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Database: UniProt
Entry: A0A0F4QFQ6_9GAMM
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Original site: A0A0F4QFQ6_9GAMM 
ID   A0A0F4QFQ6_9GAMM        Unreviewed;       193 AA.
AC   A0A0F4QFQ6;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   05-DEC-2018, entry version 13.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=TW77_20025 {ECO:0000313|EMBL:KJZ06149.1};
OS   Pseudoalteromonas rubra.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=43658 {ECO:0000313|EMBL:KJZ06149.1, ECO:0000313|Proteomes:UP000033452};
RN   [1] {ECO:0000313|EMBL:KJZ06149.1, ECO:0000313|Proteomes:UP000033452}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2471 {ECO:0000313|EMBL:KJZ06149.1,
RC   ECO:0000313|Proteomes:UP000033452};
RX   PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA   Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT   "Genome mining reveals unlocked bioactive potential of marine Gram-
RT   negative bacteria.";
RL   BMC Genomics 16:158-158(2015).
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:KJZ06149.1}.
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DR   EMBL; JXYA01000054; KJZ06149.1; -; Genomic_DNA.
DR   RefSeq; WP_046006742.1; NZ_JXYA01000054.1.
DR   EnsemblBacteria; KJZ06149; KJZ06149; TW77_20025.
DR   PATRIC; fig|43658.5.peg.4229; -.
DR   Proteomes; UP000033452; 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:UP000033452};
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:UP000033452}.
FT   DOMAIN        3     81       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   193 AA;  21596 MW;  7C51171CC518C9EC CRC64;
     MAFELPSLPY AINALEPHIS QETLEFHHGK HHNTYVVKLN GLIQGTDLEN KSLEEIVCNS
     EGGVFNNAAQ IWNHTFYWHS LAPNGGGEPT GKVAELINAK WGSFAAFQEA FNDKAVNNFG
     SSWTWLVQLA DGSLDIVNTS NAATPLTEEG VTPIITVDLW EHAYYIDYRN VRPDYLKGFW
     ALVNWDFANE NLA
//
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