GenomeNet

Database: UniProt
Entry: F8DDU6_HALXS
LinkDB: F8DDU6_HALXS
Original site: F8DDU6_HALXS 
ID   F8DDU6_HALXS            Unreviewed;       200 AA.
AC   F8DDU6;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   16-JAN-2019, entry version 37.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {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;
OC   Natrialbales; 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.,
RA   Klenk H.P., Kyrpides N., Ivanova N.;
RT   "Complete genome sequence of Halopiger xanaduensis type strain (SH-
RT   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
CC       family. {ECO:0000256|RuleBase:RU000414}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP002840; AEH39200.1; -; Genomic_DNA.
DR   RefSeq; WP_013875928.1; NC_015658.1.
DR   EnsemblBacteria; AEH39200; AEH39200; Halxa_0611.
DR   GeneID; 10795468; -.
DR   KEGG; hxa:Halxa_0611; -.
DR   KO; K04564; -.
DR   OMA; YLHSIFW; -.
DR   OrthoDB; 74803at2157; -.
DR   BioCyc; HXAN797210:GIXL-3938-MONOMER; -.
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; -; 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:UP000006794};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414};
KW   Plasmid {ECO:0000313|EMBL:AEH39200.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006794}.
FT   DOMAIN        3     84       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       91    189       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        28     28       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        76     76       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       158    158       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       162    162       Divalent metal cation.
FT                                {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
//
DBGET integrated database retrieval system