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Entry: SODF_MYCTU I6XIC6_MYCTU
LinkDB: SODF_MYCTU I6XIC6_MYCTU
Original site: SODF_MYCTU I6XIC6_MYCTU 
ID   SODF_MYCTU              Reviewed;         207 AA.
AC   P9WGE7; L0TGX2; P17670; P96231;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   07-JUN-2017, entry version 23.
DE   RecName: Full=Superoxide dismutase [Fe];
DE            EC=1.15.1.1;
GN   Name=sodB; Synonyms=sod, sodA; OrderedLocusNames=Rv3846;
GN   ORFNames=MTCY01A6.22c;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX   PubMed=1904126; DOI=10.1111/j.1365-2958.1991.tb02120.x;
RA   Zhang Y.;
RT   "Genetic analysis of superoxide dismutase, the 23 kilodalton antigen
RT   of Mycobacterium tuberculosis.";
RL   Mol. Microbiol. 5:381-391(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC   STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX   PubMed=9933629; DOI=10.1074/jbc.274.7.4281;
RA   Harth G., Horwitz M.A.;
RT   "Export of recombinant Mycobacterium tuberculosis superoxide dismutase
RT   is dependent upon both information in the protein and mycobacterial
RT   export machinery. A model for studying export of leaderless proteins
RT   by pathogenic mycobacteria.";
RL   J. Biol. Chem. 274:4281-4292(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
RA   Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
RA   Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
RA   Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
RA   Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
RA   Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
RA   Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the
RT   complete genome sequence.";
RL   Nature 393:537-544(1998).
RN   [4]
RP   PUPYLATION AT LYS-202, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=20066036; DOI=10.1371/journal.pone.0008589;
RA   Festa R.A., McAllister F., Pearce M.J., Mintseris J., Burns K.E.,
RA   Gygi S.P., Darwin K.H.;
RT   "Prokayrotic ubiquitin-like protein (Pup) proteome of Mycobacterium
RT   tuberculosis.";
RL   PLoS ONE 5:E8589-E8589(2010).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.M111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B.,
RA   Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
RA   Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
RA   Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
RA   Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high
RT   resolution mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX   PubMed=7877174; DOI=10.1006/jmbi.1994.0105;
RA   Cooper J.B., McIntyre K., Badasso M.O., Wood S.P., Zhang Y.,
RA   Garbe T.R., Young D.;
RT   "X-ray structure analysis of the iron-dependent superoxide dismutase
RT   from Mycobacterium tuberculosis at 2.0-A resolution reveals novel
RT   dimer-dimer interactions.";
RL   J. Mol. Biol. 246:531-544(1995).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF MUTANT ALA-152.
RX   PubMed=8674528; DOI=10.1016/0014-5793(96)00490-5;
RA   Cooper J.B., Saward S., Erskine P.T., Badasso M.O., Wood S.P.,
RA   Zhang Y., Young D.;
RT   "X-ray structure analysis of an engineered Fe-superoxide dismutase
RT   Gly-Ala mutant with significantly reduced stability to denaturant.";
RL   FEBS Lett. 387:105-108(1996).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF MUTANTS GLN-145 AND GLU-145.
RX   PubMed=9490054; DOI=10.1046/j.1432-1327.1998.2510795.x;
RA   Bunting K., Cooper J.B., Badasso M.O., Tickle I.J., Newton M.,
RA   Wood S.P., Zhang Y., Young D.B.;
RT   "Engineering a change in metal-ion specificity of the iron-dependent
RT   superoxide dismutase from Mycobacterium tuberculosis -X-ray structure
RT   analysis of site-directed mutants.";
RL   Eur. J. Biochem. 251:795-803(1998).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF MUTANT CYS-123.
RX   PubMed=11747311; DOI=10.1006/abbi.2001.2635;
RA   Bunting K., Cooper J.B., Tickle I.J., Young D.B.;
RT   "Engineering of an intersubunit disulfide bridge in the iron-
RT   superoxide dismutase of Mycobacterium tuberculosis.";
RL   Arch. Biochem. Biophys. 397:69-76(2002).
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: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC       Note=Binds 1 Fe cation per subunit.;
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Secreted.
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; X52861; CAA37042.1; -; Genomic_DNA.
DR   EMBL; AF061030; AAD15824.1; -; Genomic_DNA.
DR   EMBL; AL123456; CCP46675.1; -; Genomic_DNA.
DR   PIR; S15205; S15205.
DR   RefSeq; NP_218363.1; NC_000962.3.
DR   RefSeq; WP_003399735.1; NZ_KK339374.1.
DR   PDB; 1GN2; X-ray; 3.40 A; A/B/C/D/E/F/G/H=1-207.
DR   PDB; 1GN3; X-ray; 4.00 A; A/B=1-207.
DR   PDB; 1GN4; X-ray; 2.50 A; A/B/C/D=1-207.
DR   PDB; 1GN6; X-ray; 2.90 A; A/B/C/D=1-207.
DR   PDB; 1IDS; X-ray; 2.00 A; A/B/C/D=1-207.
DR   PDBsum; 1GN2; -.
DR   PDBsum; 1GN3; -.
DR   PDBsum; 1GN4; -.
DR   PDBsum; 1GN6; -.
DR   PDBsum; 1IDS; -.
DR   ProteinModelPortal; P9WGE7; -.
DR   SMR; P9WGE7; -.
DR   STRING; 83332.Rv3846; -.
DR   PaxDb; P9WGE7; -.
DR   EnsemblBacteria; CCP46675; CCP46675; Rv3846.
DR   GeneID; 886174; -.
DR   KEGG; mtu:Rv3846; -.
DR   TubercuList; Rv3846; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   PhylomeDB; P9WGE7; -.
DR   Reactome; R-HSA-1222387; Tolerance of reactive oxygen produced by macrophages.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:MTBBASE.
DR   GO; GO:0005576; C:extracellular region; IDA:MTBBASE.
DR   GO; GO:0042597; C:periplasmic space; TAS:Reactome.
DR   GO; GO:0005886; C:plasma membrane; IDA:MTBBASE.
DR   GO; GO:0005506; F:iron ion binding; IDA:MTBBASE.
DR   GO; GO:0004784; F:superoxide dismutase activity; IDA:MTBBASE.
DR   GO; GO:0052059; P:evasion or tolerance by symbiont of host-produced reactive oxygen species; TAS:Reactome.
DR   GO; GO:0009405; P:pathogenesis; IMP:MTBBASE.
DR   GO; GO:0006979; P:response to oxidative stress; IMP:MTBBASE.
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   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Iron; Isopeptide bond; Metal-binding;
KW   Oxidoreductase; Reference proteome; Secreted; Ubl conjugation.
FT   CHAIN         1    207       Superoxide dismutase [Fe].
FT                                /FTId=PRO_0000159990.
FT   METAL        28     28       Iron.
FT   METAL        76     76       Iron.
FT   METAL       160    160       Iron.
FT   METAL       164    164       Iron.
FT   CROSSLNK    202    202       Isoglutamyl lysine isopeptide (Lys-Gln)
FT                                (interchain with Q-Cter in protein Pup).
FT                                {ECO:0000269|PubMed:20066036}.
FT   TURN         13     19       {ECO:0000244|PDB:1IDS}.
FT   HELIX        22     30       {ECO:0000244|PDB:1IDS}.
FT   HELIX        32     52       {ECO:0000244|PDB:1IDS}.
FT   HELIX        59     82       {ECO:0000244|PDB:1IDS}.
FT   HELIX        93    103       {ECO:0000244|PDB:1IDS}.
FT   HELIX       106    118       {ECO:0000244|PDB:1IDS}.
FT   STRAND      121    131       {ECO:0000244|PDB:1IDS}.
FT   TURN        132    135       {ECO:0000244|PDB:1IDS}.
FT   STRAND      136    143       {ECO:0000244|PDB:1IDS}.
FT   TURN        144    146       {ECO:0000244|PDB:1IDS}.
FT   STRAND      147    149       {ECO:0000244|PDB:1IDS}.
FT   STRAND      153    160       {ECO:0000244|PDB:1IDS}.
FT   HELIX       163    165       {ECO:0000244|PDB:1IDS}.
FT   HELIX       167    170       {ECO:0000244|PDB:1IDS}.
FT   HELIX       174    180       {ECO:0000244|PDB:1IDS}.
FT   HELIX       181    183       {ECO:0000244|PDB:1IDS}.
FT   HELIX       187    198       {ECO:0000244|PDB:1IDS}.
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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Ontology (9)   
   GO (9)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (4)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   TUBERCULIST (1)   
Protein sequence (5)   
   RefSeq(pep) (2)   
   PMD (3)   
DNA sequence (3)   
   EMBL (3)   
3D Structure (5)   
   PDB (5)   
Protein domain (7)   
   InterPro (4)   
   Pfam (2)   
   PROSITE (1)   
Literature (9)   
   PubMed (9)   
All databases (43)   

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ID   I6XIC6_MYCTU            Unreviewed;       207 AA.
AC   I6XIC6;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   05-JUL-2017, entry version 41.
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   PaxDb; 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   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: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
//
  All links  
Ontology (2)   
   GO (2)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (4)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (2)   
   NCBI-Gene (1)   
Protein sequence (2)   
   RefSeq(pep) (2)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (7)   
   InterPro (4)   
   Pfam (2)   
   PROSITE (1)   
All databases (17)   

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