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Database: UniProt
Entry: A0A495JS83_9ACTN
LinkDB: A0A495JS83_9ACTN
Original site: A0A495JS83_9ACTN 
ID   A0A495JS83_9ACTN        Unreviewed;       753 AA.
AC   A0A495JS83;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   28-JUN-2023, entry version 15.
DE   RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00012314, ECO:0000256|PIRNR:PIRNR038927};
DE            EC=1.11.1.6 {ECO:0000256|ARBA:ARBA00012314, ECO:0000256|PIRNR:PIRNR038927};
GN   ORFNames=BDK92_6271 {ECO:0000313|EMBL:RKR91847.1};
OS   Micromonospora pisi.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=589240 {ECO:0000313|EMBL:RKR91847.1, ECO:0000313|Proteomes:UP000277671};
RN   [1] {ECO:0000313|EMBL:RKR91847.1, ECO:0000313|Proteomes:UP000277671}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45175 {ECO:0000313|EMBL:RKR91847.1,
RC   ECO:0000313|Proteomes:UP000277671};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Serves to protect cells from the toxic effects of hydrogen
CC       peroxide. {ECO:0000256|PIRNR:PIRNR038927}.
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|PIRNR:PIRNR038927,
CC         ECO:0000256|RuleBase:RU000498};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971,
CC         ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|PIRSR:PIRSR038927-2};
CC   -!- SIMILARITY: Belongs to the catalase family. HPII subfamily.
CC       {ECO:0000256|ARBA:ARBA00010660}.
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:RKR91847.1}.
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DR   EMBL; RBKT01000001; RKR91847.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A495JS83; -.
DR   OrthoDB; 3169619at2; -.
DR   Proteomes; UP000277671; Unassembled WGS sequence.
DR   GO; GO:0004096; F:catalase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   Gene3D; 1.20.1370.20; -; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 2.40.180.10; Catalase core domain; 1.
DR   InterPro; IPR018028; Catalase.
DR   InterPro; IPR024708; Catalase_AS.
DR   InterPro; IPR024712; Catalase_clade2.
DR   InterPro; IPR043156; Catalase_clade2_helical.
DR   InterPro; IPR011614; Catalase_core.
DR   InterPro; IPR002226; Catalase_haem_BS.
DR   InterPro; IPR010582; Catalase_immune_responsive.
DR   InterPro; IPR041399; Catalase_large_C.
DR   InterPro; IPR020835; Catalase_sf.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   PANTHER; PTHR42821; CATALASE; 1.
DR   PANTHER; PTHR42821:SF1; CATALASE-B; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   Pfam; PF06628; Catalase-rel; 1.
DR   Pfam; PF18011; Catalase_C; 1.
DR   PIRSF; PIRSF038927; Catalase_clade2; 1.
DR   PRINTS; PR00067; CATALASE.
DR   SMART; SM01060; Catalase; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 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|PIRNR:PIRNR038927};
KW   Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324,
KW   ECO:0000256|PIRNR:PIRNR038927};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR038927};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR038927};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR038927};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|PIRNR:PIRNR038927};
KW   Reference proteome {ECO:0000313|Proteomes:UP000277671}.
FT   DOMAIN          84..472
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   REGION          24..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..53
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..79
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        131
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT   ACT_SITE        203
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT   BINDING         128
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT   BINDING         167
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT   BINDING         216
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT   BINDING         414
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT   BINDING         418
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:PIRSR038927-2"
FT   BINDING         425
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
SQ   SEQUENCE   753 AA;  81390 MW;  7D9BD26FC6C9744E CRC64;
     MDSSKPAKAV KDVVGAAAEK VAEVLTPDVP GAPGSVPPTV EEPTAPRDPL PPKAEQGAPE
     TRTPTGAETG AQTTTNGQQG RFLTTAQGAR LRDTDHSLKA GPRGPVLLQD HHLREKITHF
     DHERIPERVV HARGAGAHGV FESYGTAEEI TKAGFLAKGR KTDVFVRFST VLGSRGSADT
     VRDTRGFATK FYTDEGTFDL VGNNIPVFFI QDAIKFPDII HAGKPHPDRE IPQAQSAHDT
     FWDFVSLHTE AQHHTMWNMS DRGIPRSYRM MEGFGVHTFR LVNAGGETVL AKFHWKPKLG
     VHSLTWEEAQ LLGGIDPDFH RRDLYDAIEA GAYPEWELGV QVFPDTPEET FAGIDLLDPT
     KIVPEELASV QPLGRLTLNR TPTNFFAETE QVAFHVGHLP PGIDVTNDPL LQGRLFSYVD
     TQITRLAGPN FSQIPINRPH APVNDMLRDG FHQQAVHAGV APYRPNSLDG GNPFPAGDKD
     NAFVDVPVTV AEAPKVRQNP ASFDDHFSQV RLFWQSMSPV EKEHIIRAYT FELAKCYHQA
     IKERQLQCLA NIDPVLCAQV ATGLGLPAPE PTVPLAEVAP SPALSQLGKE WPSDGRTVGI
     VVDPDAGPDN IAQLRGAVFA AGMVPLLIAP HGGTVAGVPV QRTFATARSV EFDVLLLAAA
     PAPAADAIPA RDAKAGAANT ATVDPRVLLL VDECWRHAKA IGAWGGGVTV LEQSGRAGSP
     GVVTGDSWSE VFTAVERLLT NHRVWERFAV SVA
//
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