UniProt: A0A086MY36

Database: UniProt
Entry: A0A086MY36_9ACTN

LinkDB:  A0A086MY36_9ACTN 
Original site:  A0A086MY36_9ACTN

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (14)   
   InterPro (8)   
   Pfam (2)   
   PROSITE (3)   
   SMART (1)   
All databases (22)   

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ID   A0A086MY36_9ACTN        Unreviewed;       483 AA.
AC   A0A086MY36;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN   ORFNames=FM21_23750 {ECO:0000313|EMBL:KFG73804.1};
OS   Streptomyces mutabilis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=67332 {ECO:0000313|EMBL:KFG73804.1, ECO:0000313|Proteomes:UP000029095};
RN   [1] {ECO:0000313|EMBL:KFG73804.1, ECO:0000313|Proteomes:UP000029095}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TRM45540 {ECO:0000313|EMBL:KFG73804.1,
RC   ECO:0000313|Proteomes:UP000029095};
RA   Luo X., Zhang L.;
RT   "Complete genome sequence of the Streptomyces mutabilis TRM45540.";
RL   Submitted (MAY-2014) 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:KFG73804.1}.
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DR   EMBL; JNFQ01000002; KFG73804.1; -; Genomic_DNA.
DR   RefSeq; WP_043380149.1; NZ_KN039947.1.
DR   AlphaFoldDB; A0A086MY36; -.
DR   STRING; 1915400.FM21_23750; -.
DR   HOGENOM; CLU_010645_2_0_11; -.
DR   Proteomes; UP000029095; 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}.
FT   DOMAIN          7..391
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        54
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   ACT_SITE        127
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   BINDING         337
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   483 AA;  53885 MW;  509E3EE517E09B10 CRC64;
     MTQGPLTTEA GAPVADNQNS ETAGVGGPVL VQDQLLLEKL AHFNRERIPE RVVHARGAGA
     YGTFTVTADV TKYTRAAFLS EVGKETETFL RFSTVAGNLG AADAVRDPRG FALKFYTEEG
     NYDLVGNNTP VFFIKDAIKF PDFIHTQKRD PYTGSTEMDN VWDFWSLSPE STHQVTWLFG
     DRGIPASYRH MDGFGSHTYQ WNNEAGEAFW VKYHFKTDQG IKCLTQAEAD KLAGEDPDSH
     QRDLREAIER GDFPSWTVGV QIMPVAEAAT YRFNPFDLTK VWPHADYPIV WFGKLELNRN
     PENIFAEVEQ SIFSPAHFVP GIGPSPDKML QGRLFAYGDA HRYRVGINAD HLPVNRPHAT
     EARTNSRDGY LYDGRHKGAK NYEPNSFGGP FQTDRALWQP VAVSGVTGET EAPSHAEDND
     FVQAGNLYRL MTDEEKGRLI DNLAGAISKV SREDIIERAI DNFRQADGDF GKRLEAAVQA
     LRG
//

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