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Database: UniProt
Entry: A3IN68_9CYAN
LinkDB: A3IN68_9CYAN
Original site: A3IN68_9CYAN 
ID   A3IN68_9CYAN            Unreviewed;       200 AA.
AC   A3IN68;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   16-JAN-2019, entry version 55.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=CY0110_00265 {ECO:0000313|EMBL:EAZ92045.1};
OS   Cyanothece sp. CCY0110.
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC   Cyanothecaceae; Cyanothece.
OX   NCBI_TaxID=391612 {ECO:0000313|EMBL:EAZ92045.1, ECO:0000313|Proteomes:UP000003781};
RN   [1] {ECO:0000313|EMBL:EAZ92045.1, ECO:0000313|Proteomes:UP000003781}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCY0110 {ECO:0000313|EMBL:EAZ92045.1,
RC   ECO:0000313|Proteomes:UP000003781};
RA   Stal L., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (MAR-2007) 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:EAZ92045.1}.
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DR   EMBL; AAXW01000009; EAZ92045.1; -; Genomic_DNA.
DR   RefSeq; WP_008274833.1; NZ_AAXW01000009.1.
DR   ProteinModelPortal; A3IN68; -.
DR   STRING; 391612.CY0110_00265; -.
DR   EnsemblBacteria; EAZ92045; EAZ92045; CY0110_00265.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   BioCyc; CSP391612:G10T1-2306-MONOMER; -.
DR   Proteomes; UP000003781; 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:UP000003781};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN        3     87       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       94    194       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        79     79       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       161    161       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       165    165       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   200 AA;  22244 MW;  7FCA095FB6ECDE75 CRC64;
     MGYELPKLPY DYTALEPHIS KSTLEFHHDK HHASYVSKYN AAVEGTDHDS KPIEEVIKAI
     AGDASKQGLF NNAAQAWNHS FYWNCMKPGG GGQPTGALAD KINADFGSFD KFVEEFKNAG
     ATQFGSGWAW LVLNNGTLKV VKTLNAENPI TSGQTPLLTM DVWEHAYYLD YQNSRPGYID
     TFINNLINWD FVADNMSKAS
//
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