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Database: UniProt
Entry: D1B492_SULD5
LinkDB: D1B492_SULD5
Original site: D1B492_SULD5 
ID   D1B492_SULD5            Unreviewed;       232 AA.
AC   D1B492;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   16-JAN-2019, entry version 51.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   OrderedLocusNames=Sdel_1897 {ECO:0000313|EMBL:ACZ12912.1};
OS   Sulfurospirillum deleyianum (strain ATCC 51133 / DSM 6946 / 5175).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Sulfurospirillum.
OX   NCBI_TaxID=525898 {ECO:0000313|EMBL:ACZ12912.1, ECO:0000313|Proteomes:UP000002222};
RN   [1] {ECO:0000313|Proteomes:UP000002222}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51133 / DSM 6946 / 5175
RC   {ECO:0000313|Proteomes:UP000002222};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA   Ivanova N., Ovchinnikova G., Munk A.C., Lu M., Brettin T.,
RA   Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L.,
RA   Markowitz V., Cheng J.F., Hugenholtz P., Woyke T., Wu D., Aumann P.,
RA   Schneider S., Lang E., Spring S., Klenk H.P., Eisen J.A.;
RT   "The complete genome of Sulfurospirillum deleyianum DSM 6946.";
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACZ12912.1, ECO:0000313|Proteomes:UP000002222}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51133 / DSM 6946 / 5175
RC   {ECO:0000313|Proteomes:UP000002222};
RX   PubMed=21304697; DOI=10.4056/sigs.671209;
RA   Sikorski J., Lapidus A., Copeland A., Glavina Del Rio T., Nolan M.,
RA   Lucas S., Chen F., Tice H., Cheng J.F., Saunders E., Bruce D.,
RA   Goodwin L., Pitluck S., Ovchinnikova G., Pati A., Ivanova N.,
RA   Mavromatis K., Chen A., Palaniappan K., Chain P., Land M., Hauser L.,
RA   Chang Y.J., Jeffries C.D., Brettin T., Detter J.C., Han C., Rohde M.,
RA   Lang E., Spring S., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Sulfurospirillum deleyianum type strain
RT   (5175).";
RL   Stand. Genomic Sci. 2:149-157(2010).
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}.
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DR   EMBL; CP001816; ACZ12912.1; -; Genomic_DNA.
DR   RefSeq; WP_012857660.1; NC_013512.1.
DR   ProteinModelPortal; D1B492; -.
DR   STRING; 525898.Sdel_1897; -.
DR   EnsemblBacteria; ACZ12912; ACZ12912; Sdel_1897.
DR   KEGG; sdl:Sdel_1897; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013584; -.
DR   KO; K04564; -.
DR   OMA; HNQFWEM; -.
DR   OrthoDB; 1440645at2; -.
DR   BioCyc; SDEL525898:G1GGM-1939-MONOMER; -.
DR   Proteomes; UP000002222; Chromosome.
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:UP000002222};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:ACZ12912.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002222};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     26       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        27    232       Superoxide dismutase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5003020188.
FT   DOMAIN       30    113       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      121    226       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        54     54       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       105    105       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       193    193       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       197    197       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   232 AA;  26063 MW;  CED2BF8302EC4797 CRC64;
     MFQKSLLRKR WMALVFSWLF VPALMAADAF SLAPLPYGYD ALEPVIDKET MQIHHGKHHQ
     AYVSNLNAQV ATYPELKGMS VEQIMASISK YNAAVRNNGG GHYNHALFWK LMAPVGKGGT
     PSASLSKAIE RDFGSLEKMK EAFEKAGATR FGSGWAWVIV TADKKLAVTS TPNQDNPLMD
     VTEAKGMPIL AADVWEHAYY LKYQNKRADY LKNWWSVVNW NEVNARFDAA MK
//
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