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Database: UniProt/TrEMBL
Entry: I6XIC6_MYCTU
LinkDB: I6XIC6_MYCTU
Original site: I6XIC6_MYCTU 
ID   I6XIC6_MYCTU            Unreviewed;       207 AA.
AC   I6XIC6;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   28-MAR-2018, entry version 44.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=LH57_20970 {ECO:0000313|EMBL:AIR16641.1};
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332 {ECO:0000313|EMBL:AIR16641.1, ECO:0000313|Proteomes:UP000031768};
RN   [1] {ECO:0000313|EMBL:AIR16641.1, ECO:0000313|Proteomes:UP000031768}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27294 / TMC 102 / H37Rv
RC   {ECO:0000313|Proteomes:UP000031768};
RA   Hazbon M.H., Riojas M.A., Damon A.M., Alalade R.O., Cantwell B.J.,
RA   Monaco A., King S., Sohrabi A.;
RT   "Phylogenetic analysis of Mycobacterial species using whole genome
RT   sequences.";
RL   Submitted (SEP-2014) 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; CP009480; AIR16641.1; -; Genomic_DNA.
DR   RefSeq; NP_218363.1; NC_000962.3.
DR   RefSeq; WP_003399735.1; NZ_KK339374.1.
DR   ProteinModelPortal; I6XIC6; -.
DR   SMR; I6XIC6; -.
DR   PRIDE; I6XIC6; -.
DR   EnsemblBacteria; AIR16641; AIR16641; LH57_20970.
DR   GeneID; 886174; -.
DR   KEGG; mtu:Rv3846; -.
DR   KEGG; mtv:RVBD_3846; -.
DR   PATRIC; fig|83332.111.peg.4279; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   PhylomeDB; I6XIC6; -.
DR   Proteomes; UP000031768; 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:UP000031768};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN        3     84       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       91    193       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        28     28       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        76     76       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       160    160       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       164    164       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
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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