ID   F8DDU6_HALXS            Unreviewed;       200 AA.
AC   F8DDU6;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 52.
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   OrderedLocusNames=Halxa_0611 {ECO:0000313|EMBL:AEH39200.1};
OS   Halopiger xanaduensis (strain DSM 18323 / JCM 14033 / SH-6).
OG   Plasmid pHALXA01 {ECO:0000313|EMBL:AEH39200.1,
OG   ECO:0000313|Proteomes:UP000006794}.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Halopiger.
OX   NCBI_TaxID=797210 {ECO:0000313|EMBL:AEH39200.1, ECO:0000313|Proteomes:UP000006794};
RN   [1] {ECO:0000313|Proteomes:UP000006794}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18323 / JCM 14033 / SH-6
RC   {ECO:0000313|Proteomes:UP000006794};
RC   PLASMID=Plasmid pHALXA01 {ECO:0000313|Proteomes:UP000006794};
RX   PubMed=22675596; DOI=10.4056/sigs.2505605;
RA   Anderson I., Tindall B.J., Rohde M., Lucas S., Han J., Lapidus A.,
RA   Cheng J.F., Goodwin L., Pitluck S., Peters L., Pati A., Mikhailova N.,
RA   Pagani I., Teshima H., Han C., Tapia R., Land M., Woyke T., Klenk H.P.,
RA   Kyrpides N., Ivanova N.;
RT   "Complete genome sequence of Halopiger xanaduensis type strain (SH-6(T)).";
RL   Stand. Genomic Sci. 6:31-42(2012).
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; CP002840; AEH39200.1; -; Genomic_DNA.
DR   RefSeq; WP_013875928.1; NC_015658.1.
DR   AlphaFoldDB; F8DDU6; -.
DR   GeneID; 10795468; -.
DR   KEGG; hxa:Halxa_0611; -.
DR   HOGENOM; CLU_031625_2_0_2; -.
DR   OrthoDB; 32917at2157; -.
DR   Proteomes; UP000006794; Plasmid pHALXA01.
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}; Plasmid {ECO:0000313|EMBL:AEH39200.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006794}.
FT   DOMAIN          3..84
FT                   /note="Manganese/iron superoxide dismutase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00081"
FT   DOMAIN          91..188
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;  22616 MW;  F4ACFD6E58336341 CRC64;
     MSDYELPPLP YDYDALEPHI SEQVLTWHHD THHQGYVNGW NSAEETLAEN REEGDFAGSA
     GAIRNVTHNG SGHILHDLFW QSMSPEGGDE PEGDLADRIE EDFGSYEAWK GEFEAAASNA
     GGWALLVYDS FSNQLRNVVV DKHDQGALWG SHPILALDVW EHSYYHDYGP ARGDFVDAFF
     EVVDWEEPSA RYEQAVELFE
//