ID   I0JKZ4_HALH3            Unreviewed;       280 AA.
AC   I0JKZ4;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   RecName: Full=superoxide dismutase {ECO:0000256|ARBA:ARBA00012682};
DE            EC=1.15.1.1 {ECO:0000256|ARBA:ARBA00012682};
GN   Name=sodF {ECO:0000313|EMBL:CCG44814.1};
GN   OrderedLocusNames=HBHAL_2471 {ECO:0000313|EMBL:CCG44814.1};
OS   Halobacillus halophilus (strain ATCC 35676 / DSM 2266 / JCM 20832 /
OS   KCTC 3685 / LMG 17431 / NBRC 102448 / NCIMB 2269) (Sporosarcina halophila).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX   NCBI_TaxID=866895 {ECO:0000313|EMBL:CCG44814.1, ECO:0000313|Proteomes:UP000007397};
RN   [1] {ECO:0000313|EMBL:CCG44814.1, ECO:0000313|Proteomes:UP000007397}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35676 / DSM 2266 / JCM 20832 / KCTC 3685 / LMG 17431 /
RC   NBRC 102448 / NCIMB 2269 {ECO:0000313|Proteomes:UP000007397};
RX   PubMed=22583374; DOI=10.1111/j.1462-2920.2012.02770.x;
RA   Saum S.H., Pfeiffer F., Palm P., Rampp M., Schuster S.C., Muller V.,
RA   Oesterhelt D.;
RT   "Chloride and organic osmolytes: a hybrid strategy to cope with elevated
RT   salinities by the moderately halophilic, chloride-dependent bacterium
RT   Halobacillus halophilus.";
RL   Environ. Microbiol. 15:1619-1633(2013).
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC       {ECO:0000256|ARBA:ARBA00008714}.
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DR   EMBL; HE717023; CCG44814.1; -; Genomic_DNA.
DR   AlphaFoldDB; I0JKZ4; -.
DR   STRING; 866895.HBHAL_2471; -.
DR   KEGG; hhd:HBHAL_2471; -.
DR   PATRIC; fig|866895.3.peg.1481; -.
DR   eggNOG; COG0605; Bacteria.
DR   HOGENOM; CLU_031625_1_0_9; -.
DR   Proteomes; UP000007397; 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; 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   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   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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:CCG44814.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007397}.
FT   DOMAIN          90..170
FT                   /note="Manganese/iron superoxide dismutase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00081"
FT   DOMAIN          179..262
FT                   /note="Manganese/iron superoxide dismutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02777"
SQ   SEQUENCE   280 AA;  32228 MW;  8A5F4193ECF9D785 CRC64;
     MNDQALIKYL REMDTWANHI AKADASRKIY EDPSFQEEIN ELLSNIKEWN RDASSFNLDN
     AHELNELAEK IQKRLGSHER QGNAVPIGGH QLPPLPYGYA ALEPYIDRRM MQLHHDKHHK
     SYVDGLNKAE IEMQKARKNN NYDLIKHWER EAAFNGAGHY LHTIFWEIMS PEGGGKAGGD
     LLKEIESSFG SFQKFKEHFS AAAKKVEGSG WTILVWAPRS HRLEILQAEK HQNLSQWDVI
     PLLPLDVWEH AYYLQYENDR GEIRGQLVER SELGGCSGSL
//