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Database: UniProt/TrEMBL
Entry: G2LI36_CHLTF
LinkDB: G2LI36_CHLTF
Original site: G2LI36_CHLTF 
ID   G2LI36_CHLTF            Unreviewed;       199 AA.
AC   G2LI36;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   25-OCT-2017, entry version 36.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   OrderedLocusNames=Cabther_A0491 {ECO:0000313|EMBL:AEP11252.1};
OS   Chloracidobacterium thermophilum (strain B).
OC   Bacteria; Acidobacteria; Blastocatellia; Chloracidobacterium.
OX   NCBI_TaxID=981222 {ECO:0000313|EMBL:AEP11252.1, ECO:0000313|Proteomes:UP000006791};
RN   [1] {ECO:0000313|EMBL:AEP11252.1, ECO:0000313|Proteomes:UP000006791}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B {ECO:0000313|EMBL:AEP11252.1,
RC   ECO:0000313|Proteomes:UP000006791};
RX   PubMed=21951563; DOI=10.1111/j.1462-2920.2011.02592.x;
RA   Garcia Costas A.M., Liu Z., Tomsho L.P., Schuster S.C., Ward D.M.,
RA   Bryant D.A.;
RT   "Complete genome of Candidatus Chloracidobacterium thermophilum, a
RT   chlorophyll-based photoheterotroph belonging to the phylum
RT   Acidobacteria.";
RL   Environ. Microbiol. 14:177-190(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: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {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; CP002514; AEP11252.1; -; Genomic_DNA.
DR   RefSeq; WP_014098990.1; NC_016024.1.
DR   ProteinModelPortal; G2LI36; -.
DR   STRING; 981222.Cabther_A0491; -.
DR   EnsemblBacteria; AEP11252; AEP11252; Cabther_A0491.
DR   KEGG; ctm:Cabther_A0491; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   Proteomes; UP000006791; 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   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:UP000006791};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:AEP11252.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006791}.
FT   DOMAIN        3     86       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       93    193       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        78     78       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   199 AA;  22157 MW;  30F42672B6E74199 CRC64;
     MPFDLPELPY AKDALAPHIS ATTFEFHHGK HHKAYVDNTN KLIEGTPHAD KSLEEIIQAA
     HTDGNAALFN NAAQVWNHTF FWNSMKPNGG GAPTGELADR INHAFGGLEQ FKEAFKQAGV
     TQFGSGWAWL VLDHGDLKII KTANADLPLV HGQTALLTCD VWEHAYYLDF QNRRPDFLQA
     YLDYLINWDF AAANLAQAA
//
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