ID Q9PAA4_XYLFA Unreviewed; 203 AA.
AC Q9PAA4;
DT 01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 126.
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=XF_2614 {ECO:0000313|EMBL:AAF85411.1};
OS Xylella fastidiosa (strain 9a5c).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xylella.
OX NCBI_TaxID=160492 {ECO:0000313|EMBL:AAF85411.1, ECO:0000313|Proteomes:UP000000812};
RN [1] {ECO:0000313|EMBL:AAF85411.1, ECO:0000313|Proteomes:UP000000812}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9a5c {ECO:0000313|EMBL:AAF85411.1,
RC ECO:0000313|Proteomes:UP000000812};
RX PubMed=10910347; DOI=10.1038/35018003;
RA Simpson A.J., Reinach F.C., Arruda P., Abreu F.A., Acencio M.,
RA Alvarenga R., Alves L.M., Araya J.E., Baia G.S., Baptista C.S.,
RA Barros M.H., Bonaccorsi E.D., Bordin S., Bove J.M., Briones M.R.,
RA Bueno M.R., Camargo A.A., Camargo L.E., Carraro D.M., Carrer H.,
RA Colauto N.B., Colombo C., Costa F.F., Costa M.C., Costa-Neto C.M.,
RA Coutinho L.L., Cristofani M., Dias-Neto E., Docena C., El-Dorry H.,
RA Facincani A.P., Ferreira A.J., Ferreira V.C., Ferro J.A., Fraga J.S.,
RA Franca S.C., Franco M.C., Frohme M., Furlan L.R., Garnier M., Goldman G.H.,
RA Goldman M.H., Gomes S.L., Gruber A., Ho P.L., Hoheisel J.D.,
RA Junqueira M.L., Kemper E.L., Kitajima J.P., Krieger J.E., Kuramae E.E.,
RA Laigret F., Lambais M.R., Leite L.C., Lemos E.G., Lemos M.V., Lopes S.A.,
RA Lopes C.R., Machado J.A., Machado M.A., Madeira A.M., Madeira H.M.,
RA Marino C.L., Marques M.V., Martins E.A., Martins E.M., Matsukuma A.Y.,
RA Menck C.F., Miracca E.C., Miyaki C.Y., Monteriro-Vitorello C.B., Moon D.H.,
RA Nagai M.A., Nascimento A.L., Netto L.E., Nhani A.Jr., Nobrega F.G.,
RA Nunes L.R., Oliveira M.A., de Oliveira M.C., de Oliveira R.C.,
RA Palmieri D.A., Paris A., Peixoto B.R., Pereira G.A., Pereira H.A.Jr.,
RA Pesquero J.B., Quaggio R.B., Roberto P.G., Rodrigues V., de M Rosa A.J.,
RA de Rosa V.E.Jr., de Sa R.G., Santelli R.V., Sawasaki H.E., da Silva A.C.,
RA da Silva A.M., da Silva F.R., da Silva W.A.Jr., da Silveira J.F.,
RA Silvestri M.L., Siqueira W.J., de Souza A.A., de Souza A.P., Terenzi M.F.,
RA Truffi D., Tsai S.M., Tsuhako M.H., Vallada H., Van Sluys M.A.,
RA Verjovski-Almeida S., Vettore A.L., Zago M.A., Zatz M., Meidanis J.,
RA Setubal J.C.;
RT "The genome sequence of the plant pathogen Xylella fastidiosa.";
RL Nature 406:151-159(2000).
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; AE003849; AAF85411.1; -; Genomic_DNA.
DR PIR; G82535; G82535.
DR RefSeq; WP_010895031.1; NC_002488.3.
DR AlphaFoldDB; Q9PAA4; -.
DR STRING; 160492.XF_2614; -.
DR KEGG; xfa:XF_2614; -.
DR eggNOG; COG0605; Bacteria.
DR HOGENOM; CLU_031625_0_1_6; -.
DR Proteomes; UP000000812; 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}.
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; 22644 MW; F339B9D93CDCBA7F CRC64;
MAYTLPILPY AYDALQPHID AQTMEIHYTK HHATYINNLN AALEGTEYAD LPIEELLRNL
KSLPESLQGP VRNNGGGCVN HSLFWTVMAQ GGGGKPKGEV AKAIDQQLGG FETFKDAFTK
AALSRFGSGW SLLNVTPSKT LVVESSANQD SPLCDGKTPI LCLDVWEHAY YLHYQNRRAD
YVNAFYNVIN WDEVERRYVA AMS
//
