SODF_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 03-AUG-2022, entry version 42.
DE RecName: Full=Superoxide dismutase [Fe];
DE EC=1.15.1.1 {ECO:0000269|PubMed:1904126, ECO:0000269|PubMed:9933629};
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], FUNCTION, CATALYTIC ACTIVITY, AND
RP SUBCELLULAR LOCATION.
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 of
RT Mycobacterium tuberculosis.";
RL Mol. Microbiol. 5:381-391(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-11, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
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 is
RT dependent upon both information in the protein and mycobacterial export
RT machinery. A model for studying export of leaderless proteins by pathogenic
RT 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., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT 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 "Prokaryotic 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., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [6] {ECO:0007744|PDB:1IDS}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH IRON, AND SUBUNIT.
RX PubMed=7877174; DOI=10.1006/jmbi.1994.0105;
RA Cooper J.B., McIntyre K., Badasso M.O., Wood S.P., Zhang Y., Garbe T.R.,
RA Young D.;
RT "X-ray structure analysis of the iron-dependent superoxide dismutase from
RT Mycobacterium tuberculosis at 2.0-A resolution reveals novel dimer-dimer
RT interactions.";
RL J. Mol. Biol. 246:531-544(1995).
RN [7] {ECO:0007744|PDB:1GN6}
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF MUTANT ALA-152 IN COMPLEX WITH
RP IRON.
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., Zhang Y.,
RA Young D.;
RT "X-ray structure analysis of an engineered Fe-superoxide dismutase Gly-Ala
RT mutant with significantly reduced stability to denaturant.";
RL FEBS Lett. 387:105-108(1996).
RN [8] {ECO:0007744|PDB:1GN3, ECO:0007744|PDB:1GN4}
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF MUTANTS GLN-145 AND GLU-145 IN
RP COMPLEX WITH IRON AND MANGANESE.
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., Wood S.P.,
RA 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] {ECO:0007744|PDB:1GN2}
RP X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF MUTANT CYS-123 IN COMPLEX WITH
RP IRON.
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-superoxide
RT 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 systems.
CC {ECO:0000269|PubMed:1904126, ECO:0000269|PubMed:9933629}.
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; Evidence={ECO:0000269|PubMed:1904126,
CC ECO:0000269|PubMed:9933629};
CC -!- COFACTOR:
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC Evidence={ECO:0000269|PubMed:9933629};
CC Note=Binds 1 Fe(3+) cation per subunit. {ECO:0000269|PubMed:11747311,
CC ECO:0000269|PubMed:7877174, ECO:0000269|PubMed:8674528,
CC ECO:0000269|PubMed:9490054};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:7877174,
CC ECO:0000269|PubMed:9933629}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1904126,
CC ECO:0000269|PubMed:9933629}.
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000305}.
CC -!- CAUTION: Although found extracellularly, no signal sequence is present.
CC An alternative secretory pathway may be used.
CC {ECO:0000305|PubMed:1904126, ECO:0000305|PubMed:9933629}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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_NVQJ01000057.1.
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 AlphaFoldDB; P9WGE7; -.
DR SMR; P9WGE7; -.
DR STRING; 83332.Rv3846; -.
DR PaxDb; P9WGE7; -.
DR ABCD; P9WGE7; 1 sequenced antibody.
DR DNASU; 886174; -.
DR GeneID; 45427849; -.
DR GeneID; 886174; -.
DR KEGG; mtu:Rv3846; -.
DR TubercuList; Rv3846; -.
DR eggNOG; COG0605; Bacteria.
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; HDA: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; HDA:MTBBASE.
DR GO; GO:0005506; F:iron ion binding; IDA:MTBBASE.
DR GO; GO:0030145; F:manganese ion binding; IBA:GO_Central.
DR GO; GO:0004784; F:superoxide dismutase activity; IDA:MTBBASE.
DR GO; GO:0098754; P:detoxification; IMP:MTBBASE.
DR GO; GO:0006979; P:response to oxidative stress; IMP:MTBBASE.
DR Gene3D; 1.10.287.990; -; 1.
DR Gene3D; 3.55.40.20; -; 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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Iron; Isopeptide bond;
KW Metal-binding; Oxidoreductase; Reference proteome; Secreted;
KW Ubl conjugation.
FT CHAIN 1..207
FT /note="Superoxide dismutase [Fe]"
FT /id="PRO_0000159990"
FT BINDING 28
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000269|PubMed:11747311,
FT ECO:0000269|PubMed:7877174, ECO:0000269|PubMed:8674528,
FT ECO:0000269|PubMed:9490054, ECO:0007744|PDB:1GN2,
FT ECO:0007744|PDB:1GN3, ECO:0007744|PDB:1GN6,
FT ECO:0007744|PDB:1IDS"
FT BINDING 76
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000269|PubMed:11747311,
FT ECO:0000269|PubMed:7877174, ECO:0000269|PubMed:8674528,
FT ECO:0000269|PubMed:9490054, ECO:0007744|PDB:1GN2,
FT ECO:0007744|PDB:1GN3, ECO:0007744|PDB:1GN6,
FT ECO:0007744|PDB:1IDS"
FT BINDING 160
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000269|PubMed:11747311,
FT ECO:0000269|PubMed:7877174, ECO:0000269|PubMed:8674528,
FT ECO:0000269|PubMed:9490054, ECO:0007744|PDB:1GN2,
FT ECO:0007744|PDB:1GN3, ECO:0007744|PDB:1GN6,
FT ECO:0007744|PDB:1IDS"
FT BINDING 164
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000269|PubMed:11747311,
FT ECO:0000269|PubMed:7877174, ECO:0000269|PubMed:8674528,
FT ECO:0000269|PubMed:9490054, ECO:0007744|PDB:1GN2,
FT ECO:0007744|PDB:1GN3, ECO:0007744|PDB:1GN6,
FT ECO:0007744|PDB:1IDS"
FT CROSSLNK 202
FT /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT with Q-Cter in protein Pup)"
FT /evidence="ECO:0000269|PubMed:20066036"
FT TURN 13..19
FT /evidence="ECO:0007829|PDB:1IDS"
FT HELIX 22..30
FT /evidence="ECO:0007829|PDB:1IDS"
FT HELIX 32..52
FT /evidence="ECO:0007829|PDB:1IDS"
FT HELIX 59..82
FT /evidence="ECO:0007829|PDB:1IDS"
FT HELIX 93..103
FT /evidence="ECO:0007829|PDB:1IDS"
FT HELIX 106..118
FT /evidence="ECO:0007829|PDB:1IDS"
FT STRAND 121..131
FT /evidence="ECO:0007829|PDB:1IDS"
FT TURN 132..135
FT /evidence="ECO:0007829|PDB:1IDS"
FT STRAND 136..143
FT /evidence="ECO:0007829|PDB:1IDS"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:1IDS"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:1IDS"
FT STRAND 153..160
FT /evidence="ECO:0007829|PDB:1IDS"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:1IDS"
FT HELIX 167..170
FT /evidence="ECO:0007829|PDB:1IDS"
FT HELIX 174..180
FT /evidence="ECO:0007829|PDB:1IDS"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:1IDS"
FT HELIX 187..198
FT /evidence="ECO:0007829|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
