT   "The Amphimedon queenslandica genome and the evolution of animal
RT   complexity.";
RL   Nature 466:720-726(2010).
RN   [2] {ECO:0000313|Proteomes:UP000007879}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lucas S., Shapiro H., Lindquist E., Tice H., Dalin E., Glavina del Rio T.,
RA   Bruce D., Barry K., Pitluck S., Srivastava M., Simakov O., Chapman J.,
RA   Mitros T., Hellsten U., Putnam N.H., Fahey B., Gauthier M., Larroux C.,
RA   Richards G.S., Stanke M., Adamska M., Darling A., Dacre M., Degnan S.M.,
RA   Zhai Y., Adamski M., Calcino A., Cummins S.F., Goodstein D.M., Harris C.,
RA   Shu S., Woodcroft B., Leys S.P., Manning G., Degnan B.M., Rokhsar D.S.;
RT   "The genome of the haplosclerid demosponge Amphimedon queenslandica and the
RT   evolution of animal complexity.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblMetazoa:Aqu2.1.41530_001}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (MAY-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   RefSeq; XP_011409548.1; XM_011411246.2.
DR   RefSeq; XP_019860460.1; XM_020004901.1.
DR   AlphaFoldDB; A0A1X7VNW3; -.
DR   STRING; 400682.A0A1X7VNW3; -.
DR   EnsemblMetazoa; Aqu2.1.41530_001; Aqu2.1.41530_001; Aqu2.1.41530.
DR   GeneID; 100631516; -.
DR   KEGG; aqu:100631516; -.
DR   eggNOG; KOG0047; Eukaryota.
DR   InParanoid; A0A1X7VNW3; -.
DR   OMA; FYNQGAR; -.
DR   OrthoDB; 3198922at2759; -.
DR   Proteomes; UP000007879; 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:UP000007879}.
FT   DOMAIN          26..411
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   ACT_SITE        73
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   ACT_SITE        146
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   BINDING         356
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   498 AA;  56090 MW;  79449F68FA8C570C CRC64;
     MSSKRPACFS QLEEYAKKTQ PGEVLTTTHG NPIDFKTAIQ TFGPRGPMLM QDGVYLDEMA
     HFDRERIPER VVHAKGAGAY GVFEVTHDIT KYCCAKLFSE VGKKTDLFIR FSTVGGESGS
     ADTARDPRGF AVKFYTEDGN WDLVGNNTPI FFIRDPFLFP SFIHTQKRNP VTHLKDPDMF
     WDFISLRPET THQVSFLFSD RGIPDGYRHM NGYGSHTFKL VNSKGEPVYC KFHYKTDQGI
     KNMPVGKAAE LAGTNPDYSI QDLYEAIATG NFPSWTLSIQ VMTYEQAEKC SFNPFDLTKV
     WPHADYPLIP VGKITLNRNP SNYFFDVEQS AFSPAHMPPG IEASPDKMLQ GRLFSYDDTH
     FHRLGPNFQM IPVNCPYAGK PRNYVRDGPM CVDGNQGGAP NYYPNSFNGP KDMGKHDVTI
     FPGPAGDVKR YNAADDDNFS QVGIFYNKVL NEEERTRLAQ NIAGHMKNAS PKIQERAIAN
     FSKADPDYGA RIKKYISQ
//
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