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Database: UniProt
Entry: A0A2A7MR55_MYCAG
LinkDB: A0A2A7MR55_MYCAG
Original site: A0A2A7MR55_MYCAG 
ID   A0A2A7MR55_MYCAG        Unreviewed;       206 AA.
AC   A0A2A7MR55;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|ARBA:ARBA00012682, ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|ARBA:ARBA00012682, ECO:0000256|RuleBase:RU000414};
GN   Name=sodA {ECO:0000313|EMBL:GFG50291.1};
GN   ORFNames=CQY20_26905 {ECO:0000313|EMBL:PEG34186.1}, MAGR_17320
GN   {ECO:0000313|EMBL:GFG50291.1};
OS   Mycolicibacterium agri (Mycobacterium agri).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=36811 {ECO:0000313|EMBL:PEG34186.1, ECO:0000313|Proteomes:UP000220914};
RN   [1] {ECO:0000313|EMBL:PEG34186.1, ECO:0000313|Proteomes:UP000220914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG37673 {ECO:0000313|EMBL:PEG34186.1,
RC   ECO:0000313|Proteomes:UP000220914};
RA   Tortoli E., Trovato A., Cirillo D.M.;
RT   "The new phylogeny of genus Mycobacterium.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:GFG50291.1, ECO:0000313|Proteomes:UP000465302}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 6377 {ECO:0000313|EMBL:GFG50291.1,
RC   ECO:0000313|Proteomes:UP000465302};
RX   PubMed=31287781;
RA   Matsumoto Y., Kinjo T., Motooka D., Nabeya D., Jung N., Uechi K., Horii T.,
RA   Iida T., Fujita J., Nakamura S.;
RT   "Comprehensive subspecies identification of 175 nontuberculous mycobacteria
RT   species based on 7547 genomic profiles.";
RL   Emerg. Microbes Infect. 8:1043-1053(2019).
RN   [3] {ECO:0000313|EMBL:GFG50291.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JCM 6377 {ECO:0000313|EMBL:GFG50291.1};
RA   Matsumoto Y., Motooka D., Nakamura S.;
RL   Submitted (FEB-2020) 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   -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC       produced within the cells and which are toxic to biological systems.
CC       {ECO:0000256|ARBA:ARBA00002170}.
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|ARBA:ARBA00001605,
CC         ECO:0000256|RuleBase:RU000414};
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC       {ECO:0000256|ARBA:ARBA00008714, ECO:0000256|RuleBase:RU000414}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PEG34186.1}.
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DR   EMBL; BLKS01000001; GFG50291.1; -; Genomic_DNA.
DR   EMBL; PDCP01000074; PEG34186.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A7MR55; -.
DR   OrthoDB; 9803125at2; -.
DR   Proteomes; UP000220914; Unassembled WGS sequence.
DR   Proteomes; UP000465302; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   Gene3D; 1.10.287.990; Fe,Mn superoxide dismutase (SOD) domain; 1.
DR   Gene3D; 3.55.40.20; Iron/manganese superoxide dismutase, C-terminal domain; 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   PANTHER; PTHR11404; SUPEROXIDE DISMUTASE 2; 1.
DR   PANTHER; PTHR11404:SF6; SUPEROXIDE DISMUTASE [MN], MITOCHONDRIAL; 1.
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; SSF54719; Fe,Mn superoxide dismutase (SOD), C-terminal domain; 1.
DR   SUPFAM; SSF46609; Fe,Mn superoxide dismutase (SOD), N-terminal domain; 1.
DR   PROSITE; PS00088; SOD_MN; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000349-1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000414};
KW   Reference proteome {ECO:0000313|Proteomes:UP000220914}.
FT   DOMAIN          3..84
FT                   /note="Manganese/iron superoxide dismutase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00081"
FT   DOMAIN          91..193
FT                   /note="Manganese/iron superoxide dismutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02777"
FT   BINDING         28
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         76
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         160
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         164
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
SQ   SEQUENCE   206 AA;  22931 MW;  27D4CDBC6BAE8D43 CRC64;
     MAEYTLPDLD YDYGALEPHI SGQINEIHHG KHHATYVKGA NDALAKLEEA RATGDHSAIL
     LNEKNLAFHL GGHVNHSIWW KNLSPNGGDK PTGELAAAVD EHFGAFDRFQ GQFAAAANGL
     QGSGWAVLGW DTLGQRLLTF QLYDQQANVP LGIIPLLQVD MWEHAYYLQY KNVKADYVKA
     FWNVVNWQDV QNRFTAATSK AQGLIF
//
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