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Database: UniProt/TrEMBL
Entry: J9WMW7_MYCIP
LinkDB: J9WMW7_MYCIP
Original site: J9WMW7_MYCIP 
ID   J9WMW7_MYCIP            Unreviewed;       700 AA.
AC   J9WMW7;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   28-MAR-2018, entry version 32.
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   ORFNames=MIP_05918 {ECO:0000313|EMBL:AFS15982.1};
OS   Mycobacterium indicus pranii (strain DSM 45239 / MTCC 9506).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=1232724 {ECO:0000313|EMBL:AFS15982.1, ECO:0000313|Proteomes:UP000007329};
RN   [1] {ECO:0000313|EMBL:AFS15982.1, ECO:0000313|Proteomes:UP000007329}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MTCC 9506 {ECO:0000313|EMBL:AFS15982.1};
RX   PubMed=17912347; DOI=10.1371/journal.pone.0000968;
RA   Ahmed N., Saini V., Raghuvanshi S., Khurana J.P., Tyagi A.K.,
RA   Tyagi A.K., Hasnain S.E.;
RT   "Molecular analysis of a leprosy immunotherapeutic bacillus provides
RT   insights into Mycobacterium evolution.";
RL   PLoS ONE 2:E968-E968(2007).
RN   [2] {ECO:0000313|EMBL:AFS15982.1, ECO:0000313|Proteomes:UP000007329}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45239 / MTCC 9506 {ECO:0000313|Proteomes:UP000007329};
RX   PubMed=22965120; DOI=10.1093/nar/gks793;
RA   Saini V., Raghuvanshi S., Khurana J.P., Ahmed N., Hasnain S.E.,
RA   Tyagi A.K., Tyagi A.K.;
RT   "Massive gene acquisitions in Mycobacterium indicus pranii provide a
RT   perspective on mycobacterial evolution.";
RL   Nucleic Acids Res. 40:10832-10850(2012).
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; CP002275; AFS15982.1; -; Genomic_DNA.
DR   RefSeq; WP_014942753.1; NC_018612.1.
DR   EnsemblBacteria; AFS15982; AFS15982; MIP_05918.
DR   KEGG; mid:MIP_05918; -.
DR   PATRIC; fig|1232724.3.peg.4022; -.
DR   KO; K03781; -.
DR   BioCyc; MIND1232724:G1HA1-4018-MONOMER; -.
DR   Proteomes; UP000007329; Chromosome.
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:UP000007329};
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;  77893 MW;  585E816F891A6C52 CRC64;
     MATDQNPKQR DLESARFRRD TGYLTTQQGV RVDHTDDSLS VGERGPTLLE DFHAREKITH
     FDHERIPERV VHARGAGAYG YFEPYDDSLA 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 ELGKVEMPEI
     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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