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Database: UniProt
Entry: Q9KNN7_VIBCH
LinkDB: Q9KNN7_VIBCH
Original site: Q9KNN7_VIBCH 
ID   Q9KNN7_VIBCH            Unreviewed;       222 AA.
AC   Q9KNN7;
DT   01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2000, sequence version 1.
DT   05-DEC-2018, entry version 90.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   OrderedLocusNames=VC_2694 {ECO:0000313|EMBL:AAF95835.1};
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=243277 {ECO:0000313|EMBL:AAF95835.1, ECO:0000313|Proteomes:UP000000584};
RN   [1] {ECO:0000313|EMBL:AAF95835.1, ECO:0000313|Proteomes:UP000000584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961
RC   {ECO:0000313|Proteomes:UP000000584};
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A.,
RA   Gill S.R., Nelson K.E., Read T.D., Tettelin H., Richardson D.,
RA   Ermolaeva M.D., Vamathevan J., Bass S., Qin H., Dragoi I., Sellers P.,
RA   McDonald L., Utterback T., Fleishmann R.D., Nierman W.C., White O.,
RA   Salzberg S.L., Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C.,
RA   Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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; AE003852; AAF95835.1; -; Genomic_DNA.
DR   PIR; C82044; C82044.
DR   RefSeq; NP_232322.1; NC_002505.1.
DR   RefSeq; WP_001884029.1; NC_002505.1.
DR   ProteinModelPortal; Q9KNN7; -.
DR   STRING; 243277.VC2694; -.
DR   DNASU; 2615522; -.
DR   EnsemblBacteria; AAF95835; AAF95835; VC_2694.
DR   GeneID; 2615522; -.
DR   KEGG; vch:VC2694; -.
DR   PATRIC; fig|243277.26.peg.2569; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   KO; K04564; -.
DR   OMA; YEGWKGE; -.
DR   BioCyc; VCHO:VC2694-MONOMER; -.
DR   Proteomes; UP000000584; 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:UP000000584};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000584}.
FT   DOMAIN       20    102       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      109    212       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        44     44       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        94     94       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       180    180       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       184    184       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   222 AA;  25349 MW;  1EDEE1E601E39042 CRC64;
     MLSALLIAKR YSSKEDTMPH LFPDLPYAYD ALEPYIDTKT MEVHYSKHHR TYYDKFLSAI
     KGTEHEDRPL SEIFARVSTL PAAVRNHGGG YYNHIVYWNC MKPNAGGEPQ GELAAEIERQ
     FGSFAQFKEA FSQAAVNTFG SGFVWLIVQQ GQLSITSTSN QDNPLMDVVA VRGEPILALD
     VWEHAYYIRY QNRRPEYIDA WWNVVNWEAV SENYAIALTQ AA
//
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