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Database: UniProt
Entry: L1MAP9_9CORY
LinkDB: L1MAP9_9CORY
Original site: L1MAP9_9CORY 
ID   L1MAP9_9CORY            Unreviewed;       231 AA.
AC   L1MAP9;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   16-JAN-2019, entry version 25.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=HMPREF9997_02389 {ECO:0000313|EMBL:EKX88026.1};
OS   Corynebacterium durum F0235.
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=1035195 {ECO:0000313|EMBL:EKX88026.1, ECO:0000313|Proteomes:UP000010445};
RN   [1] {ECO:0000313|EMBL:EKX88026.1, ECO:0000313|Proteomes:UP000010445}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0235 {ECO:0000313|EMBL:EKX88026.1,
RC   ECO:0000313|Proteomes:UP000010445};
RA   Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R.,
RA   Courtney L., Fronick C., O'Laughlin M., Godfrey J., Wilson R.M.,
RA   Miner T., Farmer C., Delehaunty K., Cordes M., Minx P., Tomlinson C.,
RA   Chen J., Wollam A., Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S.,
RA   Warren W., Mitreva M., Mardis E.R., Wilson R.K.;
RL   Submitted (MAY-2012) 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}.
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:EKX88026.1}.
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DR   EMBL; AMEM01000040; EKX88026.1; -; Genomic_DNA.
DR   EnsemblBacteria; EKX88026; EKX88026; HMPREF9997_02389.
DR   PATRIC; fig|1035195.3.peg.2133; -.
DR   Proteomes; UP000010445; 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:UP000010445};
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:UP000010445}.
FT   DOMAIN       35    116       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      123    225       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        59     59       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       108    108       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       192    192       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       196    196       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   231 AA;  25917 MW;  C260A525173254A9 CRC64;
     MLSPFRYAYV AKMNYSLIMV RRLYTQTKGE AMAVYELPEL DYPYDALEPH IAAEIMELHH
     SKHHQNYVNG ANAALEKLQE AREKGYIGTA VTALSKDLAF NLGGHTNHSI FWKNLSPNGG
     GEPTGALAEA INHDFGSFDK FKEHFNAAAL GLQGSGWAVL AYDKIGQRLV IEQMTDQQGN
     LSIDLVPLLL LDMWEHAFYL QYKNVKADYV NAVWNVFNWD DVAARYAAAT S
//
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