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Database: UniProt
Entry: D2UAU5_XANAP
LinkDB: D2UAU5_XANAP
Original site: D2UAU5_XANAP 
ID   D2UAU5_XANAP            Unreviewed;       235 AA.
AC   D2UAU5;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   16-JAN-2019, entry version 51.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   Name=sodA {ECO:0000313|EMBL:CBA16149.1};
GN   OrderedLocusNames=XALc_1651 {ECO:0000313|EMBL:CBA16149.1};
OS   Xanthomonas albilineans (strain GPE PC73 / CFBP 7063).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=380358 {ECO:0000313|EMBL:CBA16149.1, ECO:0000313|Proteomes:UP000001890};
RN   [1] {ECO:0000313|EMBL:CBA16149.1, ECO:0000313|Proteomes:UP000001890}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GPE PC73 / CFBP 7063 {ECO:0000313|Proteomes:UP000001890};
RX   PubMed=20017926; DOI=10.1186/1471-2164-10-616;
RA   Pieretti I., Royer M., Barbe V., Carrere S., Koebnik R.,
RA   Cociancich S., Couloux A., Darrasse A., Gouzy J., Jacques M.A.,
RA   Lauber E., Manceau C., Mangenot S., Poussier S., Segurens B.,
RA   Szurek B., Verdier V., Arlat M., Rott P.;
RT   "The complete genome sequence of Xanthomonas albilineans provides new
RT   insights into the reductive genome evolution of the xylem-limited
RT   Xanthomonadaceae.";
RL   BMC Genomics 10:616-616(2009).
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; FP565176; CBA16149.1; -; Genomic_DNA.
DR   RefSeq; WP_012916150.1; NC_013722.1.
DR   ProteinModelPortal; D2UAU5; -.
DR   EnsemblBacteria; CBA16149; CBA16149; XALC_1651.
DR   KEGG; xal:XALC_1651; -.
DR   PATRIC; fig|29447.3.peg.1612; -.
DR   HOGENOM; HOG000013584; -.
DR   KO; K04564; -.
DR   OMA; HNQFWEM; -.
DR   OrthoDB; 1440645at2; -.
DR   BioCyc; XALB380358:VB87_RS08575-MONOMER; -.
DR   Proteomes; UP000001890; 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:UP000001890};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:CBA16149.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001890};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     23       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        24    235       Superoxide dismutase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5003037006.
FT   DOMAIN       31    114       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      122    227       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        55     55       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       106    106       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       194    194       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       198    198       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   235 AA;  26005 MW;  C99629471A7FB610 CRC64;
     MKRFTLKTLC VTALLATANL ASAADTDKAP FSLPPLPYAN AALEPAIDAR TMEIHHDRHH
     KAYVDNLNEK VKDYPDLATT SLEDIQAHIS RYDTAVRNNA GGDYNHGLFW TVMAPVGKGG
     SPSPKLKAKL VQTFGSEAAF QAKFTEAAKK VFGSGWVWLI LKADGSLAIT TTANQDNPLM
     DVVAERGTPL LALDVWEHAY YLKYQNKRAD YISSWWSVVN WNQVNARFDK AVGKH
//
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