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Database: UniProt
Entry: D0J1B3_COMT2
LinkDB: D0J1B3_COMT2
Original site: D0J1B3_COMT2 
ID   D0J1B3_COMT2            Unreviewed;       211 AA.
AC   D0J1B3;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   16-JAN-2019, entry version 46.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   OrderedLocusNames=CtCNB1_3056 {ECO:0000313|EMBL:ACY33802.1};
OS   Comamonas testosteroni (strain CNB-2).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Comamonas.
OX   NCBI_TaxID=688245 {ECO:0000313|EMBL:ACY33802.1, ECO:0000313|Proteomes:UP000002360};
RN   [1] {ECO:0000313|EMBL:ACY33802.1, ECO:0000313|Proteomes:UP000002360}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNB-2 {ECO:0000313|Proteomes:UP000002360};
RX   PubMed=19734336; DOI=10.1128/AEM.00933-09;
RA   Ma Y.F., Zhang Y., Zhang J.Y., Chen D.W., Zhu Y., Zheng H., Wang S.Y.,
RA   Jiang C.Y., Zhao G.P., Liu S.J.;
RT   "The complete genome of Comamonas testosteroni reveals its genetic
RT   adaptations to changing environments.";
RL   Appl. Environ. Microbiol. 75:6812-6819(2009).
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; CP001220; ACY33802.1; -; Genomic_DNA.
DR   RefSeq; WP_012838994.1; NC_013446.2.
DR   STRING; 688245.CtCNB1_3056; -.
DR   EnsemblBacteria; ACY33802; ACY33802; CtCNB1_3056.
DR   KEGG; ctt:CtCNB1_3056; -.
DR   PATRIC; fig|688245.4.peg.3255; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013583; -.
DR   KO; K04564; -.
DR   OMA; YEGWKGE; -.
DR   OrthoDB; 1440645at2; -.
DR   Proteomes; UP000002360; 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:UP000002360};
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:UP000002360}.
FT   DOMAIN        2     89       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       96    201       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        81     81       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       168    168       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       172    172       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   211 AA;  23560 MW;  E1490461B3D92928 CRC64;
     MSYTLPPLAY DYAALEPHID AQTMEIHYSR HHQTYVNNLN AALEGSEYAQ WPLNDLLVKI
     ESLPQPLRQA VRNNGGGHAN HSLFWQVMSP KGGGLPQGAL AAAIDRDLGS FENFKTEFTK
     AAISRFGSGW AWLSVDHSGK LHVESSANQD SPLMPGIGSG NTPILTLDVW EHAYYLKYQN
     RRPEYIAAFY NVVDWNEVAR RFATATQAVR S
//
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