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Database: UniProt
Entry: F3PB77_9ACTO
LinkDB: F3PB77_9ACTO
Original site: F3PB77_9ACTO 
ID   F3PB77_9ACTO            Unreviewed;       207 AA.
AC   F3PB77;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   05-DEC-2018, entry version 29.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=HMPREF9056_02211 {ECO:0000313|EMBL:EGF53719.1};
OS   Actinomyces sp. oral taxon 170 str. F0386.
OC   Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae;
OC   Actinomyces.
OX   NCBI_TaxID=762963 {ECO:0000313|EMBL:EGF53719.1, ECO:0000313|Proteomes:UP000004404};
RN   [1] {ECO:0000313|EMBL:EGF53719.1, ECO:0000313|Proteomes:UP000004404}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0386 {ECO:0000313|EMBL:EGF53719.1,
RC   ECO:0000313|Proteomes:UP000004404};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B.,
RA   Courtney L., Fronick C., Harrison M., Strong C., Farmer C.,
RA   Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C.,
RA   Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M.,
RA   Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (FEB-2011) 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}.
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:EGF53719.1}.
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DR   EMBL; AFBL01000053; EGF53719.1; -; Genomic_DNA.
DR   RefSeq; WP_009404749.1; NZ_GL882544.1.
DR   STRING; 762963.HMPREF9056_02211; -.
DR   EnsemblBacteria; EGF53719; EGF53719; HMPREF9056_02211.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   OrthoDB; POG091H03Q7; -.
DR   Proteomes; UP000004404; Unassembled WGS sequence.
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:UP000004404};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN        4     84       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       91    193       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        28     28       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        76     76       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       160    160       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       164    164       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   207 AA;  22582 MW;  45D8B78253138135 CRC64;
     MAVYTLPELP YDYAALEPHI SGRIMELHHD KHHAAYVAGA NAALEALTAA REAGDLGAIN
     LWEKNLAFNL GGHTNHSIFW KNLSPHGGGQ PEGELAEAIK DSFGSFEKFQ AQFTAAALGI
     QGSGWAVLAY DSISGGLVIF QLFDQQGNVP VGTIPLFMVD MWEHAFYLDY LNVKADYVKA
     VWNIANWQDV AERLADAVAK AQGLIVR
//
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