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Database: UniProt
Entry: O35023
LinkDB: O35023
Original site: O35023 
ID   SODF_BACSU              Reviewed;         281 AA.
AC   O35023;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   05-DEC-2018, entry version 116.
DE   RecName: Full=Probable superoxide dismutase [Fe];
DE            EC=1.15.1.1;
GN   Name=sodF; OrderedLocusNames=BSU19330;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT   "Sequence analysis of the Bacillus subtilis chromosome region between
RT   the terC and odhAB loci cloned in a yeast artificial chromosome.";
RL   Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(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:
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   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC       Note=Binds 1 Fe cation per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
DR   EMBL; AF027868; AAB84442.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13825.1; -; Genomic_DNA.
DR   PIR; C69709; C69709.
DR   RefSeq; NP_389815.1; NC_000964.3.
DR   RefSeq; WP_004399227.1; NZ_JNCM01000036.1.
DR   ProteinModelPortal; O35023; -.
DR   SMR; O35023; -.
DR   IntAct; O35023; 1.
DR   STRING; 224308.Bsubs1_010100010671; -.
DR   PaxDb; O35023; -.
DR   PRIDE; O35023; -.
DR   EnsemblBacteria; CAB13825; CAB13825; BSU19330.
DR   GeneID; 939503; -.
DR   KEGG; bsu:BSU19330; -.
DR   PATRIC; fig|224308.179.peg.2114; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013583; -.
DR   InParanoid; O35023; -.
DR   KO; K04564; -.
DR   OMA; YLHSIFW; -.
DR   PhylomeDB; O35023; -.
DR   BioCyc; BSUB:BSU19330-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IBA:GO_Central.
DR   GO; GO:0004784; F:superoxide dismutase activity; IBA:GO_Central.
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   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; Iron; Metal-binding; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN         1    281       Probable superoxide dismutase [Fe].
FT                                /FTId=PRO_0000160112.
FT   METAL       104    104       Iron. {ECO:0000250}.
FT   METAL       152    152       Iron. {ECO:0000250}.
FT   METAL       236    236       Iron. {ECO:0000250}.
FT   METAL       240    240       Iron. {ECO:0000250}.
SQ   SEQUENCE   281 AA;  33477 MW;  7F36AC0A60E74DB0 CRC64;
     MKRESYQAEM FNWCEALKDQ IQKRGQLDQF EDQIDKMIEA LEDDQTTEED WYKQAAALYR
     DITESDDTSE RRAYVPIGKH VLPKLPYKYS ALEPYISRDI MILHHTKHHQ SYVDGLNKAE
     SELKKARATK NYDLITHWER ELAFHGAGHY LHSIFWFSMH PNGKRRPTGA LFQMIDLSFG
     SYSAFKEHFT QASKKVEGVG WAILVWAPRS GRLEILTAEK HQLFSQWDVI PLLPLDVWEH
     AYYLQYKNDR ASYVDHWWNV VDWREAEKRF EQAKEVVWKL Y
//
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