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Database: UniProt/SWISS-PROT
Entry: SODF_SYNY3
LinkDB: SODF_SYNY3
Original site: SODF_SYNY3 
ID   SODF_SYNY3              Reviewed;         199 AA.
AC   P77968;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-OCT-2017, entry version 110.
DE   RecName: Full=Superoxide dismutase [Fe];
DE            EC=1.15.1.1;
GN   Name=sodB; OrderedLocusNames=slr1516;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae;
OC   Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T.,
RA   Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S.,
RA   Shimpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M.,
RA   Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the
RT   entire genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-21.
RX   PubMed=9298645; DOI=10.1002/elps.1150180806;
RA   Sazuka T., Ohara O.;
RT   "Towards a proteome project of cyanobacterium Synechocystis sp. strain
RT   PCC6803: linking 130 protein spots with their respective genes.";
RL   Electrophoresis 18:1252-1258(1997).
CC   -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC       produced within the cells and which are toxic to biological
CC       systems.
CC   -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC       Note=Binds 1 Fe cation per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
DR   EMBL; BA000022; BAA18027.1; -; Genomic_DNA.
DR   PIR; S75466; S75466.
DR   ProteinModelPortal; P77968; -.
DR   SMR; P77968; -.
DR   STRING; 1148.SYNGTS_1451; -.
DR   PRIDE; P77968; -.
DR   EnsemblBacteria; BAA18027; BAA18027; BAA18027.
DR   KEGG; syn:slr1516; -.
DR   HOGENOM; HOG000013584; -.
DR   InParanoid; P77968; -.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   PhylomeDB; P77968; -.
DR   Proteomes; UP000001425; Chromosome.
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   1: Evidence at protein level;
KW   Complete proteome; Direct protein sequencing; Iron; Metal-binding;
KW   Oxidoreductase; Reference proteome.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:9298645}.
FT   CHAIN         2    199       Superoxide dismutase [Fe].
FT                                /FTId=PRO_0000160003.
FT   METAL        27     27       Iron. {ECO:0000250}.
FT   METAL        79     79       Iron. {ECO:0000250}.
FT   METAL       161    161       Iron. {ECO:0000250}.
FT   METAL       165    165       Iron. {ECO:0000250}.
SQ   SEQUENCE   199 AA;  21677 MW;  C0CBE22553AC085E CRC64;
     MAYALPNLPY DYTALEPCIS KSTLEFHHDK HHAAYVNNFN NAVAGTDLDN QSIEDVIKAV
     AGDASKAGIF NNAAQAWNHS FYWNCMKPGG GGQPSGALAD KINADFGSFD AFVEAFKQAG
     ATQFGSGWAW LVLDNGTLKV TKTGNAENPM TAGQTPLLTM DVWEHAYYLD YQNRRPDYIA
     DFLGKLVNWD FVAANLAAA
//
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