ID A0A045J2K2_MYCTX Unreviewed; 240 AA.
AC A0A045J2K2;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN Name=sodC {ECO:0000313|EMBL:SGH34044.1};
GN ORFNames=A4S10_00458 {ECO:0000313|EMBL:OMH58309.1}, ERS007679_01806
GN {ECO:0000313|EMBL:COV41997.1}, ERS007681_02027
GN {ECO:0000313|EMBL:CFE39643.1}, ERS007688_00844
GN {ECO:0000313|EMBL:CFE47727.1}, ERS007720_01916
GN {ECO:0000313|EMBL:COW17610.1}, ERS007739_01141
GN {ECO:0000313|EMBL:COX35401.1}, ERS007741_01316
GN {ECO:0000313|EMBL:COW04990.1}, ERS027646_00218
GN {ECO:0000313|EMBL:CKR61870.1}, ERS027659_01203
GN {ECO:0000313|EMBL:CKR35140.1}, ERS027661_03006
GN {ECO:0000313|EMBL:CKS38543.1}, ERS053720_01016
GN {ECO:0000313|EMBL:CFH74432.1}, GJE03_02255
GN {ECO:0000313|EMBL:QGK77749.1}, SAMEA2683035_00905
GN {ECO:0000313|EMBL:SGH34044.1};
OS Mycobacterium tuberculosis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=1773 {ECO:0000313|EMBL:SGH34044.1, ECO:0000313|Proteomes:UP000182946};
RN [1] {ECO:0000313|EMBL:CFH74432.1, ECO:0000313|Proteomes:UP000046674}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0351H {ECO:0000313|EMBL:CFH74432.1,
RC ECO:0000313|Proteomes:UP000046674}, and N09902308
RC {ECO:0000313|EMBL:COX35401.1};
RG Pathogen Informatics;
RA Murphy D.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OMH58309.1, ECO:0000313|Proteomes:UP000189452}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6548 {ECO:0000313|EMBL:OMH58309.1,
RC ECO:0000313|Proteomes:UP000189452};
RA Bigi M., Bigi F., Soria M.A.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:SGH34044.1, ECO:0000313|Proteomes:UP000182946}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2926STDY5723788 {ECO:0000313|EMBL:SGH34044.1,
RC ECO:0000313|Proteomes:UP000182946}, Bir 172
RC {ECO:0000313|EMBL:CKR61870.1, ECO:0000313|Proteomes:UP000048948}, Bir
RC 185 {ECO:0000313|EMBL:CKR35140.1, ECO:0000313|Proteomes:UP000050164},
RC Bir 187 {ECO:0000313|EMBL:CKS38543.1,
RC ECO:0000313|Proteomes:UP000049023}, G09801536
RC {ECO:0000313|EMBL:COV41997.1, ECO:0000313|Proteomes:UP000045842},
RC G09901357 {ECO:0000313|EMBL:CFE39643.1,
RC ECO:0000313|Proteomes:UP000048289}, H09601792
RC {ECO:0000313|EMBL:CFE47727.1, ECO:0000313|Proteomes:UP000046947},
RC M09401471 {ECO:0000313|EMBL:COW17610.1,
RC ECO:0000313|Proteomes:UP000044938}, N09902308
RC {ECO:0000313|Proteomes:UP000039021}, and P00601463
RC {ECO:0000313|EMBL:COW04990.1, ECO:0000313|Proteomes:UP000048600};
RG Pathogen Informatics;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:OMH58309.1, ECO:0000313|Proteomes:UP000189452}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6548 {ECO:0000313|EMBL:OMH58309.1,
RC ECO:0000313|Proteomes:UP000189452};
RA Bigi M.M., Lopez B., Blanco F.C., Sasiain M.C., De La Barrera S.,
RA Ritacco V., Bigi F., Soria M.A.;
RT "Protein polymorphisms may explain contrasting epidemiological fitness of
RT two variants of a multidrug-resistant Mycobacterium tuberculosis strain.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:QGK77749.1, ECO:0000313|Proteomes:UP000388593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AUSMDU00018547 {ECO:0000313|EMBL:QGK77749.1,
RC ECO:0000313|Proteomes:UP000388593};
RA Baines S.L., Goncalves da Silva A., Carter G.P., Jennison A.V.,
RA Rathnayake I.U., Graham R.M.A., Sintchenko V., Wang Q., Rockett R.J.,
RA Timms V.J., Martinez E., Ballard S., Tomita T., Isles N., Horan K.A.,
RA Pitchers W., Stinear T.P., Williamson D.A., Howden B.P., Seemann T.;
RT "Complete microbial genomes for public health in Australia and Southwest
RT Pacific.";
RL Submitted (NOV-2019) 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. May play a role in
CC favoring mycobacterial survival in phagocytes.
CC {ECO:0000256|ARBA:ARBA00024900}.
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 Evidence={ECO:0000256|RuleBase:RU000393};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000256|RuleBase:RU000393};
CC Note=Binds 1 copper ion per subunit. {ECO:0000256|RuleBase:RU000393};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU000393};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU000393};
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000256|RuleBase:RU000393}.
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DR EMBL; CFOE01000239; CFE39643.1; -; Genomic_DNA.
DR EMBL; CFOH01000091; CFE47727.1; -; Genomic_DNA.
DR EMBL; CFSW01000005; CFH74432.1; -; Genomic_DNA.
DR EMBL; CNFT01000207; CKR35140.1; -; Genomic_DNA.
DR EMBL; CNGE01000019; CKR61870.1; -; Genomic_DNA.
DR EMBL; CNFU01000717; CKS38543.1; -; Genomic_DNA.
DR EMBL; CSAD01000213; COV41997.1; -; Genomic_DNA.
DR EMBL; CHKL01000110; COW04990.1; -; Genomic_DNA.
DR EMBL; CSAJ01000216; COW17610.1; -; Genomic_DNA.
DR EMBL; CSBK01000400; COX35401.1; -; Genomic_DNA.
DR EMBL; LWDQ01000001; OMH58309.1; -; Genomic_DNA.
DR EMBL; CP045962; QGK77749.1; -; Genomic_DNA.
DR EMBL; FPTZ01000004; SGH34044.1; -; Genomic_DNA.
DR RefSeq; WP_003402198.1; NZ_WUCS01000008.1.
DR PATRIC; fig|1773.206.peg.4133; -.
DR OMA; HADADNF; -.
DR Proteomes; UP000039021; Unassembled WGS sequence.
DR Proteomes; UP000044938; Unassembled WGS sequence.
DR Proteomes; UP000045842; Unassembled WGS sequence.
DR Proteomes; UP000046674; Unassembled WGS sequence.
DR Proteomes; UP000046947; Unassembled WGS sequence.
DR Proteomes; UP000048289; Unassembled WGS sequence.
DR Proteomes; UP000048600; Unassembled WGS sequence.
DR Proteomes; UP000048948; Unassembled WGS sequence.
DR Proteomes; UP000049023; Unassembled WGS sequence.
DR Proteomes; UP000050164; Unassembled WGS sequence.
DR Proteomes; UP000182946; Unassembled WGS sequence.
DR Proteomes; UP000189452; Chromosome.
DR Proteomes; UP000388593; Chromosome.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
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; Superoxide dismutase, copper/zinc binding domain; 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:SF105; SUPEROXIDE DISMUTASE [CU-ZN]; 1.
DR PANTHER; PTHR10003; SUPEROXIDE DISMUTASE CU-ZN -RELATED; 1.
DR Pfam; PF00080; Sod_Cu; 1.
DR SUPFAM; SSF49329; Cu,Zn superoxide dismutase-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Copper {ECO:0000256|RuleBase:RU000393};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|RuleBase:RU000393};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000393,
KW ECO:0000313|EMBL:SGH34044.1}; Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|RuleBase:RU000393}.
FT SIGNAL 1..39
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 40..240
FT /note="Superoxide dismutase [Cu-Zn]"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015026371"
FT DOMAIN 86..237
FT /note="Superoxide dismutase copper/zinc binding"
FT /evidence="ECO:0000259|Pfam:PF00080"
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"
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
//
