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 03-AUG-2022, entry version 141.
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; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=64091;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2720491; DOI=10.1139/m89-026;
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; DOI=10.1016/s0021-9258(18)63850-5;
RA May B.P., Dennis P.P.;
RT "Evolution and regulation of the gene encoding superoxide dismutase from
RT 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; 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 [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., 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).
RN [5]
RP PROTEIN SEQUENCE OF 2-57, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY
RP REGULATION, AND SUBUNIT.
RX PubMed=3104309; DOI=10.1128/jb.169.4.1417-1422.1987;
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, COFACTOR, AND
RP 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 systems.
CC {ECO:0000269|PubMed:3104309, ECO:0000269|PubMed:3341765}.
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; Evidence={ECO:0000269|PubMed:3104309,
CC ECO:0000269|PubMed:3341765};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:3104309, ECO:0000269|PubMed:3341765};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000269|PubMed:3104309,
CC ECO:0000269|PubMed:3341765};
CC -!- ACTIVITY 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 family.
CC {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; WP_010902860.1; NC_002607.1.
DR AlphaFoldDB; P09737; -.
DR SMR; P09737; -.
DR STRING; 64091.VNG_1190G; -.
DR PaxDb; P09737; -.
DR PRIDE; P09737; -.
DR EnsemblBacteria; AAG19564; AAG19564; VNG_1190G.
DR GeneID; 5952858; -.
DR GeneID; 62886701; -.
DR KEGG; hal:VNG_1190G; -.
DR PATRIC; fig|64091.14.peg.912; -.
DR HOGENOM; CLU_031625_2_1_2; -.
DR InParanoid; P09737; -.
DR OMA; YLHSIFW; -.
DR OrthoDB; 74803at2157; -.
DR PhylomeDB; P09737; -.
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 1: Evidence at protein level;
KW Direct protein sequencing; Manganese; Metal-binding; Oxidoreductase;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3104309"
FT CHAIN 2..200
FT /note="Superoxide dismutase [Mn] 1"
FT /id="PRO_0000160114"
FT BINDING 29
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 2
FT /note="S -> T (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="E -> N (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="A -> V (in Ref. 3; AAA73373)"
FT /evidence="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
