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Database: UniProt/SWISS-PROT
Entry: SODM1_HALSA
LinkDB: SODM1_HALSA
Original site: SODM1_HALSA 
ID   SODM1_HALSA             Reviewed;         200 AA.
AC   P09737; Q03303; Q9HQF1;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   01-OCT-2014, entry version 110.
DE   RecName: Full=Superoxide dismutase [Mn] 1;
DE            EC=1.15.1.1;
GN   Name=sod1; Synonyms=sod; OrderedLocusNames=VNG_1190G;
OS   Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS   (Halobacterium halobium).
OC   Archaea; Euryarchaeota; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=64091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2720491;
RA   May B.P., Tam P., Dennis P.P.;
RT   "The expression of the superoxide dismutase gene in Halobacterium
RT   cutirubrum and Halobacterium volcanii.";
RL   Can. J. Microbiol. 35:171-175(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2745441;
RA   May B.P., Dennis P.P.;
RT   "Evolution and regulation of the gene encoding superoxide dismutase
RT   from the archaebacterium Halobacterium cutirubrum.";
RL   J. Biol. Chem. 264:12253-12258(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=GRB;
RX   PubMed=8449865;
RA   Joshi P.B., Dennis P.P.;
RT   "Characterization of paralogous and orthologous members of the
RT   superoxide dismutase gene family from genera of the halophilic
RT   archaebacteria.";
RL   J. Bacteriol. 175:1561-1571(1993).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX   PubMed=11016950; DOI=10.1073/pnas.190337797;
RA   Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M.,
RA   Shukla H.D., Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J.,
RA   Swartzell S., Weir D., Hall J., Dahl T.A., Welti R., Goo Y.A.,
RA   Leithauser B., Keller K., Cruz R., Danson M.J., Hough D.W.,
RA   Maddocks D.G., Jablonski P.E., Krebs M.P., Angevine C.M., Dale H.,
RA   Isenbarger T.A., Peck R.F., Pohlschroder M., Spudich J.L., Jung K.-H.,
RA   Alam M., Freitas T., Hou S., Daniels C.J., Dennis P.P., Omer A.D.,
RA   Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L., DasSarma S.;
RT   "Genome sequence of Halobacterium species NRC-1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
RN   [5]
RP   PROTEIN SEQUENCE OF 2-57, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP   ENZYME REGULATION, AND SUBUNIT.
RX   PubMed=3104309;
RA   May B.P., Dennis P.P.;
RT   "Superoxide dismutase from the extremely halophilic archaebacterium
RT   Halobacterium cutirubrum.";
RL   J. Bacteriol. 169:1417-1422(1987).
RN   [6]
RP   PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, CATALYTIC ACTIVITY,
RP   COFACTOR, AND SUBUNIT.
RC   STRAIN=NRL;
RX   PubMed=3341765; DOI=10.1016/0003-9861(88)90511-5;
RA   Salin M.L., Oesterhelt D.;
RT   "Purification of a manganese-containing superoxide dismutase from
RT   Halobacterium halobium.";
RL   Arch. Biochem. Biophys. 260:806-810(1988).
CC   -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC       produced within the cells and which are toxic to biological
CC       systems. {ECO:0000269|PubMed:3104309, ECO:0000269|PubMed:3341765}.
CC   -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {ECO:0000269|PubMed:3104309, ECO:0000269|PubMed:3341765}.
CC   -!- COFACTOR: Binds 1 manganese ion per subunit.
CC       {ECO:0000269|PubMed:3104309, ECO:0000269|PubMed:3341765}.
CC   -!- ENZYME REGULATION: Inhibited by hydrogen peroxide. Is resistant to
CC       cyanide and azide inhibition. {ECO:0000269|PubMed:3104309}.
CC   -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000269|PubMed:3104309,
CC       ECO:0000269|PubMed:3341765}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
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DR   EMBL; J04956; AAA72217.1; -; Genomic_DNA.
DR   EMBL; M97484; AAA73373.1; -; Genomic_DNA.
DR   EMBL; AE004437; AAG19564.1; -; Genomic_DNA.
DR   PIR; A34319; A34319.
DR   PIR; H84274; H84274.
DR   PIR; T50043; T50043.
DR   RefSeq; NP_280084.1; NC_002607.1.
DR   RefSeq; WP_010902860.1; NC_002607.1.
DR   ProteinModelPortal; P09737; -.
DR   STRING; 64091.VNG1190G; -.
DR   PaxDb; P09737; -.
DR   PRIDE; P09737; -.
DR   EnsemblBacteria; AAG19564; AAG19564; VNG_1190G.
DR   GeneID; 1447864; -.
DR   KEGG; hal:VNG1190G; -.
DR   eggNOG; COG0605; -.
DR   KO; K04564; -.
DR   OMA; SEHSNPE; -.
DR   PhylomeDB; P09737; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
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   PANTHER; PTHR11404; PTHR11404; 1.
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   1: Evidence at protein level;
KW   Complete proteome; Direct protein sequencing; Manganese;
KW   Metal-binding; Oxidoreductase; Reference proteome.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:3104309}.
FT   CHAIN         2    200       Superoxide dismutase [Mn] 1.
FT                                /FTId=PRO_0000160114.
FT   METAL        29     29       Manganese. {ECO:0000250}.
FT   METAL        76     76       Manganese. {ECO:0000250}.
FT   METAL       158    158       Manganese. {ECO:0000250}.
FT   METAL       162    162       Manganese. {ECO:0000250}.
FT   CONFLICT      2      2       S -> T (in Ref. 5; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     52     52       E -> N (in Ref. 5; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    100    100       A -> V (in Ref. 3; AAA73373).
FT                                {ECO:0000305}.
SQ   SEQUENCE   200 AA;  22385 MW;  CA1433C6A8884819 CRC64;
     MSEYELPPLP YDYDALEPHI SEQVLTWHHD THHQGYVNGW NDAEETLAEN RETGDHASTA
     GALGDVTHNG SGHILHTLFW QSMSPAGGDE PSGALADRIA ADFGSYENWR AEFEAAASAA
     SGWALLVYDS HSNTLRNVAV DNHDEGALWG SHPILALDVW EHSYYYDYGP DRGSFVDAFF
     EVVDWDEPTE RFEQAAERFE
//
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