SODM2_HALSA
ID SODM2_HALSA Reviewed; 200 AA.
AC P09224; Q03299; Q9HQ47;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 3.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Superoxide dismutase [Mn] 2;
DE EC=1.15.1.1;
GN Name=sod2; Synonyms=slg, sod1; OrderedLocusNames=VNG_1332G;
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=64091;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3240866; DOI=10.1016/0378-1119(88)90113-8;
RA Salin M.L., Duke M.V., Oesterhelt D., Ma D.-P.;
RT "Cloning and determination of the nucleotide sequence of the Mn-containing
RT superoxide dismutase gene from Halobacterium halobium.";
RL Gene 70:153-159(1988).
RN [2]
RP ERRATUM OF PUBMED:3240866.
RA Salin M.L., Duke M.V., Oesterhelt D., Ma D.-P.;
RL Gene 87:153-153(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2681164; DOI=10.1128/jb.171.11.6323-6329.1989;
RA Takao M., Kobayashi T., Oikawa A., Yasui A.;
RT "Tandem arrangement of photolyase and superoxide dismutase genes in
RT Halobacterium halobium.";
RL J. Bacteriol. 171:6323-6329(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1694523; DOI=10.1128/jb.172.7.3725-3729.1990;
RA May B.P., Dennis P.P.;
RT "Unusual evolution of a superoxide dismutase-like gene from the extremely
RT halophilic archaebacterium Halobacterium cutirubrum.";
RL J. Bacteriol. 172:3725-3729(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=GRB;
RX PubMed=8449865; DOI=10.1128/jb.175.6.1561-1571.1993;
RA Joshi P.B., Dennis P.P.;
RT "Characterization of paralogous and orthologous members of the superoxide
RT dismutase gene family from genera of the halophilic archaebacteria.";
RL J. Bacteriol. 175:1561-1571(1993).
RN [6]
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., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
CC -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC produced within the cells and which are toxic to biological systems.
CC {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; M22408; AAA72704.1; -; Genomic_DNA.
DR EMBL; M24544; AAA72750.1; -; Genomic_DNA.
DR EMBL; M26502; AAA72770.1; -; Genomic_DNA.
DR EMBL; M97483; AAA73372.1; -; Genomic_DNA.
DR EMBL; AE004437; AAG19670.1; -; Genomic_DNA.
DR PIR; B84288; B84288.
DR PIR; C32580; DSHSNH.
DR PIR; T50047; T50047.
DR RefSeq; WP_010902966.1; NC_002607.1.
DR AlphaFoldDB; P09224; -.
DR SMR; P09224; -.
DR STRING; 64091.VNG_1332G; -.
DR PaxDb; P09224; -.
DR EnsemblBacteria; AAG19670; AAG19670; VNG_1332G.
DR GeneID; 5952922; -.
DR GeneID; 62886811; -.
DR KEGG; hal:VNG_1332G; -.
DR PATRIC; fig|64091.14.peg.1018; -.
DR HOGENOM; CLU_031625_2_1_2; -.
DR InParanoid; P09224; -.
DR OMA; YEGWKGE; -.
DR OrthoDB; 74803at2157; -.
DR PhylomeDB; P09224; -.
DR Proteomes; UP000000554; 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; 3.55.40.20; -; 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 Manganese; Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..200
FT /note="Superoxide dismutase [Mn] 2"
FT /id="PRO_0000160115"
FT BINDING 28
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 76
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT CONFLICT 24
FT /note="V -> A (in Ref. 5; AAA73372)"
FT /evidence="ECO:0000305"
FT CONFLICT 46
FT /note="T -> N (in Ref. 5; AAA73372)"
FT /evidence="ECO:0000305"
FT CONFLICT 49
FT /note="E -> G (in Ref. 5; AAA73372)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="S -> T (in Ref. 1; AAA72704)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 200 AA; 22208 MW; 736E7B223BDAE260 CRC64;
MSQHELPSLP YDYDALEPHI SEQVVTWHHD THHQSYVDGL NSAEETLAEN RETGDHASTA
GALGDVTHNG CGHYLHTMFW EHMSPDGGGE PSGALADRIA ADFGSYENWR AEFEVAAGAA
SGWALLVYDP VAKQLRNVAV DNHDEGALWG SHPILALDVW EHSYYYDYGP DRGSFVDAFF
EVIDWDPIAA NYDDVVSLFE