ID Q494B0_BLOPB Unreviewed; 205 AA.
AC Q494B0;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 101.
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:AAZ40671.1};
GN OrderedLocusNames=BPEN_021 {ECO:0000313|EMBL:AAZ40671.1};
OS Blochmannia pennsylvanicus (strain BPEN).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; ant endosymbionts; Blochmannia.
OX NCBI_TaxID=291272 {ECO:0000313|EMBL:AAZ40671.1, ECO:0000313|Proteomes:UP000007794};
RN [1] {ECO:0000313|EMBL:AAZ40671.1, ECO:0000313|Proteomes:UP000007794}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BPEN {ECO:0000313|EMBL:AAZ40671.1,
RC ECO:0000313|Proteomes:UP000007794};
RX PubMed=16077009; DOI=10.1101/gr.3771305;
RA Degnan P.H., Lazarus A.B., Wernegreen J.J.;
RT "Genome sequence of Blochmannia pennsylvanicus indicates parallel
RT evolutionary trends among bacterial mutualists of insects.";
RL Genome Res. 15:1023-1033(2005).
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}.
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DR EMBL; CP000016; AAZ40671.1; -; Genomic_DNA.
DR RefSeq; WP_011282577.1; NC_007292.1.
DR AlphaFoldDB; Q494B0; -.
DR STRING; 291272.BPEN_021; -.
DR KEGG; bpn:BPEN_021; -.
DR eggNOG; COG0605; Bacteria.
DR HOGENOM; CLU_031625_0_1_6; -.
DR OrthoDB; 9803125at2; -.
DR Proteomes; UP000007794; 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; 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.
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:UP000007794}.
FT DOMAIN 3..89
FT /note="Manganese/iron superoxide dismutase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00081"
FT DOMAIN 96..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 82
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 168
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 172
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
SQ SEQUENCE 205 AA; 23867 MW; 3698686426B7E153 CRC64;
MSFILPSLTY SYDALEPFLD EKTMKIHHTK HHQAYIDNAN AALIDLPEFS NLPVIELIKK
LNHLPNHKKT ILRNNAGGHI NHSLFWKYLK KNTILQGSLK DAIEYNFSSI SSFKEHFEKT
AISRFGSGWV WLIKHNNILS IVSTANQDNP LMGIDISGTN GYPILGLDVW EHAYYLKYQN
RRLDYIRSFW NVVNWDEVYA QFNQV
//