GenomeNet

Database: UniProt/TrEMBL
Entry: A0A1U7CMS2_9BACT
LinkDB: A0A1U7CMS2_9BACT
Original site: A0A1U7CMS2_9BACT 
ID   A0A1U7CMS2_9BACT        Unreviewed;       205 AA.
AC   A0A1U7CMS2;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   30-AUG-2017, entry version 4.
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:APW60208.1};
GN   ORFNames=BSF38_01674 {ECO:0000313|EMBL:APW60208.1};
OS   Paludisphaera borealis.
OC   Bacteria; Planctomycetes; Planctomycetia; Planctomycetales;
OC   Isosphaeraceae; Paludisphaera.
OX   NCBI_TaxID=1387353 {ECO:0000313|EMBL:APW60208.1, ECO:0000313|Proteomes:UP000186309};
RN   [1] {ECO:0000313|EMBL:APW60208.1, ECO:0000313|Proteomes:UP000186309}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PX4 {ECO:0000313|EMBL:APW60208.1,
RC   ECO:0000313|Proteomes:UP000186309};
RA   Ivanova A.;
RT   "Comparative genomics of four Isosphaeraceae planctomycetes: a common
RT   pool of plasmids and glycoside hydrolase genes.";
RL   Submitted (DEC-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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP019082; APW60208.1; -; Genomic_DNA.
DR   RefSeq; WP_076344681.1; NZ_CP019082.1.
DR   Proteomes; UP000186309; 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:UP000186309};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:APW60208.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186309}.
FT   DOMAIN        3     90       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       98    199       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        28     28       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        83     83       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       166    166       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       170    170       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   205 AA;  22386 MW;  1FF021A3B6D14C21 CRC64;
     MAEYTLPPLP YDFGALEPHI DAKTMEIHHD KHHAAYVNNL NAALKDHPDH QGKPIEALIA
     NLNALPEGIR TAVRNNGGGH ANHSFFWQII GPGGGGEPKG ALAQAITSEL GGFPAFKEAF
     AKAAATRFGS GWAWLALGKD GKLAVTSTAN QDSPIMDGQT PILGIDVWEH AYYLKYQNRR
     PDYVSAFWNV INWDEVGRRY DAAKS
//
DBGET integrated database retrieval system