SODM_STAXY
ID SODM_STAXY Reviewed; 199 AA.
AC Q9K4V3; Q6PXZ5; Q6PXZ6; Q6PXZ7; Q6PXZ8; Q6PY00; Q6PY03; Q6PY06; Q6PY21;
AC Q6PY22; Q6PY24; Q6PY25; Q6PY27; Q6PY28; Q6RYX8; Q6RYX9; Q8VKW0; Q8VLZ4;
AC Q8VLZ5;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Superoxide dismutase [Mn/Fe];
DE EC=1.15.1.1 {ECO:0000305|PubMed:11526011};
GN Name=sodA; Synonyms=sod {ECO:0000303|PubMed:11526011};
OS Staphylococcus xylosus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1288;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, INDUCTION,
RP AND COFACTOR.
RC STRAIN=DSM 20267 / Isolate C2A;
RX PubMed=11526011; DOI=10.1128/aem.67.9.4096-4104.2001;
RA Barriere C., Brueckner R., Talon R.;
RT "Characterization of the single superoxide dismutase of Staphylococcus
RT xylosus.";
RL Appl. Environ. Microbiol. 67:4096-4104(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=1K07, 25K26, 41M06, 42M06, 5SI3K, 5SI4K, 5SI5K, A4065G, AS141,
RC ATCC 29971 / CIP 81.66 / DSM 20266 / JCM 2418 / LMG 20217 / NCTC 11043 /
RC CCM 2738, C4063G, C4068G, CS7, DS20, L11, S022, S087, S734, S878, S892,
RC S904, S935, Sx011, Sx1256, and Sx910;
RA Blaiotta G., Fusco V., Ercolini D., Coppola S.;
RT "Sequence polymorphism of Staphylococcus xylosus katA and sodA genes:
RT detection of some atypical Staphylococcus xylosus strains.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 9-159.
RC STRAIN=41M06, CS6, and DS20;
RA Blaiotta G., Zinno P., Gianluigi M.;
RT "Superoxide dismutase and catalase activities in coagulase-negative
RT staphylococci (CNS) isolated from fermented dry sausages.";
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 18-160.
RC STRAIN=ATCC 29971 / CIP 81.66 / DSM 20266 / JCM 2418 / LMG 20217 / NCTC
RC 11043 / CCM 2738, NEM2021, and NEM2022;
RX PubMed=11724835; DOI=10.1128/jcm.39.12.4296-4301.2001;
RA Poyart C., Quesne G., Boumaila C., Trieu-Cuot P.;
RT "Rapid and accurate species-level identification of coagulase-negative
RT staphylococci by using the sodA gene as a target.";
RL J. Clin. Microbiol. 39:4296-4301(2001).
RN [5]
RP FUNCTION.
RC STRAIN=DSM 20267 / Isolate C2A;
RX PubMed=11470359; DOI=10.1111/j.1574-6968.2001.tb10754.x;
RA Barriere C., Centeno D., Lebert A., Leroy-Setrin S., Berdague J.L.,
RA Talon R.;
RT "Roles of superoxide dismutase and catalase of Staphylococcus xylosus in
RT the inhibition of linoleic acid oxidation.";
RL FEMS Microbiol. Lett. 201:181-185(2001).
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. Also contributes to the inhibition of lipid oxidation.
CC Manganese-preferring enzyme, less active with iron than with manganese.
CC {ECO:0000269|PubMed:11470359, ECO:0000269|PubMed:11526011}.
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:0000305|PubMed:11526011};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20697;
CC Evidence={ECO:0000305|PubMed:11526011};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:11526011};
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC Evidence={ECO:0000269|PubMed:11526011};
CC Note=Binds 1 Mn(2+) or Fe(3+) ion per subunit.
CC {ECO:0000269|PubMed:11526011};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- INDUCTION: Transcription increases slightly by internally generated
CC superoxide stress. {ECO:0000269|PubMed:11526011}.
CC -!- MISCELLANEOUS: The levels of SOD activity and sodA expression were
CC growth-phase dependent, occurring most during stationary phase.
CC Expression is not affected by manganese. Is not essential for aerobic
CC growth in complex medium. {ECO:0000269|PubMed:11526011}.
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; AJ276960; CAB95744.1; -; Genomic_DNA.
DR EMBL; AY571678; AAS78509.1; -; Genomic_DNA.
DR EMBL; AY571679; AAS78510.1; -; Genomic_DNA.
DR EMBL; AY571680; AAS78511.1; -; Genomic_DNA.
DR EMBL; AY571681; AAS78512.1; -; Genomic_DNA.
DR EMBL; AY571682; AAS78513.1; -; Genomic_DNA.
DR EMBL; AY571683; AAS78514.1; -; Genomic_DNA.
DR EMBL; AY571684; AAS78515.1; -; Genomic_DNA.
DR EMBL; AY571685; AAS78516.1; -; Genomic_DNA.
DR EMBL; AY571686; AAS78517.1; -; Genomic_DNA.
DR EMBL; AY571687; AAS78518.1; -; Genomic_DNA.
DR EMBL; AY571688; AAS78520.1; -; Genomic_DNA.
DR EMBL; AY571689; AAS78522.1; -; Genomic_DNA.
DR EMBL; AY571690; AAS78524.1; -; Genomic_DNA.
DR EMBL; AY571691; AAS78526.1; -; Genomic_DNA.
DR EMBL; AY571692; AAS78527.1; -; Genomic_DNA.
DR EMBL; AY571693; AAS78529.1; -; Genomic_DNA.
DR EMBL; AY571694; AAS78531.1; -; Genomic_DNA.
DR EMBL; AY571697; AAS78534.1; -; Genomic_DNA.
DR EMBL; AY571699; AAS78536.1; -; Genomic_DNA.
DR EMBL; AY571700; AAS78537.1; -; Genomic_DNA.
DR EMBL; AY571702; AAS78539.1; -; Genomic_DNA.
DR EMBL; AY571703; AAS78540.1; -; Genomic_DNA.
DR EMBL; AY571704; AAS78541.1; -; Genomic_DNA.
DR EMBL; AY571705; AAS78542.1; -; Genomic_DNA.
DR EMBL; AY571706; AAS78543.1; -; Genomic_DNA.
DR EMBL; AY571707; AAS78544.1; -; Genomic_DNA.
DR EMBL; AY485205; AAR83767.1; -; Genomic_DNA.
DR EMBL; AY485206; AAR83768.1; -; Genomic_DNA.
DR EMBL; AY485207; AAR83769.1; -; Genomic_DNA.
DR EMBL; AJ343933; CAC86515.1; -; Genomic_DNA.
DR EMBL; AJ343959; CAC86541.1; -; Genomic_DNA.
DR EMBL; AJ343960; CAC86542.1; -; Genomic_DNA.
DR RefSeq; WP_017724588.1; NZ_VEDS01000002.1.
DR AlphaFoldDB; Q9K4V3; -.
DR SMR; Q9K4V3; -.
DR STRING; 1288.SXYLSMQ121_1239; -.
DR GeneID; 45496908; -.
DR eggNOG; COG0605; Bacteria.
DR OrthoDB; 1440645at2; -.
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; -; 1.
DR Gene3D; 3.55.40.20; -; 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 Pfam; PF02777; Sod_Fe_C; 1.
DR Pfam; PF00081; Sod_Fe_N; 1.
DR PIRSF; PIRSF000349; SODismutase; 1.
DR PRINTS; PR01703; MNSODISMTASE.
DR SUPFAM; SSF46609; SSF46609; 1.
DR SUPFAM; SSF54719; SSF54719; 1.
DR PROSITE; PS00088; SOD_MN; 1.
PE 1: Evidence at protein level;
KW Iron; Manganese; Metal-binding; Oxidoreductase; Stress response.
FT CHAIN 1..199
FT /note="Superoxide dismutase [Mn/Fe]"
FT /id="PRO_0000226590"
FT BINDING 27
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000250|UniProtKB:P80293"
FT BINDING 27
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P80293"
FT BINDING 81
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000250|UniProtKB:P80293"
FT BINDING 81
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P80293"
FT BINDING 161
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000250|UniProtKB:P80293"
FT BINDING 161
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P80293"
FT BINDING 165
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000250|UniProtKB:P80293"
FT BINDING 165
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P80293"
FT VARIANT 11..12
FT /note="GF -> AY (in strain: CS6)"
FT VARIANT 12
FT /note="F -> C (in strain: 5SI5K)"
FT VARIANT 23
FT /note="T -> P (in strain: NEM2021)"
FT VARIANT 25
FT /note="E -> V (in strain: 5SI5K)"
FT VARIANT 43
FT /note="V -> I (in strain: S087)"
FT VARIANT 61
FT /note="D -> G (in strain: S087)"
FT VARIANT 96
FT /note="G -> D (in strain: NEM2021)"
FT VARIANT 105
FT /note="Q -> H (in strain: NEM2022)"
FT VARIANT 111
FT /note="A -> T (in strain: 1K07)"
FT VARIANT 147
FT /note="D -> V (in strain: A4065G)"
FT VARIANT 150..151
FT /note="IT -> MN (in strain: A4065G)"
FT VARIANT 150
FT /note="I -> M (in strain: C4068G)"
FT VARIANT 181
FT /note="A -> S (in strain: 42M06)"
FT VARIANT 189
FT /note="E -> G (in strain: 41M06)"
FT CONFLICT 10
FT /note="Y -> F (in Ref. 2; AAS78509)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 199 AA; 22535 MW; A44EBE636368A2A2 CRC64;
MAFELPNLPY GFDALEPHID QQTMEIHHGK HHNTYVTKLN AAVEGTDLES KSIEEIVANL
DSVPENIQTA VRNNGGGHLN HSLFWELLTP NSEEKGTVVD KIKEQWGSLD AFKEEFADKA
AARFGSGWAW LVVNNGNLEI VTTPNQDNPI TEGKTPILGL DVWEHAYYLK YQNKRPDYIS
AFWNVVNWEK VDELYNAAK
