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Database: UniProt
Entry: Q9PC60_XYLFA
LinkDB: Q9PC60_XYLFA
Original site: Q9PC60_XYLFA 
ID   Q9PC60_XYLFA            Unreviewed;       242 AA.
AC   Q9PC60;
DT   01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2000, sequence version 1.
DT   16-JAN-2019, entry version 107.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   OrderedLocusNames=XF_1921 {ECO:0000313|EMBL:AAF84727.1};
OS   Xylella fastidiosa (strain 9a5c).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xylella.
OX   NCBI_TaxID=160492 {ECO:0000313|EMBL:AAF84727.1, ECO:0000313|Proteomes:UP000000812};
RN   [1] {ECO:0000313|EMBL:AAF84727.1, ECO:0000313|Proteomes:UP000000812}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9a5c {ECO:0000313|EMBL:AAF84727.1,
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.,
RA   Goldman G.H., Goldman M.H., Gomes S.L., Gruber A., Ho P.L.,
RA   Hoheisel J.D., Junqueira M.L., Kemper E.L., Kitajima J.P.,
RA   Krieger J.E., Kuramae E.E., Laigret F., Lambais M.R., Leite L.C.,
RA   Lemos E.G., Lemos M.V., Lopes S.A., Lopes C.R., Machado J.A.,
RA   Machado M.A., Madeira A.M., Madeira H.M., Marino C.L., Marques M.V.,
RA   Martins E.A., Martins E.M., Matsukuma A.Y., Menck C.F., Miracca E.C.,
RA   Miyaki C.Y., Monteriro-Vitorello C.B., Moon D.H., Nagai M.A.,
RA   Nascimento A.L., Netto L.E., Nhani A.Jr., Nobrega F.G., Nunes L.R.,
RA   Oliveira M.A., de Oliveira M.C., de Oliveira R.C., Palmieri D.A.,
RA   Paris A., Peixoto B.R., Pereira G.A., Pereira H.A.Jr., Pesquero J.B.,
RA   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.,
RA   da Silva A.C., da Silva A.M., da Silva F.R., da Silva W.A.Jr.,
RA   da Silveira J.F., Silvestri M.L., Siqueira W.J., de Souza A.A.,
RA   de Souza A.P., Terenzi M.F., Truffi D., Tsai S.M., Tsuhako M.H.,
RA   Vallada H., Van Sluys M.A., Verjovski-Almeida S., Vettore A.L.,
RA   Zago M.A., Zatz M., Meidanis J., 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
CC       family. {ECO:0000256|RuleBase:RU000414}.
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DR   EMBL; AE003849; AAF84727.1; -; Genomic_DNA.
DR   PIR; F82620; F82620.
DR   RefSeq; WP_010894387.1; NC_002488.3.
DR   ProteinModelPortal; Q9PC60; -.
DR   STRING; 160492.XF1921; -.
DR   EnsemblBacteria; AAF84727; AAF84727; XF_1921.
DR   GeneID; 1127472; -.
DR   KEGG; xfa:XF_1921; -.
DR   PATRIC; fig|160492.11.peg.2043; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   KO; K04564; -.
DR   OMA; HNQFWEM; -.
DR   BioCyc; XFAS160492:XF_RS08325-MONOMER; -.
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; -; 1.
DR   Gene3D; 2.40.500.20; -; 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   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000000812};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000812};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     25       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        26    242       Superoxide dismutase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5004335800.
FT   DOMAIN       34    117       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      125    228       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        58     58       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       109    109       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       196    196       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       200    200       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   242 AA;  27070 MW;  DDB1789591CE2809 CRC64;
     MFLLRQGHLT LCLIAALLAS FLSFASTQPQ IAPFTLPPLP YAVSALEPAI DTQTMTLHHD
     FHHKAYVDNL NAAIKDIPTL SGKTLEQLLA IASTLPPAVR NNAGGDWNHS EFWKMMAPVG
     KGGKPSAALE TQIKKDFGSL DAFKERFNKA ATGRFGSGWA WMILTSSGLQ ITSTPNQDNP
     LMDVAEVRGQ PLLALDVWEH AYYLKYKYKR ADYLNAWWTV VNWNEVNHLF EVAKKEQHNL
     NH
//
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