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Database: UniProt
Entry: R1GS30_9GAMM
LinkDB: R1GS30_9GAMM
Original site: R1GS30_9GAMM 
ID   R1GS30_9GAMM            Unreviewed;       194 AA.
AC   R1GS30;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   16-JAN-2019, entry version 19.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=G113_14170 {ECO:0000313|EMBL:EOD54460.1};
OS   Aeromonas molluscorum 848.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=1268236 {ECO:0000313|EMBL:EOD54460.1, ECO:0000313|Proteomes:UP000013526};
RN   [1] {ECO:0000313|EMBL:EOD54460.1, ECO:0000313|Proteomes:UP000013526}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=848 {ECO:0000313|EMBL:EOD54460.1,
RC   ECO:0000313|Proteomes:UP000013526};
RX   PubMed=23788549;
RA   Spataro N., Farfan M., Albarral V., Sanglas A., Loren J.G.,
RA   Fuste M.C., Bosch E.;
RT   "Draft Genome Sequence of Aeromonas molluscorum Strain 848TT, Isolated
RT   from Bivalve Molluscs.";
RL   Genome Announc. 1:E00382-13(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:EOD54460.1}.
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DR   EMBL; AQGQ01000105; EOD54460.1; -; Genomic_DNA.
DR   RefSeq; WP_005904485.1; NZ_AQGQ01000105.1.
DR   EnsemblBacteria; EOD54460; EOD54460; G113_14170.
DR   PATRIC; fig|1268236.3.peg.2783; -.
DR   OrthoDB; 1440645at2; -.
DR   Proteomes; UP000013526; 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:UP000013526};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN        3     82       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       89    190       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        74     74       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       158    158       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       162    162       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   194 AA;  21630 MW;  AAED95E794982DBA CRC64;
     MAFELPALPY AINALEPHIS QETLEYHHGK HHNTYVVNLN NLVPGTEFEG KSLEEIIKTS
     TGGIFNNAAQ IWNHTFYWHC LSPNGGNEPT GALADAIAKQ FGSFAEFKDA FTKSAIGNFG
     SSWTWLVKKA DGTLAIVNTS NAGCPLTEAG TTPLLTVDLW EHAYYIDFRN MRPKYMETFW
     TLVNWEFVAK NLAA
//
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