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-MAY-2013, entry version 104.
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.
CC -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC -!- COFACTOR: Binds 1 manganese ion per subunit.
CC -!- ENZYME REGULATION: Inhibited by hydrogen peroxide. Is resistant to
CC cyanide and azide inhibition.
CC -!- SUBUNIT: Homodimer or homotetramer.
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC family.
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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 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; MAPPGKG; -.
DR ProtClustDB; CLSK511336; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004784; F:superoxide dismutase activity; IEA:EC.
DR GO; GO:0006801; P:superoxide metabolic process; IEA:InterPro.
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; SODismutase; 1.
DR SUPFAM; SSF54719; SODismutase; 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.
FT CHAIN 2 200 Superoxide dismutase [Mn] 1.
FT /FTId=PRO_0000160114.
FT METAL 29 29 Manganese (By similarity).
FT METAL 76 76 Manganese (By similarity).
FT METAL 158 158 Manganese (By similarity).
FT METAL 162 162 Manganese (By similarity).
FT CONFLICT 2 2 S -> T (in Ref. 5; AA sequence).
FT CONFLICT 52 52 E -> N (in Ref. 5; AA sequence).
FT CONFLICT 100 100 A -> V (in Ref. 3; AAA73373).
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
//
