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Database: UniProt
Entry: W1NBM2_9GAMM
LinkDB: W1NBM2_9GAMM
Original site: W1NBM2_9GAMM 
ID   W1NBM2_9GAMM            Unreviewed;       192 AA.
AC   W1NBM2;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   16-JAN-2019, entry version 26.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=BJB45_16445 {ECO:0000313|EMBL:ERL52868.1};
OS   Halomonas huangheensis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=1178482 {ECO:0000313|EMBL:ERL52868.1, ECO:0000313|Proteomes:UP000019113};
RN   [1] {ECO:0000313|EMBL:ERL52868.1, ECO:0000313|Proteomes:UP000019113}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BJGMM-B45 {ECO:0000313|EMBL:ERL52868.1,
RC   ECO:0000313|Proteomes:UP000019113};
RA   Miao C., Wan Y., Jin W.;
RT   "draft genome of Halomonas huanghegensis, strain BJGMM-B45T.";
RL   Submitted (AUG-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}.
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:ERL52868.1}.
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DR   EMBL; AVBC01000014; ERL52868.1; -; Genomic_DNA.
DR   RefSeq; WP_021817495.1; NZ_CP013106.1.
DR   EnsemblBacteria; ERL52868; ERL52868; BJB45_16445.
DR   KEGG; hhu:AR456_10255; -.
DR   PATRIC; fig|1178482.3.peg.545; -.
DR   KO; K04564; -.
DR   OrthoDB; 1440645at2; -.
DR   Proteomes; UP000019113; 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; 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.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000019113};
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:UP000019113}.
FT   COILED       50     70       {ECO:0000256|SAM:Coils}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        74     74       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       157    157       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       161    161       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   192 AA;  21548 MW;  810BB02C355DBFF7 CRC64;
     MRFELPALPY DRHSLEPHLS AAMVDAHYSG YHLACIQRLN TRLECLNPTA DSLEELLDST
     DDEIAYLAAE VWNHAFYWHC LTPWGNTTPA AELKADIDGA FGSLAGFHQA FKTSALAHIG
     SGWIWLIRNH DGQLTIITTN DGQAPLAQGI KPLIGIDLWE HAWYLDFQNN RDAYLDAIST
     LINWDFVTLN NG
//
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