ID F7XVQ6_MIDMI Unreviewed; 207 AA.
AC F7XVQ6;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN Name=sodA {ECO:0000313|EMBL:AEI88755.1};
GN OrderedLocusNames=midi_00448 {ECO:0000313|EMBL:AEI88755.1};
OS Midichloria mitochondrii (strain IricVA).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Candidatus Midichloriaceae; Midichloria.
OX NCBI_TaxID=696127 {ECO:0000313|EMBL:AEI88755.1, ECO:0000313|Proteomes:UP000006639};
RN [1] {ECO:0000313|EMBL:AEI88755.1, ECO:0000313|Proteomes:UP000006639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IricVA {ECO:0000313|EMBL:AEI88755.1,
RC ECO:0000313|Proteomes:UP000006639};
RX PubMed=21690562; DOI=10.1093/molbev/msr159;
RA Sassera D., Lo N., Epis S., D'Auria G., Montagna M., Comandatore F.,
RA Horner D., Pereto J., Luciano A.M., Franciosi F., Ferri E., Crotti E.,
RA Bazzocchi C., Daffonchio D., Sacchi L., Moya A., Latorre A., Bandi C.;
RT "Phylogenomic evidence for the presence of a flagellum and cbb3 oxidase in
RT the free-living mitochondrial ancestor.";
RL Mol. Biol. Evol. 28:3285-3296(2011).
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 Catalyzes the dismutation of superoxide anion radicals into O2 and H2O2
CC by successive reduction and oxidation of the transition metal ion at
CC the active site. {ECO:0000256|ARBA:ARBA00024318}.
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:ARBA00024290};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20697;
CC Evidence={ECO:0000256|ARBA:ARBA00024290};
CC -!- COFACTOR:
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC Evidence={ECO:0000256|ARBA:ARBA00001965};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000256|ARBA:ARBA00008714, ECO:0000256|RuleBase:RU000414}.
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DR EMBL; CP002130; AEI88755.1; -; Genomic_DNA.
DR RefSeq; WP_013950967.1; NC_015722.1.
DR AlphaFoldDB; F7XVQ6; -.
DR STRING; 696127.midi_00448; -.
DR KEGG; mmn:midi_00448; -.
DR HOGENOM; CLU_031625_0_0_5; -.
DR OrthoDB; 9803125at2; -.
DR Proteomes; UP000006639; Chromosome.
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; PTHR42769; SUPEROXIDE DISMUTASE; 1.
DR PANTHER; PTHR42769:SF3; SUPEROXIDE DISMUTASE [FE] 2, CHLOROPLASTIC; 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:UP000006639}.
FT DOMAIN 9..92
FT /note="Manganese/iron superoxide dismutase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00081"
FT DOMAIN 100..202
FT /note="Manganese/iron superoxide dismutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02777"
FT BINDING 33
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 85
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 169
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 173
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
SQ SEQUENCE 207 AA; 24254 MW; D83F13BDBF6066DC CRC64;
MNKEEKYPFK LSDLPYAKNA LEPTISANTL SFHHEKHHQT YVTNLNNLIK DRHFSSLSLE
EIIKETANEI AEIAIFNNAA QVWNHTFYWH CMRQGGGGAP TGNLLRQIER DFDNYDNFRA
EFSRAALSRF GSGWAWLIWD KDQRRLLVTK TGNADLPMVH GQVALLTIDV WEHAYYLDYQ
NRRVDYITAF LDHLVNWQFA EEIFARC
//
