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Database: UniProt/TrEMBL
Entry: A0A0G3GLF6_9CORY
LinkDB: A0A0G3GLF6_9CORY
Original site: A0A0G3GLF6_9CORY 
ID   A0A0G3GLF6_9CORY        Unreviewed;       199 AA.
AC   A0A0G3GLF6;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   25-OCT-2017, entry version 11.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   Name=sodA {ECO:0000313|EMBL:AKK02066.1};
GN   ORFNames=CEPID_00860 {ECO:0000313|EMBL:AKK02066.1};
OS   Corynebacterium epidermidicanis.
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=1050174 {ECO:0000313|EMBL:AKK02066.1, ECO:0000313|Proteomes:UP000035368};
RN   [1] {ECO:0000313|EMBL:AKK02066.1, ECO:0000313|Proteomes:UP000035368}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45586 {ECO:0000313|EMBL:AKK02066.1,
RC   ECO:0000313|Proteomes:UP000035368};
RA   Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT   "Complete genome sequence of Corynebacterium epidermidicanis DSM
RT   45586, isolated from the skin of a dog suffering from pruritus.";
RL   Submitted (MAY-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}.
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DR   EMBL; CP011541; AKK02066.1; -; Genomic_DNA.
DR   RefSeq; WP_047239355.1; NZ_CP011541.1.
DR   EnsemblBacteria; AKK02066; AKK02066; CEPID_00860.
DR   KEGG; cei:CEPID_00860; -.
DR   PATRIC; fig|1050174.4.peg.181; -.
DR   KO; K04564; -.
DR   Proteomes; UP000035368; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
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:UP000035368};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:AKK02066.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035368}.
FT   DOMAIN        3     85       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       92    194       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        28     28       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        77     77       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       161    161       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       165    165       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   199 AA;  22433 MW;  8786B52BE2206B22 CRC64;
     MAKYELPQLD YAYDALEPHI SAEIMELHHT KHHQNYVNGA NTALEKLEDA RKNGYIGVAV
     TALSKDLAFN LGGHTNHSLF WKNLAPNAGG KPTGELLEAI ERDFGSFEDF QAHFEAAALG
     LQGSGWAVLA WDTIGERLVI EQMTDQQGNL SIDLRPLLLL DMWEHAFYLQ YKNVKADYVK
     AVWNVFNWDE VAKRYAAAK
//
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