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Database: UniProt
Entry: A0A022KQ66_9MICO
LinkDB: A0A022KQ66_9MICO
Original site: A0A022KQ66_9MICO 
ID   A0A022KQ66_9MICO        Unreviewed;       209 AA.
AC   A0A022KQ66;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   16-JAN-2019, entry version 19.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=D641_0113460 {ECO:0000313|EMBL:EYT48055.1};
OS   Brachybacterium muris UCD-AY4.
OC   Bacteria; Actinobacteria; Micrococcales; Dermabacteraceae;
OC   Brachybacterium.
OX   NCBI_TaxID=1249481 {ECO:0000313|EMBL:EYT48055.1, ECO:0000313|Proteomes:UP000019754};
RN   [1] {ECO:0000313|EMBL:EYT48055.1, ECO:0000313|Proteomes:UP000019754}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCD-AY4 {ECO:0000313|EMBL:EYT48055.1,
RC   ECO:0000313|Proteomes:UP000019754};
RX   PubMed=23516213;
RA   Lo J.R., Lang J.M., Darling A.E., Eisen J.A., Coil D.A.;
RT   "Draft genome sequence of an Actinobacterium, Brachybacterium muris
RT   strain UCD-AY4.";
RL   Genome Announc. 1:E0008613-E0008613(2013).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000256|RuleBase:RU000414}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:18421; EC=1.15.1.1;
CC         Evidence={ECO:0000256|RuleBase:RU000414};
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000256|RuleBase:RU000414}.
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:EYT48055.1}.
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DR   EMBL; AORC01000019; EYT48055.1; -; Genomic_DNA.
DR   RefSeq; WP_017824024.1; NZ_AORC01000019.1.
DR   EnsemblBacteria; EYT48055; EYT48055; D641_0113460.
DR   OrthoDB; 1440645at2; -.
DR   Proteomes; UP000019754; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   Gene3D; 1.10.287.990; -; 1.
DR   Gene3D; 2.40.500.20; -; 1.
DR   InterPro; IPR001189; Mn/Fe_SOD.
DR   InterPro; IPR019833; Mn/Fe_SOD_BS.
DR   InterPro; IPR019832; Mn/Fe_SOD_C.
DR   InterPro; IPR019831; Mn/Fe_SOD_N.
DR   InterPro; IPR036324; Mn/Fe_SOD_N_sf.
DR   InterPro; IPR036314; SOD_C_sf.
DR   Pfam; PF02777; Sod_Fe_C; 1.
DR   Pfam; PF00081; Sod_Fe_N; 1.
DR   PIRSF; PIRSF000349; SODismutase; 1.
DR   PRINTS; PR01703; MNSODISMTASE.
DR   SUPFAM; SSF46609; SSF46609; 1.
DR   SUPFAM; SSF54719; SSF54719; 1.
DR   PROSITE; PS00088; SOD_MN; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000019754};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019754}.
FT   DOMAIN        3     84       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       91    193       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        28     28       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        76     76       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       160    160       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       164    164       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   209 AA;  22999 MW;  D2D657E459B2EC28 CRC64;
     MAEYTLPDLD YDYGALAPSI SGKIMELHHS KHHATYVKGA NTALEKLAAA RESGEFGNVN
     QLSKDLAFNL GGHTNHSIFW KNLSPEGGDK PTGELASAID EYFGSFDAFR KHFTAAALGI
     QGSGWAVLAY EPVGGNLVIE QFYDQQNGVP VATIPLFQLD MWEHAFYLDY QNVKADYVEA
     IWKIVNWADV QARFENARSN ASGLVVPKA
//
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