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Database: UniProt/TrEMBL
Entry: I3DUM3_BACMT
LinkDB: I3DUM3_BACMT
Original site: I3DUM3_BACMT 
ID   I3DUM3_BACMT            Unreviewed;       187 AA.
AC   I3DUM3;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   25-OCT-2017, entry version 29.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=BMMGA3_14090 {ECO:0000313|EMBL:AIE61176.1};
OS   Bacillus methanolicus MGA3.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=796606 {ECO:0000313|EMBL:AIE61176.1, ECO:0000313|Proteomes:UP000027602};
RN   [1] {ECO:0000313|EMBL:AIE61176.1, ECO:0000313|Proteomes:UP000027602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGA3 {ECO:0000313|EMBL:AIE61176.1,
RC   ECO:0000313|Proteomes:UP000027602};
RX   PubMed=25758049;
RA   Irla M., Neshat A., Brautaset T., Ruckert C., Kalinowski J.,
RA   Wendisch V.F.;
RT   "Transcriptome analysis of thermophilic methylotrophic Bacillus
RT   methanolicus MGA3 using RNA-sequencing provides detailed insights into
RT   its previously uncharted transcriptional landscape.";
RL   BMC Genomics 16:73-73(2015).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000256|RuleBase:RU000393}.
CC   -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {ECO:0000256|RuleBase:RU000393}.
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC       Note=Binds 1 copper ion per subunit.
CC       {ECO:0000256|RuleBase:RU000393};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC       Note=Binds 1 zinc ion per subunit.
CC       {ECO:0000256|RuleBase:RU000393};
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000256|RuleBase:RU000393}.
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DR   EMBL; CP007739; AIE61176.1; -; Genomic_DNA.
DR   RefSeq; WP_003349582.1; NZ_CP007739.1.
DR   EnsemblBacteria; AIE61176; AIE61176; BMMGA3_14090.
DR   KEGG; bmet:BMMGA3_14090; -.
DR   KO; K04565; -.
DR   Proteomes; UP000027602; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR   Gene3D; 2.60.40.200; -; 1.
DR   InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR   InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR   InterPro; IPR018152; SOD_Cu/Zn_BS.
DR   InterPro; IPR001424; SOD_Cu_Zn_dom.
DR   PANTHER; PTHR10003; PTHR10003; 1.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   SUPFAM; SSF49329; SSF49329; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000027602};
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027602};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       34    167       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   187 AA;  20090 MW;  34A9D2546AB0710A CRC64;
     MKIGRMIILV FLLVGCAEEN PKSVDVEMFN TVGDSLGKIK ITEQASGVKL KVNLDGLPPG
     EHAMHIHETG KCEPPDFKSA GNHFNPDNKQ HGLLHPKGSH AGDLPNLIVE DDGKVKAEIM
     APQITLQNGK TSLFTKEGTS IVIHEGKDDG MTQPAGDSGS RIACGKISMD KGQTEQKKAQ
     DDKQGEQ
//
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