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Database: UniProt/TrEMBL
Entry: A0A1D7TH19_9PROT
LinkDB: A0A1D7TH19_9PROT
Original site: A0A1D7TH19_9PROT 
ID   A0A1D7TH19_9PROT        Unreviewed;       198 AA.
AC   A0A1D7TH19;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   28-MAR-2018, entry version 8.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=SHALO_0522 {ECO:0000313|EMBL:AOO64312.1};
OS   Sulfurospirillum halorespirans DSM 13726.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Sulfurospirillum.
OX   NCBI_TaxID=1193502 {ECO:0000313|EMBL:AOO64312.1, ECO:0000313|Proteomes:UP000094609};
RN   [1] {ECO:0000313|Proteomes:UP000094609}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13726 / PCE-M2 {ECO:0000313|Proteomes:UP000094609};
RA   Goris T., Zimmermann J., Schenz B., Lemos M., Hackermueller J.,
RA   Diekert G.;
RT   "Complete genome sequence of the organohalide-respiring
RT   Epsilonproteobacterium Sulfurospirillum halorespirans.";
RL   Submitted (AUG-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: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {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; CP017111; AOO64312.1; -; Genomic_DNA.
DR   RefSeq; WP_069477254.1; NZ_CP017111.1.
DR   EnsemblBacteria; AOO64312; AOO64312; SHALO_0522.
DR   KEGG; shal:SHALO_0522; -.
DR   PATRIC; fig|1193502.14.peg.532; -.
DR   KO; K04564; -.
DR   Proteomes; UP000094609; 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; -; 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:UP000094609};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:AOO64312.1}.
FT   DOMAIN        4     87       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       94    194       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        79     79       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       161    161       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       165    165       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   198 AA;  21838 MW;  754DD35BB132D2F2 CRC64;
     MAITLPALPY EANALEPHIS ANTLGFHHGK HHQTYVTNLN NLIQGTELAE ESLEKIILAV
     ANKPEKVGIF NNAAQVWNHT FYWNCMKKGG GGAPSGAIAT KITEDFGSFE AFVEAFKSAG
     LTQFGSGWAW LVLEGGKLKI TKTANADTPL AHDQKAILTV DVWEHAYYLD YQNKRADYLD
     VFLKSLVNWD FANANLKA
//
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