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Database: UniProt/TrEMBL
Entry: F5Z250_MYCSD
LinkDB: F5Z250_MYCSD
Original site: F5Z250_MYCSD 
ID   F5Z250_MYCSD            Unreviewed;       713 AA.
AC   F5Z250;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   31-JAN-2018, entry version 42.
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   OrderedLocusNames=JDM601_3050 {ECO:0000313|EMBL:AEF37050.1};
OS   Mycobacterium sinense (strain JDM601).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=875328 {ECO:0000313|EMBL:AEF37050.1, ECO:0000313|Proteomes:UP000009224};
RN   [1] {ECO:0000313|EMBL:AEF37050.1, ECO:0000313|Proteomes:UP000009224}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JDM601 {ECO:0000313|EMBL:AEF37050.1,
RC   ECO:0000313|Proteomes:UP000009224};
RX   PubMed=21685274; DOI=10.1128/JB.05291-11;
RA   Zhang Z.Y., Sun Z.Q., Wang Z.L., Wen Z.L., Sun Q.W., Zhu Z.Q.,
RA   Song Y.Z., Zhao J.W., Wang H.H., Zhang S.L., Guo X.K.;
RT   "Complete gnome sequence of a novel clinical isolate, the
RT   nontuberculous Mycobacterium strain JDM601.";
RL   J. Bacteriol. 193:4300-4301(2011).
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; CP002329; AEF37050.1; -; Genomic_DNA.
DR   STRING; 875328.JDM601_3050; -.
DR   EnsemblBacteria; AEF37050; AEF37050; JDM601_3050.
DR   KEGG; mjd:JDM601_3050; -.
DR   eggNOG; ENOG4105CH6; Bacteria.
DR   eggNOG; COG0753; LUCA.
DR   KO; K03781; -.
DR   OMA; VMWQMSD; -.
DR   OrthoDB; POG091H0424; -.
DR   BioCyc; MSP875328:GHLX-3094-MONOMER; -.
DR   Proteomes; UP000009224; 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:UP000009224};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009224}.
FT   DOMAIN       24    413       Catalase. {ECO:0000259|SMART:SM01060}.
FT   ACT_SITE     71     71       {ECO:0000256|PIRSR:PIRSR038927-1}.
FT   ACT_SITE    145    145       {ECO:0000256|PIRSR:PIRSR038927-1}.
FT   METAL       359    359       Iron (heme axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR038927-2}.
SQ   SEQUENCE   713 AA;  78629 MW;  8F47D6EF8984DC9B CRC64;
     MATEDPKQRQ LDEHRYDRQS GYLTTQQGLR VDHTDDALTA GERGPTLLED FHAREKVMHF
     DHERIPERVV HARGSGAYGY FEPYDDSLAE YTAAKFLTSP GTKTPVFVRF STVAGFRGSA
     DTVRDVRGFA TKFYTEQGNY DLVGNNFPVF FIQDGIKFPD FVHAVKPEPD NEIPQAQSAH
     DTLWDFVSLQ PETLHAIMWL MSDRSLPRSF RMMQGFGVHT FRFVNAKGQG TFVKFHWKPK
     LGVHSLIWDE CQKIAGKDPD FNRRDLWDSI EAGQYPEWEL GVQLVAESDE FNFDFDLLDA
     TKIIPEEQVP VRPVGKMVLN RNPDNFFAET EQVAFCTANV VPGIDFTNDP LLQFRNFSYL
     DTQLIRLGGP NFNHLPINRP VAPVHTNQHD GYSQHAIPVG KSSYYKNSLG GGCPALAGGD
     DEVYRHYTQK VDGDKIRKRA ASFENHYSQA RMFYKSMSEP EAKHIVAAYA FELGKCETVE
     IRQRVVEQLN HIDHDLARQV AEKLGLSAPD ERQLDAAAEK VGTSPALSQL HAATVPPESR
     GAPTIESRKI AVLAADGVDV TGVQSFVEAM RRRGAVAEVL APTGGGELAG GSGGQLGVDR
     AITTMASVLY DAVVVPCGPE AMHTLAADGY AMHFITEAYK HLKPIGAFGA GVELLPKAGI
     VERLAEDTGV TVSTGVVTTA AAAGDLGEEF FDAFAAVLAK HRVWDRAADA VPA
//
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