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Database: UniProt
Entry: V9VPI4_9RHOB
LinkDB: V9VPI4_9RHOB
Original site: V9VPI4_9RHOB 
ID   V9VPI4_9RHOB            Unreviewed;       199 AA.
AC   V9VPI4;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   16-JAN-2019, entry version 25.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=METH_07875 {ECO:0000313|EMBL:AHD00621.1};
OS   Leisingera methylohalidivorans DSM 14336.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Leisingera.
OX   NCBI_TaxID=999552 {ECO:0000313|EMBL:AHD00621.1, ECO:0000313|Proteomes:UP000018780};
RN   [1] {ECO:0000313|EMBL:AHD00621.1, ECO:0000313|Proteomes:UP000018780}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14336 {ECO:0000313|EMBL:AHD00621.1,
RC   ECO:0000313|Proteomes:UP000018780};
RG   DOE Joint Genome Institute;
RA   Klenk H.-P., Huntemann M., Han J., Chen A., Kyrpides N.,
RA   Mavromatis K., Markowitz V., Palaniappan K., Ivanova N.,
RA   Schaumberg A., Pati A., Liolios K., Nordberg H.P., Cantor M.N.,
RA   Hua S.X., Woyke T.;
RL   Submitted (SEP-2013) 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; CP006773; AHD00621.1; -; Genomic_DNA.
DR   RefSeq; WP_024089845.1; NC_023135.1.
DR   EnsemblBacteria; AHD00621; AHD00621; METH_07875.
DR   KEGG; lmd:METH_07875; -.
DR   PATRIC; fig|999552.6.peg.1583; -.
DR   KO; K04564; -.
DR   OrthoDB; 1440645at2; -.
DR   BioCyc; LMET999552:G1HML-1512-MONOMER; -.
DR   Proteomes; UP000018780; 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:UP000018780};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN        3     89       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       98    198       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        28     28       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        82     82       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       164    164       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       168    168       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   199 AA;  22058 MW;  BF2616A8E25253DB CRC64;
     MAFELPDLPY AHDALAAKGM SAETLEYHHD LHHKAYVDNG NKLIAGTEWD GKSLEEIIKG
     TYDAGSVAQN GIFNNISQLW NHNQFWEMMG PGDSAMPGEL EKALVESFGS VDDFKSQFSA
     AGAGQFGSGW AWLVKNADGS LAVTKTENGV NPLCFNQTAL LGCDVWEHSY YIDFRNKRPA
     YLTNFLDNLV NWENVASRM
//
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