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Database: UniProt
Entry: A0A0W7Y4Y8_9BACI
LinkDB: A0A0W7Y4Y8_9BACI
Original site: A0A0W7Y4Y8_9BACI 
ID   A0A0W7Y4Y8_9BACI        Unreviewed;       201 AA.
AC   A0A0W7Y4Y8;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   05-DEC-2018, entry version 10.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=AK833_17065 {ECO:0000313|EMBL:KUF30176.1};
OS   Lysinibacillus sp. F5.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae;
OC   Lysinibacillus.
OX   NCBI_TaxID=1700846 {ECO:0000313|EMBL:KUF30176.1, ECO:0000313|Proteomes:UP000053086};
RN   [1] {ECO:0000313|EMBL:KUF30176.1, ECO:0000313|Proteomes:UP000053086}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F5 {ECO:0000313|EMBL:KUF30176.1,
RC   ECO:0000313|Proteomes:UP000053086};
RA   Chan X.Y., Chan K.G., Hong K.W., Tan A., Chen J.W.;
RT   "Draft Genome of marine Lysinibacillus sp. F5.";
RL   Submitted (OCT-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}.
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:KUF30176.1}.
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DR   EMBL; LKIE01000084; KUF30176.1; -; Genomic_DNA.
DR   RefSeq; WP_036120319.1; NZ_LKIE01000084.1.
DR   EnsemblBacteria; KUF30176; KUF30176; AK833_17065.
DR   Proteomes; UP000053086; 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:UP000053086};
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:UP000053086}.
FT   DOMAIN        2     88       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       96    195       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        81     81       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   201 AA;  22213 MW;  DDD2DF8F902F47AE CRC64;
     MAYELPQLTY AYDALEPHID AKTMEIHHSK HHNTYVTNLN AAVEGTEFAE KNINDLIANL
     DALPADKQTA VRNNGGGHAN HTLFWEVIAP GGSNTPVGEV AKAIDAKFGS FDAFKEEFAK
     AATTRFGSGW AWLIVDGDSV AVTSTPNQDS PVMEGKTPIL GLDVWEHAYY LNYQNRRPDY
     IGSFWNVVNW DVVEAKFQAA K
//
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