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
//
