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Database: UniProt
Entry: K7S3H8_9HELI
LinkDB: K7S3H8_9HELI
Original site: K7S3H8_9HELI 
ID   K7S3H8_9HELI            Unreviewed;       226 AA.
AC   K7S3H8;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   16-JAN-2019, entry version 28.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=B649_04345 {ECO:0000313|EMBL:AFV97183.1};
OS   Candidatus Sulfuricurvum sp. RIFRC-1.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Sulfuricurvum.
OX   NCBI_TaxID=1249480 {ECO:0000313|EMBL:AFV97183.1, ECO:0000313|Proteomes:UP000000224};
RN   [1] {ECO:0000313|EMBL:AFV97183.1, ECO:0000313|Proteomes:UP000000224}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIFRC-1 {ECO:0000313|EMBL:AFV97183.1};
RA   Bartels D., Handley K., O'Loughlin E.J., Glass E.M., Paczian T.,
RA   Brulc J., Desai N., Domanus M., D'Souza M., Gilbert J.A., Long P.E.,
RA   Skinner K., Wilkening J., Williams K., Antonopoulos D., Kemner K.M.,
RA   Meyer F.;
RL   Submitted (SEP-2012) 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; CP003920; AFV97183.1; -; Genomic_DNA.
DR   ProteinModelPortal; K7S3H8; -.
DR   KEGG; sulr:B649_04345; -.
DR   PATRIC; fig|1249480.3.peg.879; -.
DR   KO; K04564; -.
DR   BioCyc; USUL1249480:G13GT-889-MONOMER; -.
DR   Proteomes; UP000000224; 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:UP000000224};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN        2     81       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       88    188       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        74     74       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       156    156       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       160    160       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   226 AA;  26199 MW;  53B50AB3D54495D3 CRC64;
     MKHNLMELPF EQTALQPYIS AETIAYHYGK HHAGYVNKLN SLIEGTEYEE KPLEYIVKYA
     HNAIFNNAAQ IYNHDFYWKG LKNIPSAPSV ELLGLIERDF GSMKAFKDTF LTAGAALFGS
     GWVWLSISKE KRLEIKMTSN ADTPIRHGDT PLLTCDVWEH AYYIDYRNTR QEYLSNWWKL
     INWNFVSDNL SDFMNDPIAG YNQPCNAINS VCEYVDFMQN NERTPS
//
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