ID   D3SY04_NATMM            Unreviewed;       200 AA.
AC   D3SY04;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|ARBA:ARBA00012682, ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|ARBA:ARBA00012682, ECO:0000256|RuleBase:RU000414};
GN   Name=sod {ECO:0000313|EMBL:ADD04044.1};
GN   OrderedLocusNames=Nmag_0456 {ECO:0000313|EMBL:ADD04044.1};
GN   ORFNames=C500_02699 {ECO:0000313|EMBL:ELY33202.1};
OS   Natrialba magadii (strain ATCC 43099 / DSM 3394 / CCM 3739 / CIP 104546 /
OS   IAM 13178 / JCM 8861 / NBRC 102185 / NCIMB 2190 / MS3) (Natronobacterium
OS   magadii).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natrialba.
OX   NCBI_TaxID=547559 {ECO:0000313|EMBL:ADD04044.1, ECO:0000313|Proteomes:UP000001879};
RN   [1] {ECO:0000313|Proteomes:UP000001879}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43099 / DSM 3394 / CCM 3739 / CIP 104546 / IAM 13178 / JCM
RC   8861 / NBRC 102185 / NCIMB 2190 / MS3
RC   {ECO:0000313|Proteomes:UP000001879};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Davenport K., Saunders E., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Mikhailova N., De Castro R.E.,
RA   Maupin-Furlow J.A., Woyke T.;
RT   "Complete sequence of chromosome of Natrialba magadii ATCC 43099.";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADD04044.1, ECO:0000313|Proteomes:UP000001879}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43099 {ECO:0000313|EMBL:ADD04044.1}, and ATCC 43099 / DSM
RC   3394 / CCM 3739 / CIP 104546 / IAM 13178 / JCM 8861 / NBRC 102185 /
RC   NCIMB 2190 / MS3 {ECO:0000313|Proteomes:UP000001879};
RX   PubMed=22559199; DOI=10.1186/1471-2164-13-165;
RA   Siddaramappa S., Challacombe J.F., Decastro R.E., Pfeiffer F., Sastre D.E.,
RA   Gimenez M.I., Paggi R.A., Detter J.C., Davenport K.W., Goodwin L.A.,
RA   Kyrpides N., Tapia R., Pitluck S., Lucas S., Woyke T., Maupin-Furlow J.A.;
RT   "A comparative genomics perspective on the genetic content of the
RT   alkaliphilic haloarchaeon Natrialba magadii ATCC 43099T.";
RL   BMC Genomics 13:165-165(2012).
RN   [3] {ECO:0000313|EMBL:ELY33202.1, ECO:0000313|Proteomes:UP000011543}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43099 / DSM 3394 / CCM 3739 / CIP 104546 / IAM 13178 / JCM
RC   8861 / NBRC 102185 / NCIMB 2190 / MS3
RC   {ECO:0000313|Proteomes:UP000011543}, and MS-3
RC   {ECO:0000313|EMBL:ELY33202.1};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
RN   [4] {ECO:0000313|EMBL:ADD04044.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 43099 {ECO:0000313|EMBL:ADD04044.1};
RA   Pfeiffer F.;
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000256|RuleBase:RU000414}.
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         Evidence={ECO:0000256|RuleBase:RU000414};
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC       {ECO:0000256|ARBA:ARBA00008714, ECO:0000256|RuleBase:RU000414}.
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DR   EMBL; CP001932; ADD04044.1; -; Genomic_DNA.
DR   EMBL; AOHS01000010; ELY33202.1; -; Genomic_DNA.
DR   RefSeq; WP_004214016.1; NZ_AOHS01000010.1.
DR   AlphaFoldDB; D3SY04; -.
DR   SMR; D3SY04; -.
DR   STRING; 547559.Nmag_0456; -.
DR   PaxDb; 547559-Nmag_0456; -.
DR   GeneID; 8823280; -.
DR   KEGG; nmg:Nmag_0456; -.
DR   PATRIC; fig|547559.17.peg.511; -.
DR   eggNOG; arCOG04147; Archaea.
DR   HOGENOM; CLU_031625_2_1_2; -.
DR   OrthoDB; 32917at2157; -.
DR   Proteomes; UP000001879; Chromosome.
DR   Proteomes; UP000011543; Unassembled WGS sequence.
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; Fe,Mn superoxide dismutase (SOD) domain; 1.
DR   Gene3D; 3.55.40.20; Iron/manganese superoxide dismutase, C-terminal domain; 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   NCBIfam; NF041312; Superox_dis_Halo; 1.
DR   PANTHER; PTHR11404; SUPEROXIDE DISMUTASE 2; 1.
DR   PANTHER; PTHR11404:SF6; SUPEROXIDE DISMUTASE [MN], MITOCHONDRIAL; 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; SSF54719; Fe,Mn superoxide dismutase (SOD), C-terminal domain; 1.
DR   SUPFAM; SSF46609; Fe,Mn superoxide dismutase (SOD), N-terminal domain; 1.
DR   PROSITE; PS00088; SOD_MN; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000349-1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000414};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001879}.
FT   DOMAIN          4..84
FT                   /note="Manganese/iron superoxide dismutase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00081"
FT   DOMAIN          91..190
FT                   /note="Manganese/iron superoxide dismutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02777"
FT   BINDING         28
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         76
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         158
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         162
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
SQ   SEQUENCE   200 AA;  22380 MW;  F79CC69075A0DBF5 CRC64;
     MTDHELPPLP YDYDALEPSI SEQVVTWHHD THHQGYVNGL NSAEETLAEN RESGDFDSTP
     GALSNVTHNG CGHYLHTLFW ENMSPDGGGE PAGDIADRIE EDFGSYEGWK GEFEAAAGAA
     GGWALLVYDP VAKQLRNVAV DKHDQGALWG SHPILALDVW EHSYYYDYGP DRGSFIEGFF
     DVINWDSVED EYQKCLDHFE
//