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Database: UniProt/TrEMBL
Entry: A0A0M9VLM6_9MICO
LinkDB: A0A0M9VLM6_9MICO
Original site: A0A0M9VLM6_9MICO 
ID   A0A0M9VLM6_9MICO        Unreviewed;       211 AA.
AC   A0A0M9VLM6;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   28-MAR-2018, entry version 11.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=XI38_05550 {ECO:0000313|EMBL:KOS11323.1};
OS   Microbacterium chocolatum.
OC   Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=84292 {ECO:0000313|EMBL:KOS11323.1, ECO:0000313|Proteomes:UP000037737};
RN   [1] {ECO:0000313|EMBL:KOS11323.1, ECO:0000313|Proteomes:UP000037737}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SIT 101 {ECO:0000313|EMBL:KOS11323.1,
RC   ECO:0000313|Proteomes:UP000037737};
RA   Li X., Xu Y.;
RT   "Complete genome sequence of Microbacterium chocolatum SIT 101, a
RT   bacterium enantioselectively hydrolyzing mesomeric diesters.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {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:KOS11323.1}.
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DR   EMBL; LAVO01000005; KOS11323.1; -; Genomic_DNA.
DR   RefSeq; WP_053547325.1; NZ_KQ440286.1.
DR   EnsemblBacteria; KOS11323; KOS11323; XI38_05550.
DR   KEGG; mcw:A8L33_09450; -.
DR   PATRIC; fig|84292.3.peg.1141; -.
DR   KO; K04564; -.
DR   Proteomes; UP000037737; 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:UP000037737};
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:UP000037737}.
FT   DOMAIN        3     84       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       94    196       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       163    163       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       167    167       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   211 AA;  23179 MW;  572F73DD88F0D0F0 CRC64;
     MAKYTLPDLP YDFAALEPHI SGKIMELHHD KHHQAYVTGA NTALEQLAEA RESGNLANVN
     KLEKDLAFNL GGHVNHSIFW TNLAPANDGG GGEPEGELRA AIDEFFGGFD RFKAHFTAAA
     TGIQGSGWAV LSWDPIGEQL IIQQLFDQQS NTAQGTIPVF QLDMWEHAFY LDYLNVKADY
     VSAAWNIANW QNVAQRLDAA RGKTAGLLVL S
//
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