SODC_MYCBO
ID SODC_MYCBO Reviewed; 240 AA.
AC P0A609; A0A1R3XVH6; P96278; X2BF16;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Superoxide dismutase [Cu-Zn];
DE EC=1.15.1.1;
DE Flags: Precursor;
GN Name=sodC; OrderedLocusNames=BQ2027_MB0440;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
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.
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; Evidence={ECO:0000305};
CC Note=Binds 1 copper ion per subunit. {ECO:0000305};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000305};
CC -!- ACTIVITY REGULATION: Inhibited by the copper chelator diethyl
CC dithiocarbamate.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor.
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; LT708304; SIT99025.1; -; Genomic_DNA.
DR RefSeq; NP_854103.1; NC_002945.3.
DR RefSeq; WP_003402198.1; NC_002945.4.
DR AlphaFoldDB; P0A609; -.
DR SMR; P0A609; -.
DR PATRIC; fig|233413.5.peg.479; -.
DR OMA; HADADNF; -.
DR Proteomes; UP000001419; Chromosome.
DR GO; GO:0005886; C:plasma membrane; 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 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 3: Inferred from homology;
KW Antioxidant; Cell membrane; Copper; Disulfide bond; Lipoprotein; Membrane;
KW Metal-binding; Oxidoreductase; Palmitate; Signal; Zinc.
FT SIGNAL 1..32
FT /evidence="ECO:0000305"
FT CHAIN 33..240
FT /note="Superoxide dismutase [Cu-Zn]"
FT /id="PRO_0000032837"
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 /evidence="ECO:0000250"
FT BINDING 118
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
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 /evidence="ECO:0000250"
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
