SODC_MYCTU
ID SODC_MYCTU Reviewed; 240 AA.
AC P9WGE9; L0T6G1; P0A608; P96278;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Superoxide dismutase [Cu-Zn];
DE EC=1.15.1.1;
DE Flags: Precursor;
GN Name=sodC; OrderedLocusNames=Rv0432; ORFNames=MTCY22G10.29;
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 [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 [2]
RP CHARACTERIZATION.
RX PubMed=11563965; DOI=10.1042/0264-6021:3590017;
RA D'Orazio M., Folcarelli S., Mariani F., Colizzi V., Rotilio G.,
RA Battistoni A.;
RT "Lipid modification of the Cu,Zn superoxide dismutase from Mycobacterium
RT tuberculosis.";
RL Biochem. J. 359:17-22(2001).
RN [3]
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 [4]
RP X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) OF 33-240 IN COMPLEX WITH COPPER
RP IONS, ABSENCE OF ZINC BINDING, AND SUBUNIT.
RX PubMed=15155722; DOI=10.1074/jbc.m404699200;
RA Spagnolo L., Toro I., D'Orazio M., O'Neill P., Pedersen J.Z., Carugo O.,
RA Rotilio G., Battistoni A., Djinovic-Carugo K.;
RT "Unique features of the sodC-encoded superoxide dismutase from
RT Mycobacterium tuberculosis, a fully functional copper-containing enzyme
RT lacking zinc in the active site.";
RL J. Biol. Chem. 279:33447-33455(2004).
CC -!- FUNCTION: Destroys radicals which are normally produced within the
CC cells and which are toxic to biological systems. May play a role in
CC favoring mycobacterial survival in phagocytes (By similarity).
CC {ECO:0000250}.
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=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Note=Binds 1 copper ion per subunit.;
CC -!- ACTIVITY REGULATION: Inhibited by the copper chelator diethyl
CC dithiocarbamate.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15155722}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC -!- MISCELLANEOUS: Does not bind zinc ions. Has normal enzyme activity in
CC the absence of zinc ions.
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000305}.
CC -!- CAUTION: Lacks two conserved histidine residues that bind copper and
CC zinc. {ECO:0000305}.
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DR EMBL; AL123456; CCP43163.1; -; Genomic_DNA.
DR PIR; F70631; F70631.
DR RefSeq; NP_214946.1; NC_000962.3.
DR RefSeq; WP_003402198.1; NZ_NVQJ01000002.1.
DR PDB; 1PZS; X-ray; 1.63 A; A=33-240.
DR PDBsum; 1PZS; -.
DR AlphaFoldDB; P9WGE9; -.
DR SMR; P9WGE9; -.
DR STRING; 83332.Rv0432; -.
DR PaxDb; P9WGE9; -.
DR DNASU; 886358; -.
DR GeneID; 886358; -.
DR KEGG; mtu:Rv0432; -.
DR TubercuList; Rv0432; -.
DR eggNOG; COG2032; Bacteria.
DR OMA; HADADNF; -.
DR PhylomeDB; P9WGE9; -.
DR Reactome; R-HSA-1222387; Tolerance of reactive oxygen produced by macrophages.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005576; C:extracellular region; HDA:MTBBASE.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; IDA:MTBBASE.
DR GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR GO; GO:0004784; F:superoxide dismutase activity; IDA:MTBBASE.
DR GO; GO:0045454; P:cell redox homeostasis; IMP:MTBBASE.
DR GO; GO:0019430; P:removal of superoxide radicals; IBA:GO_Central.
DR GO; GO:0075136; P:response to host; IEP:MTBBASE.
DR GO; GO:0033194; P:response to hydroperoxide; IMP:MTBBASE.
DR GO; GO:0006979; P:response to oxidative stress; IMP:MTBBASE.
DR GO; GO:0052163; P:symbiont defense to host-produced nitric oxide; IDA:MTBBASE.
DR GO; GO:0052164; P:symbiont defense to host-produced reactive oxygen species; IDA:MTBBASE.
DR CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR Gene3D; 2.60.40.200; -; 1.
DR InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR InterPro; IPR018152; SOD_Cu/Zn_BS.
DR InterPro; IPR001424; SOD_Cu_Zn_dom.
DR PANTHER; PTHR10003; PTHR10003; 1.
DR Pfam; PF00080; Sod_Cu; 1.
DR SUPFAM; SSF49329; SSF49329; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antioxidant; Cell membrane; Copper; Disulfide bond;
KW Lipoprotein; Membrane; Metal-binding; Oxidoreductase; Palmitate;
KW Reference proteome; Signal; Zinc.
FT SIGNAL 1..32
FT /evidence="ECO:0000305"
FT CHAIN 33..240
FT /note="Superoxide dismutase [Cu-Zn]"
FT /id="PRO_0000032840"
FT REGION 36..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 116
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT BINDING 118
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT BINDING 144
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT BINDING 195
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT LIPID 33
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000305"
FT LIPID 33
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000305"
FT DISULFID 123..234
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:1PZS"
FT STRAND 83..92
FT /evidence="ECO:0007829|PDB:1PZS"
FT STRAND 95..108
FT /evidence="ECO:0007829|PDB:1PZS"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:1PZS"
FT STRAND 115..120
FT /evidence="ECO:0007829|PDB:1PZS"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:1PZS"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:1PZS"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:1PZS"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:1PZS"
FT STRAND 171..178
FT /evidence="ECO:0007829|PDB:1PZS"
FT HELIX 181..185
FT /evidence="ECO:0007829|PDB:1PZS"
FT STRAND 191..197
FT /evidence="ECO:0007829|PDB:1PZS"
FT TURN 206..208
FT /evidence="ECO:0007829|PDB:1PZS"
FT HELIX 220..225
FT /evidence="ECO:0007829|PDB:1PZS"
FT STRAND 230..239
FT /evidence="ECO:0007829|PDB:1PZS"
SQ SEQUENCE 240 AA; 23844 MW; AFC08C0B302B84FC CRC64;
MPKPADHRNH AAVSTSVLSA LFLGAGAALL SACSSPQHAS TVPGTTPSIW TGSPAPSGLS
GHDEESPGAQ SLTSTLTAPD GTKVATAKFE FANGYATVTI ATTGVGKLTP GFHGLHIHQV
GKCEPNSVAP TGGAPGNFLS AGGHYHVPGH TGTPASGDLA SLQVRGDGSA MLVTTTDAFT
MDDLLSGAKT AIIIHAGADN FANIPPERYV QVNGTPGPDE TTLTTGDAGK RVACGVIGSG
