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Database: UniProt/TrEMBL
Entry: K7VT96_9NOST
LinkDB: K7VT96_9NOST
Original site: K7VT96_9NOST 
ID   K7VT96_9NOST            Unreviewed;       200 AA.
AC   K7VT96;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   25-OCT-2017, entry version 24.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=ANA_C10606 {ECO:0000313|EMBL:AFW93405.1};
OS   Anabaena sp. 90.
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena.
OX   NCBI_TaxID=46234 {ECO:0000313|EMBL:AFW93405.1, ECO:0000313|Proteomes:UP000010101};
RN   [1] {ECO:0000313|EMBL:AFW93405.1, ECO:0000313|Proteomes:UP000010101}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=90 {ECO:0000313|EMBL:AFW93405.1};
RX   PubMed=23148582; DOI=10.1186/1471-2164-13-613;
RA   Wang H., Sivonen K., Rouhiainen L., Fewer D.P., Lyra C.,
RA   Rantala-Ylinen A., Vestola J., Jokela J., Rantasarkka K., Li Z.,
RA   Liu B.;
RT   "Genome-derived insights into the biology of the hepatotoxic bloom-
RT   forming cyanobacterium Anabaena sp. strain 90.";
RL   BMC Genomics 13:613-613(2012).
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; CP003284; AFW93405.1; -; Genomic_DNA.
DR   RefSeq; WP_015078569.1; NC_019427.1.
DR   ProteinModelPortal; K7VT96; -.
DR   EnsemblBacteria; AFW93405; AFW93405; ANA_C10606.
DR   KEGG; anb:ANA_C10606; -.
DR   PATRIC; fig|46234.3.peg.684; -.
DR   KO; K04564; -.
DR   OrthoDB; POG091H03Q7; -.
DR   Proteomes; UP000010101; Chromosome chANA01.
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:UP000010101};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:AFW93405.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010101}.
FT   DOMAIN        3     88       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       95    195       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        28     28       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        80     80       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       162    162       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       166    166       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   200 AA;  22112 MW;  E897E4026704AD3B CRC64;
     MAFTQLALPF ASDALESYGM KAETFEYHYG KHHKAYVDNL NKLVDGTELA NKSLEEVIQI
     AFGDSAKAGI FNNAAQVWNH SFFWNCLKPA GGGAPTGALA AKIEQDFGSF EKFKEEFSTA
     AATQFGSGWA WLVDDGGTLK VMKTPNAENP LAHGKKALLT IDVWEHAYYI DFKNARPGFI
     KNFLDNLVNW DFVAENFAKA
//
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