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Database: UniProt
Entry: A0A0M4R1V4_9PSEU
LinkDB: A0A0M4R1V4_9PSEU
Original site: A0A0M4R1V4_9PSEU 
ID   A0A0M4R1V4_9PSEU        Unreviewed;       199 AA.
AC   A0A0M4R1V4;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   16-JAN-2019, entry version 16.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=WY02_22610 {ECO:0000313|EMBL:ALE80738.1};
OS   Pseudonocardia sp. AL041005-10.
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Pseudonocardia.
OX   NCBI_TaxID=445576 {ECO:0000313|EMBL:ALE80738.1};
RN   [1] {ECO:0000313|EMBL:ALE80738.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AL041005-10 {ECO:0000313|EMBL:ALE80738.1};
RX   PubMed=26438860; DOI=10.1073/pnas.1515348112;
RA   Sit C.S., Van Arnam E.B., Ramadhar T.R.;
RT   "Variable genetic architectures produce virtually identical molecules
RT   in bacterial symbionts of fungus-growing ants.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:13150-13154(2015).
RN   [2] {ECO:0000313|EMBL:ALE80738.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=AL041005-10 {ECO:0000313|EMBL:ALE80738.1};
RA   Syromyatnikov M.Y., Popov V.N.;
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:
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}.
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DR   EMBL; CP011862; ALE80738.1; -; Genomic_DNA.
DR   RefSeq; WP_062400780.1; NZ_CP011862.1.
DR   EnsemblBacteria; ALE80738; ALE80738; WY02_22610.
DR   KEGG; psea:WY02_22610; -.
DR   PATRIC; fig|445576.3.peg.4946; -.
DR   KO; K04564; -.
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   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
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   199 AA;  22059 MW;  3C179718622A4311 CRC64;
     MAEYTLPDLP YDYSALAPHI APEIMELHHS KHHNTYVQGL NTTLDKLADA REKNDFGAVV
     GLEKTLAFNL GGHVNHSAFW NNLSPDGGDK PTGDLAAAIE KDFGSFDGFQ AHFTAAATTI
     QGSGWAILGH DRLGDRLLIH QLYDQQSQLP AGQTPIVLLD MWEHAFYLQY KNVKPDYVKA
     WWNVVNWADA AERFAAAKG
//
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