ID   B3ER22_AMOA5            Unreviewed;       205 AA.
AC   B3ER22;
DT   22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2008, sequence version 1.
DT   27-MAR-2024, entry version 78.
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   OrderedLocusNames=Aasi_0230 {ECO:0000313|EMBL:ACE05674.1};
OS   Amoebophilus asiaticus (strain 5a2).
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Amoebophilaceae;
OC   Candidatus Amoebophilus.
OX   NCBI_TaxID=452471 {ECO:0000313|EMBL:ACE05674.1, ECO:0000313|Proteomes:UP000001227};
RN   [1] {ECO:0000313|EMBL:ACE05674.1, ECO:0000313|Proteomes:UP000001227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5a2 {ECO:0000313|EMBL:ACE05674.1,
RC   ECO:0000313|Proteomes:UP000001227};
RX   PubMed=20023027; DOI=10.1128/JB.01379-09;
RA   Schmitz-Esser S., Tischler P., Arnold R., Montanaro J., Wagner M.,
RA   Rattei T., Horn M.;
RT   "The genome of the amoeba symbiont 'Candidatus Amoebophilus asiaticus'
RT   reveals common mechanisms for host cell interaction among amoeba-associated
RT   bacteria.";
RL   J. Bacteriol. 192:1045-1057(2010).
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   -!- 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:RU000414};
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; CP001102; ACE05674.1; -; Genomic_DNA.
DR   RefSeq; WP_012472432.1; NC_010830.1.
DR   AlphaFoldDB; B3ER22; -.
DR   STRING; 452471.Aasi_0230; -.
DR   KEGG; aas:Aasi_0230; -.
DR   eggNOG; COG0605; Bacteria.
DR   HOGENOM; CLU_031625_0_1_10; -.
DR   OrthoDB; 9803125at2; -.
DR   Proteomes; UP000001227; 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; 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; PTHR43595; 37S RIBOSOMAL PROTEIN S26, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43595:SF2; 37S RIBOSOMAL PROTEIN S26, 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.
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:UP000001227}.
FT   DOMAIN          3..84
FT                   /note="Manganese/iron superoxide dismutase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00081"
FT   DOMAIN          92..199
FT                   /note="Manganese/iron superoxide dismutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02777"
FT   BINDING         27
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         77
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         166
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         170
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
SQ   SEQUENCE   205 AA;  23181 MW;  7A2B76B6403BC0BA CRC64;
     MAFELPTLPY APEALEPHID ATTMQLHHAK HHQAYLDKFN KAIEGTDLAA RSIEDILKNV
     SNYSVVVRNN GGGYYNHNLF WPMLTPNGGG EPTGAIVDAI NQKFQGFAQF KEAFAQAALE
     QFGSGWAWLC KDITGELFIC STANQDNPIM DIVEEGSRGI PVLGLDVWEH GYYLKYQNRR
     AEYIDAFWNI VNWEEVNKRF QAPMP
//