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Database: UniProt/TrEMBL
Entry: G0GB51_SPITZ
LinkDB: G0GB51_SPITZ
Original site: G0GB51_SPITZ 
ID   G0GB51_SPITZ            Unreviewed;       206 AA.
AC   G0GB51;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   07-JUN-2017, entry version 27.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   OrderedLocusNames=Spith_0799 {ECO:0000313|EMBL:AEJ61075.1};
OS   Spirochaeta thermophila (strain ATCC 700085 / DSM 6578 / Z-1203).
OC   Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Spirochaeta.
OX   NCBI_TaxID=869211 {ECO:0000313|EMBL:AEJ61075.1, ECO:0000313|Proteomes:UP000007254};
RN   [1] {ECO:0000313|EMBL:AEJ61075.1, ECO:0000313|Proteomes:UP000007254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700085 / DSM 6578 / Z-1203
RC   {ECO:0000313|Proteomes:UP000007254};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Mikailova N., Pagani I.,
RA   Chertkov O., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S.,
RA   Merkhoffer B., Schneider S., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Spirochaeta thermophila DSM 6578.";
RL   Submitted (JUN-2011) 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: 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; CP002903; AEJ61075.1; -; Genomic_DNA.
DR   RefSeq; WP_014624452.1; NC_017583.1.
DR   EnsemblBacteria; AEJ61075; AEJ61075; Spith_0799.
DR   KEGG; stq:Spith_0799; -.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   OrthoDB; POG091H03Q7; -.
DR   BioCyc; STHE869211:GLKE-806-MONOMER; -.
DR   Proteomes; UP000007254; 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   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:UP000007254};
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:UP000007254}.
FT   DOMAIN        2     90       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       97    198       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        82     82       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       165    165       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       169    169       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   206 AA;  23063 MW;  44BBCB5C4D78B808 CRC64;
     MSFTLPSLPY PYDALEPHID ARTMEIHHTK HHAGYVNNLN AALEKAPAAK DKDLVFLLRN
     LKSLPEEVQT AVRNNGGGHA NHSLFWTVLS PKGGGTPRDA VGKAIASTFG SFDAFKEAFS
     KAAATRFGSG WAWLVVNAYG ELQVYSTPNQ DSPYMDGFIP ILGLDVWEHA YYLSYQNRRP
     DYIAAFWNVV NWEEVERRYK EALASL
//
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