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Database: UniProt/SWISS-PROT
Entry: SODF_MYCTO
LinkDB: SODF_MYCTO
Original site: SODF_MYCTO 
ID   SODF_MYCTO              Reviewed;         207 AA.
AC   P9WGE6; L0TGX2; P17670; P96231;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   28-MAR-2018, entry version 21.
DE   RecName: Full=Superoxide dismutase [Fe];
DE            EC=1.15.1.1;
GN   Name=sodB; Synonyms=sod, sodA; OrderedLocusNames=MT3960;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/JB.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H.,
RA   Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D.,
RA   Salzberg S.L., Delcher A., Utterback T.R., Weidman J.F., Khouri H.M.,
RA   Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C.,
RA   Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC       produced within the cells and which are toxic to biological
CC       systems. {ECO:0000250}.
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: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
CC   -!- CAUTION: Although found extracellularly, no signal sequence is
CC       present. An alternative secretory pathway may be used.
CC       {ECO:0000305}.
DR   EMBL; AE000516; AAK48327.1; -; Genomic_DNA.
DR   PIR; S15205; S15205.
DR   RefSeq; WP_003399735.1; NZ_KK341227.1.
DR   ProteinModelPortal; P9WGE6; -.
DR   SMR; P9WGE6; -.
DR   EnsemblBacteria; AAK48327; AAK48327; MT3960.
DR   KEGG; mtc:MT3960; -.
DR   PATRIC; fig|83331.31.peg.4258; -.
DR   KO; K04564; -.
DR   OrthoDB; POG091H03Q7; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; Iron; Metal-binding; Oxidoreductase; Secreted.
FT   CHAIN         1    207       Superoxide dismutase [Fe].
FT                                /FTId=PRO_0000428375.
FT   METAL        28     28       Iron. {ECO:0000250}.
FT   METAL        76     76       Iron. {ECO:0000250}.
FT   METAL       160    160       Iron. {ECO:0000250}.
FT   METAL       164    164       Iron. {ECO:0000250}.
SQ   SEQUENCE   207 AA;  23034 MW;  DEE8F5921DABE54A CRC64;
     MAEYTLPDLD WDYGALEPHI SGQINELHHS KHHATYVKGA NDAVAKLEEA RAKEDHSAIL
     LNEKNLAFNL AGHVNHTIWW KNLSPNGGDK PTGELAAAIA DAFGSFDKFR AQFHAAATTV
     QGSGWAALGW DTLGNKLLIF QVYDHQTNFP LGIVPLLLLD MWEHAFYLQY KNVKVDFAKA
     FWNVVNWADV QSRYAAATSQ TKGLIFG
//
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