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Database: UniProt/TrEMBL
Entry: A0A1X2KUG8_9MYCO
LinkDB: A0A1X2KUG8_9MYCO
Original site: A0A1X2KUG8_9MYCO 
ID   A0A1X2KUG8_9MYCO        Unreviewed;       700 AA.
AC   A0A1X2KUG8;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   28-MAR-2018, entry version 9.
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:OSC25297.1};
GN   ORFNames=B8W68_14745 {ECO:0000313|EMBL:OSC25297.1};
OS   Mycobacterium paraintracellulare.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=1138383 {ECO:0000313|EMBL:OSC25297.1, ECO:0000313|Proteomes:UP000193540};
RN   [1] {ECO:0000313|EMBL:OSC25297.1, ECO:0000313|Proteomes:UP000193540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 29084 {ECO:0000313|EMBL:OSC25297.1,
RC   ECO:0000313|Proteomes:UP000193540};
RA   Tortoli E., Trovato A., Cirillo D.M.;
RT   "The new phylogeny of genus Mycobacterium.";
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OSC25297.1}.
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DR   EMBL; NCXN01000017; OSC25297.1; -; Genomic_DNA.
DR   RefSeq; WP_014385592.1; NZ_NCXN01000017.1.
DR   KEGG; mir:OCQ_40330; -.
DR   KO; K03781; -.
DR   BioCyc; MINT1138383:G1H6Y-4007-MONOMER; -.
DR   Proteomes; UP000193540; 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; 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:UP000193540};
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};
KW   Peroxidase {ECO:0000256|PIRNR:PIRNR038927,
KW   ECO:0000256|RuleBase:RU000498}.
FT   DOMAIN       25    414       Catalase. {ECO:0000259|SMART:SM01060}.
FT   ACT_SITE     72     72       {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   700 AA;  77879 MW;  CF9E4145EDDC863A CRC64;
     MATDQNPKQR DLESARFRRD TGYLTTQQGV RVDHTDDSLS VGERGPTLLE DFHAREKITH
     FDHERIPERV VHARGAGAYG YFEPYDDSLS QYTAARFLTT PGLQTPVFVR FSTVAGSRGS
     ADTVRDVRGF ATKFYTEQGN YDLVGNNFPV FFIQDGIKFP DFVHAVKPEP HNEIPQAQSA
     HDTLWDFVAL QPETLHTIMW LMSDRALPRS YRMMQGFGVH TFRLVNDRGE GTFVKFHWKP
     RLGVHSLIWD ECQKIAGKDP DYNRRDLWEA IESGQYPEWE LGVQLVPEED EFSFDFDLLD
     ATKIIPEEQV PVRPVGKMVL NRNPDNFFAE TEQVAFHTAN VVPGIDFTND PLLQFRNFSY
     LDTQLIRLGG PNFAQLPINR PVAEVRTNQH DGYGQHAIPQ GRSSYYKNTI GGGCPALADE
     NVFRHYTQRL DGQTMRKRAE SFENHYSQAR MFWMSMTRVE AEHIVAAFAF ELGKVETPEI
     RSAVVAQLAR VDGELAAQVA AKLGLPAPPE EQVDTVTASP ALSQVTDAGD TIESRKVAVL
     AANGVDVVGT QRFIELMGQR GAVVEVLAPV AGGTLEGGSG GELPVDRSFT TMASVLYDAV
     VVACGPRSIA TLSNDGYAVH FVTEAYKHLK PIGAYGAGVD LLRTAGITNR LAEDTDVLND
     QSVITTKAAA DELPDRFVEE FAGALAQHRC WQRRTDPVPA
//
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