ID   Q87A43_XYLFT            Unreviewed;       203 AA.
AC   Q87A43;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 112.
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=sodM {ECO:0000313|EMBL:AAO29817.1};
GN   OrderedLocusNames=PD_1988 {ECO:0000313|EMBL:AAO29817.1};
OS   Xylella fastidiosa (strain Temecula1 / ATCC 700964).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xylella.
OX   NCBI_TaxID=183190 {ECO:0000313|EMBL:AAO29817.1, ECO:0000313|Proteomes:UP000002516};
RN   [1] {ECO:0000313|EMBL:AAO29817.1, ECO:0000313|Proteomes:UP000002516}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Temecula1 / ATCC 700964 {ECO:0000313|Proteomes:UP000002516};
RX   PubMed=12533478; DOI=10.1128/JB.185.3.1018-1026.2003;
RA   Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B., Miyaki C.Y.,
RA   Furlan L.R., Camargo L.E., da Silva A.C., Moon D.H., Takita M.A.,
RA   Lemos E.G., Machado M.A., Ferro M.I., da Silva F.R., Goldman M.H.,
RA   Goldman G.H., Lemos M.V., El-Dorry H., Tsai S.M., Carrer H., Carraro D.M.,
RA   de Oliveira R.C., Nunes L.R., Siqueira W.J., Coutinho L.L., Kimura E.T.,
RA   Ferro E.S., Harakava R., Kuramae E.E., Marino C.L., Giglioti E.,
RA   Abreu I.L., Alves L.M., do Amaral A.M., Baia G.S., Blanco S.R., Brito M.S.,
RA   Cannavan F.S., Celestino A.V., da Cunha A.F., Fenille R.C., Ferro J.A.,
RA   Formighieri E.F., Kishi L.T., Leoni S.G., Oliveira A.R., Rosa V.E.Jr.,
RA   Sassaki F.T., Sena J.A., de Souza A.A., Truffi D., Tsukumo F., Yanai G.M.,
RA   Zaros L.G., Civerolo E.L., Simpson A.J., Almeida N.F.Jr., Setubal J.C.,
RA   Kitajima J.P.;
RT   "Comparative analyses of the complete genome sequences of Pierce's disease
RT   and citrus variegated chlorosis strains of Xylella fastidiosa.";
RL   J. Bacteriol. 185:1018-1026(2003).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE009442; AAO29817.1; -; Genomic_DNA.
DR   RefSeq; WP_004087549.1; NC_004556.1.
DR   AlphaFoldDB; Q87A43; -.
DR   GeneID; 58017506; -.
DR   KEGG; xft:PD_1988; -.
DR   HOGENOM; CLU_031625_0_1_6; -.
DR   Proteomes; UP000002516; 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:UP000002516}.
FT   DOMAIN          3..89
FT                   /note="Manganese/iron superoxide dismutase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00081"
FT   DOMAIN          96..197
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         164
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"
SQ   SEQUENCE   203 AA;  22769 MW;  8EA59DCBDB913903 CRC64;
     MAYTLPILPY AYDALEPHID AQTMEIHYTK HHATYINNLN AALEGTEYAD LPIEELLRNL
     KSLPESLQVP VRNNGGGHAN HSLFWTVMAQ DGGGKPKGEV AKAIDQQLGG FETFKDAFTK
     AALSRFGSGW SLLNVTPSKT LVVESSANQD SPLCDGKTSI LCLDVWEHAY YLHYQNRRAD
     YVNAFYNVIN WDEVERRYVV AMS
//