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Database: UniProt
Entry: A0A1H8B2U3_9RHOB
LinkDB: A0A1H8B2U3_9RHOB
Original site: A0A1H8B2U3_9RHOB 
ID   A0A1H8B2U3_9RHOB        Unreviewed;       228 AA.
AC   A0A1H8B2U3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   05-DEC-2018, entry version 5.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=SAMN04488003_104137 {ECO:0000313|EMBL:SEM77056.1};
OS   Loktanella fryxellensis.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Loktanella.
OX   NCBI_TaxID=245187 {ECO:0000313|EMBL:SEM77056.1, ECO:0000313|Proteomes:UP000199585};
RN   [1] {ECO:0000313|EMBL:SEM77056.1, ECO:0000313|Proteomes:UP000199585}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16213 {ECO:0000313|EMBL:SEM77056.1,
RC   ECO:0000313|Proteomes:UP000199585};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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:
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; FOCI01000004; SEM77056.1; -; Genomic_DNA.
DR   Proteomes; UP000199585; 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   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:UP000199585};
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:UP000199585};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     19       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        20    228       Superoxide dismutase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5011639985.
FT   DOMAIN       24    108       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      118    221       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        49     49       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       100    100       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       188    188       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       192    192       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   228 AA;  24922 MW;  DD7FB60DBFE42519 CRC64;
     MKHFLSVVAL SATPFAAVAQ TDGTFTLTDL PYATDALAPV ILQETMELHH GKHHQSYVDN
     LNAAITAGDA PADLTLQELV AAAGTYPDAV RNNAGGHWNH DFFWNTMAPA DATGEMSDAL
     SEAITGVFGS QEEFETAFQE AGAARFGSGW VWLIVDDQDQ LQITTTPNQD NPLMDVADVQ
     GTPLLGNDVW EHAYYLSYNN RRADYLGEWW GVVDWPEVSD RYDAALAD
//
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