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Database: UniProt
Entry: D5RL70_9PROT
LinkDB: D5RL70_9PROT
Original site: D5RL70_9PROT 
ID   D5RL70_9PROT            Unreviewed;       247 AA.
AC   D5RL70;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   28-MAR-2018, entry version 29.
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:EFH11947.1};
GN   ORFNames=HMPREF0731_1831 {ECO:0000313|EMBL:EFH11947.1};
OS   Roseomonas cervicalis ATCC 49957.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Roseomonas.
OX   NCBI_TaxID=525371 {ECO:0000313|EMBL:EFH11947.1, ECO:0000313|Proteomes:UP000005324};
RN   [1] {ECO:0000313|EMBL:EFH11947.1, ECO:0000313|Proteomes:UP000005324}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49957 {ECO:0000313|EMBL:EFH11947.1,
RC   ECO:0000313|Proteomes:UP000005324};
RA   Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C.,
RA   Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L.,
RA   Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y.,
RA   Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L.,
RA   Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F.,
RA   Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M.,
RA   Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S.,
RA   Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J.,
RA   Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J.,
RA   Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D.,
RA   Worley K., Gibbs R.;
RL   Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
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   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EFH11947.1}.
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DR   EMBL; ADVL01000299; EFH11947.1; -; Genomic_DNA.
DR   RefSeq; WP_007006000.1; NZ_GG770871.1.
DR   EnsemblBacteria; EFH11947; EFH11947; HMPREF0731_1831.
DR   OrthoDB; POG091H03Q7; -.
DR   Proteomes; UP000005324; Unassembled WGS sequence.
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   InterPro; IPR006311; TAT_signal.
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.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000005324};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:EFH11947.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005324};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     20       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        21    247       Superoxide dismutase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5003075561.
FT   DOMAIN       42    128       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      135    236       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        66     66       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       121    121       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       203    203       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       207    207       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   247 AA;  26659 MW;  03D466CC1CAF7A09 CRC64;
     MTTPLIARRG ALFAAGSLLA AGLLPGRVFA QAAAPAQPSG PFTLPALPYA ANALEPHIDA
     ATMELHHGRH HAAYVNNLNA ALRDHGQLAS LKLEELLAKL GEAPEAVRTT LRNNGGGHAN
     HSMFWQIMGG RGGNPSGELA EAINRDLGGM EKFRTDFNGA GARVFGSGWV FVTVDREGKL
     ALNSRPNQDT PLMDGQRVLM GNDVWEHAYY LKYNNRRPEY LAAWWNVLDW AKIGERYAAA
     KAGTLGV
//
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