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Database: UniProt/TrEMBL
Entry: A0A093CWI6_9PSEU
LinkDB: A0A093CWI6_9PSEU
Original site: A0A093CWI6_9PSEU 
ID   A0A093CWI6_9PSEU        Unreviewed;       701 AA.
AC   A0A093CWI6;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   20-DEC-2017, entry version 17.
DE   RecName: Full=Catalase {ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|RuleBase:RU000498};
GN   Name=katE {ECO:0000313|EMBL:AJK57927.1};
GN   ORFNames=BB31_33030 {ECO:0000313|EMBL:AJK57927.1};
OS   Amycolatopsis lurida NRRL 2430.
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Amycolatopsis.
OX   NCBI_TaxID=1460371 {ECO:0000313|EMBL:AJK57927.1, ECO:0000313|Proteomes:UP000029326};
RN   [1] {ECO:0000313|EMBL:AJK57927.1, ECO:0000313|Proteomes:UP000029326}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 2430 {ECO:0000313|EMBL:AJK57927.1,
RC   ECO:0000313|Proteomes:UP000029326};
RX   PubMed=25323720;
RA   Kwun M.J., Hong H.J.;
RT   "Draft Genome Sequence of Amycolatopsis lurida NRRL 2430, Producer of
RT   the Glycopeptide Family Antibiotic Ristocetin.";
RL   Genome Announc. 2:0-0(2014).
CC   -!- FUNCTION: Serves to protect cells from the toxic effects of
CC       hydrogen peroxide. {ECO:0000256|PIRNR:PIRNR038927}.
CC   -!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O.
CC       {ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|RuleBase:RU000498}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|PIRNR:PIRNR038927,
CC         ECO:0000256|PIRSR:PIRSR038927-2};
CC   -!- SIMILARITY: Belongs to the catalase family.
CC       {ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|RuleBase:RU000498}.
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DR   EMBL; CP007219; AJK57927.1; -; Genomic_DNA.
DR   KEGG; alu:BB31_33030; -.
DR   KO; K03781; -.
DR   Proteomes; UP000029326; Chromosome.
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   Gene3D; 2.40.180.10; -; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR018028; Catalase.
DR   InterPro; IPR024708; Catalase_AS.
DR   InterPro; IPR024712; Catalase_clade2.
DR   InterPro; IPR011614; Catalase_core.
DR   InterPro; IPR037060; Catalase_core_sf.
DR   InterPro; IPR002226; Catalase_haem_BS.
DR   InterPro; IPR010582; Catalase_immune_responsive.
DR   InterPro; IPR020835; Catalase_sf.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR002818; DJ-1/PfpI.
DR   PANTHER; PTHR42821; PTHR42821; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   Pfam; PF06628; Catalase-rel; 1.
DR   Pfam; PF01965; DJ-1_PfpI; 1.
DR   PIRSF; PIRSF038927; Catalase_clade2; 1.
DR   PRINTS; PR00067; CATALASE.
DR   SMART; SM01060; Catalase; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   SUPFAM; SSF56634; SSF56634; 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   Complete proteome {ECO:0000313|Proteomes:UP000029326};
KW   Heme {ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|RuleBase:RU000498};
KW   Hydrogen peroxide {ECO:0000256|PIRNR:PIRNR038927,
KW   ECO:0000256|RuleBase:RU000498};
KW   Iron {ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|PIRSR:PIRSR038927-2,
KW   ECO:0000256|RuleBase:RU000498};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR038927,
KW   ECO:0000256|PIRSR:PIRSR038927-2, ECO:0000256|RuleBase:RU000498};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR038927,
KW   ECO:0000256|RuleBase:RU000498, ECO:0000313|EMBL:AJK57927.1};
KW   Peroxidase {ECO:0000256|PIRNR:PIRNR038927,
KW   ECO:0000256|RuleBase:RU000498, ECO:0000313|EMBL:AJK57927.1}.
FT   DOMAIN       26    414       Catalase. {ECO:0000259|SMART:SM01060}.
FT   ACT_SITE     73     73       {ECO:0000256|PIRSR:PIRSR038927-1}.
FT   ACT_SITE    146    146       {ECO:0000256|PIRSR:PIRSR038927-1}.
FT   METAL       360    360       Iron (heme axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR038927-2}.
SQ   SEQUENCE   701 AA;  77303 MW;  82FD36190AF52210 CRC64;
     MAQHREDAKD EQLGGSRVDP GQSALTTQQG VRVDHTNDSL TAGVRGPTLL EDFHAREKIT
     HFDHERIPER VVHARGAGAY GFFEAYDDAL ADYTVAEFLT SGEKIPVFVR FSTVAGSRGS
     ADTVRDVRGF ATKFYTRQGN YDLVGNNMPV FFIQDGIKFP DFVHAVKPEP RNEIPQAQSA
     HDTFWDFVSL QPESLHMVLW LMSDRALPRS YRMMQGFGVH TFRLVNADGE GTFVKFHWKP
     VLGTHSLVWD ECQKIAGKDP DFNRRDLWDA IEAGQYPEWE LGVQLVAEDS EHDFDFDLLD
     PTKIIPEEQV PVRAVGRMVL DRNPEDFFAE TEQIAFHTAN VVPGIDFTND PLLQARNFSY
     LDTQLIRLGG PNFSQLPVNR PIAPVHTNQR DGHGQQNIHQ GRTSYFPNSL GGGCPAIADS
     GVFRHYTEAV AGHKIRERSE SFKDFYSQAT LFWNSMSQVE REHIVAAFRF ELGKVEDREV
     RARTVVELNN VDHDLAARVA EGIGVTVPAA PATPHHDRTS PALSQLNQPS VAPTGRKVAV
     LAADGVDTIG VRRLVEALTE QGAIAEVLAP TEAELRPGGE GDPLRPDRQL NTMASVLYDA
     VAVPCGPSAI TVLERDGYAV HFVAEAYKHG KPVAAFGSGL DLLRRAGVTA NLADGSETLI
     DQGVVTTTAA EATLPDGFFA AFLAQLGEHR TWTRKTDAIP A
//
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