GenomeNet

Database: UniProt/TrEMBL
Entry: A0A068T6Y7_RHIGA
LinkDB: A0A068T6Y7_RHIGA
Original site: A0A068T6Y7_RHIGA 
ID   A0A068T6Y7_RHIGA        Unreviewed;       200 AA.
AC   A0A068T6Y7;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   25-OCT-2017, entry version 15.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=RG1141_CH07500 {ECO:0000313|EMBL:CDN53110.1};
OS   Neorhizobium galegae bv. officinalis bv. officinalis str. HAMBI 1141.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Neorhizobium.
OX   NCBI_TaxID=1028801 {ECO:0000313|EMBL:CDN53110.1, ECO:0000313|Proteomes:UP000028186};
RN   [1] {ECO:0000313|Proteomes:UP000028186}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAMBI 1141 {ECO:0000313|Proteomes:UP000028186};
RA   Oesterman J., Marsh J., Laine P.K., Alatalo E., Sullivan J.,
RA   Young J.P.W., Thomas-Oates J., Paulin L., Lindstroem K.;
RT   "Genome sequencing of two Neorhizobium galegae strains reveals a noeT
RT   gene responsible for the unusual acetylation of the nodulation
RT   factors.";
RL   BMC Genomics 15:500-500(2014).
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: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {ECO:0000256|RuleBase:RU000414}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000256|RuleBase:RU000414}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; HG938355; CDN53110.1; -; Genomic_DNA.
DR   RefSeq; WP_038540989.1; NZ_HG938355.1.
DR   EnsemblBacteria; CDN53110; CDN53110; RG1141_CH07500.
DR   KEGG; ngl:RG1141_CH07500; -.
DR   PATRIC; fig|1028801.3.peg.763; -.
DR   KO; K04564; -.
DR   Proteomes; UP000028186; Chromosome I.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
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:UP000028186};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN        3     85       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       95    194       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        77     77       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       160    160       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       164    164       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   200 AA;  22413 MW;  96FB0DC8C4C124FD CRC64;
     MAFELPELPY DYEALSPFMS KETLEFHHDK HHKAYVDNGN KLAAEAGMAD LSLEEVVKKS
     FGTNQGLFNN AAQHYNHVHF WKWMKKGGGG TKLPGKLEAA VASDLGGYDK FKADLIAAGT
     TQFGSGWAWL SVKDGKLVIS KTPNGENPLV HGAEPILGVD VWEHSYYIDY RNARPKYLEA
     FVDSLINWDY VLERYEAATK
//
DBGET integrated database retrieval system