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Database: UniProt
Entry: M7NBI4_9BACL
LinkDB: M7NBI4_9BACL
Original site: M7NBI4_9BACL 
ID   M7NBI4_9BACL            Unreviewed;       201 AA.
AC   M7NBI4;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-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   Name=sodA {ECO:0000313|EMBL:EMR05933.1};
GN   ORFNames=C772_02204 {ECO:0000313|EMBL:EMR05933.1};
OS   Bhargavaea cecembensis DSE10.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae; Bhargavaea.
OX   NCBI_TaxID=1235279 {ECO:0000313|EMBL:EMR05933.1, ECO:0000313|Proteomes:UP000011919};
RN   [1] {ECO:0000313|EMBL:EMR05933.1, ECO:0000313|Proteomes:UP000011919}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSE10 {ECO:0000313|EMBL:EMR05933.1,
RC   ECO:0000313|Proteomes:UP000011919};
RX   PubMed=23766406;
RA   Shivaji S., Ara S., Begum Z., Ruth M., Singh A., Kumar Pinnaka A.;
RT   "Draft Genome Sequence of Bhargavaea cecembensis Strain DSE10T,
RT   Isolated from a Deep-Sea Sediment Sample Collected at a Depth of 5,904
RT   m from the Chagos-Laccadive Ridge System in the Indian Ocean.";
RL   Genome Announc. 1:e00346-13(2013).
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:EMR05933.1}.
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DR   EMBL; AOFT01000010; EMR05933.1; -; Genomic_DNA.
DR   RefSeq; WP_008299949.1; NZ_AOFT01000010.1.
DR   EnsemblBacteria; EMR05933; EMR05933; C772_02204.
DR   PATRIC; fig|1235279.3.peg.2210; -.
DR   OrthoDB; 1440645at2; -.
DR   BioCyc; BCEC1235279:G1HG2-2179-MONOMER; -.
DR   Proteomes; UP000011919; 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:UP000011919};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:EMR05933.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011919}.
FT   DOMAIN        3     89       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       96    196       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;  22625 MW;  6E6D020BF397B08D CRC64;
     MAFKLPELPY AYDALEPSID KETMEIHHTK HHNTYVTNLN AAVEGTDLAE KSIEDVLRNF
     DSVPEDKKTA VRNNGGGHAN HSLFWQILSP NGGGQPSGAL AEAIDKKFGS FDKFKEEFET
     AAKGRFGSGW AWLVVNNGEV EVTSTANQDS PLMEGKTPVL GLDVWEHAYY LKYQNRRPEY
     ASAFWNVVNW EEVSKRYEEA K
//
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