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Database: UniProt
Entry: G4EN46_MYCIO
LinkDB: G4EN46_MYCIO
Original site: G4EN46_MYCIO 
ID   G4EN46_MYCIO            Unreviewed;       208 AA.
AC   G4EN46;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   16-JAN-2019, entry version 25.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=GUU_04129 {ECO:0000313|EMBL:EGZ31013.1};
OS   Mycoplasma iowae 695.
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=1048830 {ECO:0000313|EMBL:EGZ31013.1};
RN   [1] {ECO:0000313|EMBL:EGZ31013.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=695 {ECO:0000313|EMBL:EGZ31013.1};
RX   PubMed=22207750; DOI=10.1128/JB.06297-11;
RA   Wei S., Guo Z., Li T., Zhang T., Li X., Zhou Z., Li Z., Liu M.,
RA   Luo R., Bi D., Chen H., Zhou R., Jin H.;
RT   "Genome sequence of Mycoplasma iowae strain 695, an unusual pathogen
RT   causing deaths in turkeys.";
RL   J. Bacteriol. 194:547-548(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   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EGZ31013.1}.
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DR   EMBL; AGFP01000048; EGZ31013.1; -; Genomic_DNA.
DR   ProteinModelPortal; G4EN46; -.
DR   EnsemblBacteria; EGZ31013; EGZ31013; GUU_04129.
DR   PATRIC; fig|1048830.3.peg.733; -.
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   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN        2     88       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       96    194       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        26     26       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        81     81       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       164    164       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       168    168       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   208 AA;  24174 MW;  EB519E172A53FA4B CRC64;
     MYKLPLLGMN YDDLEPHIDA QTMEIHYTKH HQAYVDNLNA AIEKHPELDN KPLKELLLNF
     DKIPADIKGA IQNHGGGHHN HSLFWLILKK NGGAKPTGKL LEMINRDLGS FENFKEQFET
     HAKSKFGSGW AWLVINKDNK LEVTSTSNQD SPLMFGQKPV LGLDVWEHAY YLKYQNRRID
     YIKEFWNVIN WENVLKFVED ALVIECDK
//
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