SODM1_HALVD
ID SODM1_HALVD Reviewed; 200 AA.
AC Q03300; D4GRE0;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Superoxide dismutase [Mn] 1;
DE EC=1.15.1.1;
GN Name=sod1; OrderedLocusNames=HVO_A0475;
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OG Plasmid pHV4.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
CC -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC produced within the cells and which are toxic to biological systems.
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; M97486; AAA73375.1; -; Genomic_DNA.
DR EMBL; CP001955; ADE01978.1; -; Genomic_DNA.
DR PIR; T50045; T50045.
DR RefSeq; WP_013035130.1; NC_013966.1.
DR AlphaFoldDB; Q03300; -.
DR SMR; Q03300; -.
DR STRING; 309800.C498_00220; -.
DR EnsemblBacteria; ADE01978; ADE01978; HVO_A0475.
DR GeneID; 8923864; -.
DR KEGG; hvo:HVO_A0475; -.
DR eggNOG; arCOG04147; Archaea.
DR HOGENOM; CLU_031625_2_0_2; -.
DR OMA; YLHSIFW; -.
DR Proteomes; UP000008243; Plasmid pHV4.
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; Plasmid; Reference proteome.
FT CHAIN 1..200
FT /note="Superoxide dismutase [Mn] 1"
FT /id="PRO_0000160116"
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 43..44
FT /note="AE -> DD (in Ref. 1; AAA73375)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="L -> V (in Ref. 1; AAA73375)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="A -> L (in Ref. 1; AAA73375)"
FT /evidence="ECO:0000305"
FT CONFLICT 121
FT /note="G -> A (in Ref. 1; AAA73375)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 200 AA; 22412 MW; 689652AC88E45203 CRC64;
MSDYELDPLP YEYDALEPHI SEQVLTWHHD THHQGYVNGW NAAEETLAEN REAGEFGSSA
GALRNVTHNG SGHILHDLFW QNMSPEGGDE PEGALAERIA EDFGSYEAWK GEFEAAAGAA
GGWALLVYDS FSNQLRNVVV DKHDQGALWG SHPILALDVW EHSYYHDYGP ARGDFVSAFF
EVVDWDEPAA RYEQAVELFE