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Database: UniProt/TrEMBL
Entry: A0A143PHC2_9BACT
LinkDB: A0A143PHC2_9BACT
Original site: A0A143PHC2_9BACT 
ID   A0A143PHC2_9BACT        Unreviewed;       198 AA.
AC   A0A143PHC2;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   30-AUG-2017, entry version 9.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   Name=sodA {ECO:0000313|EMBL:AMY07643.1};
GN   ORFNames=LuPra_00817 {ECO:0000313|EMBL:AMY07643.1};
OS   Luteitalea pratensis.
OC   Bacteria; Acidobacteria; Acidobacteria subdivision 6; Luteitalea.
OX   NCBI_TaxID=1855912 {ECO:0000313|EMBL:AMY07643.1, ECO:0000313|Proteomes:UP000076079};
RN   [1] {ECO:0000313|Proteomes:UP000076079}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 100886 HEG_-6_39 {ECO:0000313|Proteomes:UP000076079};
RA   Huang S., Vieira S., Bunk B., Riedel T., Sproeer C., Overmann J.;
RT   "First Complete Genome Sequence of a Subdivision 6 Acidobacterium.";
RL   Submitted (APR-2016) 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: 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; CP015136; AMY07643.1; -; Genomic_DNA.
DR   EnsemblBacteria; AMY07643; AMY07643; LuPra_00817.
DR   KEGG; abac:LuPra_00817; -.
DR   PATRIC; fig|1813736.3.peg.853; -.
DR   KO; K04564; -.
DR   Proteomes; UP000076079; Chromosome.
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   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:UP000076079};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:AMY07643.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076079}.
FT   DOMAIN        3     90       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       97    196       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        82     82       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   198 AA;  22010 MW;  0B95A69C6BB61D2F CRC64;
     MPYELPPLPY AHNALEPFID EQTMQIHHGK HHQTYVNNVN AALEKYPELQ GKPIDQLIAD
     LNAIPEDIRT AVRNNGGGHA NHTFFWAVMA PNAGGSPTGK IAEAINAKFG SFDAFKEAFA
     KAGTTRFGSG WAWLIKSGSG VEVTSTPNQD SPLMEGKMPL LGLDVWEHAY YLKYQNKRPD
     YIAAWWNVVN WDAVNNAF
//
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