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Database: UniProt
Entry: B9LPE7_HALLT
LinkDB: B9LPE7_HALLT
Original site: B9LPE7_HALLT 
ID   B9LPE7_HALLT            Unreviewed;       199 AA.
AC   B9LPE7;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   16-JAN-2019, entry version 60.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   OrderedLocusNames=Hlac_1650 {ECO:0000313|EMBL:ACM57235.1};
OS   Halorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 /
OS   ACAM 34).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria;
OC   Haloferacales; Halorubraceae; Halorubrum.
OX   NCBI_TaxID=416348 {ECO:0000313|EMBL:ACM57235.1, ECO:0000313|Proteomes:UP000000740};
RN   [1] {ECO:0000313|EMBL:ACM57235.1, ECO:0000313|Proteomes:UP000000740}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34
RC   {ECO:0000313|Proteomes:UP000000740};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Anderson I., DasSarma S., Cavicchioli R., Richardson P.;
RT   "Complete sequence of chromosome1 of Halorubrum lacusprofundi ATCC
RT   49239.";
RL   Submitted (JAN-2009) 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
CC       family. {ECO:0000256|RuleBase:RU000414}.
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DR   EMBL; CP001365; ACM57235.1; -; Genomic_DNA.
DR   RefSeq; WP_015910373.1; NC_012029.1.
DR   ProteinModelPortal; B9LPE7; -.
DR   STRING; 416348.Hlac_1650; -.
DR   EnsemblBacteria; ACM57235; ACM57235; Hlac_1650.
DR   GeneID; 7399600; -.
DR   KEGG; hla:Hlac_1650; -.
DR   eggNOG; arCOG04147; Archaea.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013583; -.
DR   KO; K04564; -.
DR   OMA; YEGWKGE; -.
DR   OrthoDB; 74803at2157; -.
DR   BioCyc; HLAC416348:GIWW-1687-MONOMER; -.
DR   Proteomes; UP000000740; Chromosome 1.
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; 2.40.500.20; -; 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   Complete proteome {ECO:0000313|Proteomes:UP000000740};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:ACM57235.1}.
FT   DOMAIN        2     83       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       90    187       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        75     75       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       157    157       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       161    161       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   199 AA;  22613 MW;  CAE023F1B1E745F9 CRC64;
     MSYELDPLPY DYDALEPHLS EQVLEWHHDT HHQGYVNGWN SAEETLEANR EEHDFSSSGG
     AIRNVTHNSS GHILHDLFWQ NMSPEGGDEP DGALADRIAE DFGSYDAWKG EFEAAASAAS
     GWALLVYDTF SNQLRNVVVD KHDQGAIWGG HPILALDVWE HSYYHDYGPA RGEFVDNFFE
     VVDWNEPATR YEQAVELFE
//
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