ID A0A1D9GHS8_9ALTE Unreviewed; 192 AA.
AC A0A1D9GHS8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 28-MAR-2018, entry version 8.
DE RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN ORFNames=BKP64_02650 {ECO:0000313|EMBL:AOY87169.1};
OS Marinobacter salinus.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Marinobacter.
OX NCBI_TaxID=1874317 {ECO:0000313|EMBL:AOY87169.1, ECO:0000313|Proteomes:UP000177445};
RN [1] {ECO:0000313|EMBL:AOY87169.1, ECO:0000313|Proteomes:UP000177445}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hb8 {ECO:0000313|EMBL:AOY87169.1,
RC ECO:0000313|Proteomes:UP000177445};
RA Park S.-J.;
RT "Marinobacter salinus sp. nov., a moderately halophilic bacterium
RT isolated from a tidal flat environment.";
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: 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}.
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DR EMBL; CP017715; AOY87169.1; -; Genomic_DNA.
DR RefSeq; WP_070965663.1; NZ_CP017715.1.
DR KEGG; msq:BKP64_02650; -.
DR KO; K04564; -.
DR Proteomes; UP000177445; 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:UP000177445};
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:UP000177445}.
FT DOMAIN 3 82 Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT DOMAIN 89 189 Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
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; 21493 MW; F98B807919D55546 CRC64;
MAFELPALPY EKNALEPHIS QETLEYHYGK HHNTYVTKLN GLVEGTDNAS KSLEDIIKSA
SGPLFNNAAQ VWNHTFYWHC LSPNGGGEPT GAAKDAIEKA FGSFEDFKKE FNDKAANNFG
SGWTWLVKKA DGSVAIANTS NAETPLTGAD KPVLTVDVWE HAYYIDYRNS RPNYLEAFWN
LVNWDFVNEN LA
//
