ID B2MYX8_STRIN Unreviewed; 202 AA.
AC B2MYX8;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 58.
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:ACC77469.1};
GN ORFNames=DIY07_03475 {ECO:0000313|EMBL:RLU57806.1};
OS Streptococcus iniae (Streptococcus shiloi).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1346 {ECO:0000313|EMBL:ACC77469.1};
RN [1] {ECO:0000313|EMBL:ACC77469.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=QMA0076 {ECO:0000313|EMBL:ACC77469.1};
RA Tumbol R.A.;
RT "The leukocyte populations of barramundi and their interactions with the
RT bacterial pathogen Streptococcus iniae.";
RL Thesis (2008), The University of Queensland, St. Lucia, Brisbane,
RL Australia.
RN [2] {ECO:0000313|EMBL:RLU57806.1, ECO:0000313|Proteomes:UP000269148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QMA0445 {ECO:0000313|EMBL:RLU57806.1,
RC ECO:0000313|Proteomes:UP000269148};
RA Barnes A.C., Silayeva O.;
RT "Mutators as drivers of adaptation in pathogenic bacteria and a risk factor
RT for host jumps and vaccine escape.";
RL Submitted (JUN-2018) 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 -!- 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 -!- 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; EU661272; ACC77469.1; -; Genomic_DNA.
DR EMBL; QLQD01000034; RLU57806.1; -; Genomic_DNA.
DR RefSeq; WP_003101122.1; NZ_QLSP01000031.1.
DR GeneID; 66799658; -.
DR KEGG; sio:DW64_02990; -.
DR KEGG; siq:DQ08_03000; -.
DR KEGG; siz:SI82_03215; -.
DR PATRIC; fig|1346.30.peg.614; -.
DR OrthoDB; 9803125at2; -.
DR Proteomes; UP000269148; 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; 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:UP000269148}.
FT DOMAIN 5..89
FT /note="Manganese/iron superoxide dismutase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00081"
FT DOMAIN 96..195
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 81
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 163
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 167
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
SQ SEQUENCE 202 AA; 22597 MW; 4AD7DBC11FD37878 CRC64;
MAIILPELPY AYDALEPQFD QETMTLHHDK HHATYVANAN AALEKHPEIG ENLEELLANV
ESIPADIRQA LINNGGGHLN HALFWELLSP EKTEVTKEVA SAIDQAFGSF DAFKEQFAAA
ATGRFGSGWA WLVVTKEGSL EITSTANQDT PISEGKKPIL ALDVWEHAYY LNYRNVRPNY
INAFFEIINW NKVDELFKAA KA
//
