ID A0A0E3NRG6_9EURY Unreviewed; 203 AA.
AC A0A0E3NRG6;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 16-JAN-2019, entry version 21.
DE RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN ORFNames=MSWH1_2108 {ECO:0000313|EMBL:AKB22379.1};
OS Methanosarcina sp. WH1.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=1434102 {ECO:0000313|EMBL:AKB22379.1, ECO:0000313|Proteomes:UP000033112};
RN [1] {ECO:0000313|EMBL:AKB22379.1, ECO:0000313|Proteomes:UP000033112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH1 {ECO:0000313|EMBL:AKB22379.1,
RC ECO:0000313|Proteomes:UP000033112};
RA Henriksen J.R., Luke J., Reinhart S., Benedict M.N., Youngblut N.D.,
RA Metcalf M.E., Whitaker R.J., Metcalf W.W.;
RT "Methanogenic archaea and the global carbon cycle.";
RL Submitted (JUL-2014) 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; CP009504; AKB22379.1; -; Genomic_DNA.
DR RefSeq; WP_048128602.1; NZ_CP009504.1.
DR EnsemblBacteria; AKB22379; AKB22379; MSWH1_2108.
DR GeneID; 24836911; -.
DR KEGG; mef:MSWH1_2108; -.
DR PATRIC; fig|1434102.4.peg.2759; -.
DR KO; K04564; -.
DR OrthoDB; 74803at2157; -.
DR Proteomes; UP000033112; 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:UP000033112};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW ECO:0000256|RuleBase:RU000414};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW ECO:0000313|EMBL:AKB22379.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033112}.
FT DOMAIN 6 85 Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT DOMAIN 95 196 Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT METAL 30 30 Divalent metal cation.
FT {ECO:0000256|PIRSR:PIRSR000349-1}.
FT METAL 78 78 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 203 AA; 23748 MW; 201A466DB2E2D270 CRC64;
MAKELYKLPP LKYGYADLAP YISEEQLRIH HDKHHQGYVN NTNALLEMMD KARKEGTDFD
YKTTAKALSF NLGGHVLHDY FWWEMTPASN ASKEPVGELA DVIKDDFGSF ERFKKEFSQV
ASSVEGSGWA ALTFCNDTKR LGIMQIEKHN VNLVPDFPIL MDLDVWEHAY YIDYKNDRSK
FIEGFWNIVD WEEIDKYFKK TQK
//
