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Database: UniProt
Entry: A0A0Q5QPR0_9FLAO
LinkDB: A0A0Q5QPR0_9FLAO
Original site: A0A0Q5QPR0_9FLAO 
ID   A0A0Q5QPR0_9FLAO        Unreviewed;       224 AA.
AC   A0A0Q5QPR0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   16-JAN-2019, entry version 13.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=ASG01_06625 {ECO:0000313|EMBL:KQR95513.1};
OS   Chryseobacterium sp. Leaf180.
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Chryseobacterium.
OX   NCBI_TaxID=1736289 {ECO:0000313|EMBL:KQR95513.1, ECO:0000313|Proteomes:UP000051405};
RN   [1] {ECO:0000313|EMBL:KQR95513.1, ECO:0000313|Proteomes:UP000051405}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf180 {ECO:0000313|EMBL:KQR95513.1,
RC   ECO:0000313|Proteomes:UP000051405};
RX   PubMed=26633631; DOI=.1038/nature16192;
RA   Bai Y., Muller D.B., Srinivas G., Garrido-Oter R., Potthoff E.,
RA   Rott M., Dombrowski N., Munch P.C., Spaepen S., Remus-Emsermann M.,
RA   Huttel B., McHardy A.C., Vorholt J.A., Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiota.";
RL   Nature 528:364-369(2015).
RN   [2] {ECO:0000313|Proteomes:UP000051405}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf180 {ECO:0000313|Proteomes:UP000051405};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000051405}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf180 {ECO:0000313|Proteomes:UP000051405};
RA   Vorholt J.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KQR95513.1}.
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DR   EMBL; LMPJ01000001; KQR95513.1; -; Genomic_DNA.
DR   RefSeq; WP_055861683.1; NZ_LMPJ01000001.1.
DR   EnsemblBacteria; KQR95513; KQR95513; ASG01_06625.
DR   OrthoDB; 1440645at2; -.
DR   Proteomes; UP000051405; 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:UP000051405};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051405};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     20       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        21    224       Superoxide dismutase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5006260112.
FT   DOMAIN       22    103       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      111    216       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        46     46       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        96     96       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       183    183       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       187    187       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   224 AA;  25130 MW;  8DD7F741383073F8 CRC64;
     MKMIKVAAFS AVLMAQFAMA QFKQSPLPYA YNALEGNIDA KTMEIHYSKH AAGYVANLNK
     AIAGTPQEKQ SLFQILSKAG TLPMAVRNNA GGHYNHELFW TVMTPEKNTK PSAKLSKAIN
     DSFGSMEAFK EKMSKAGADR FGSGWAWLSV DQNGKLFVSS TPNQDNPLMD VVEERGTPIF
     GIDVWEHAYY LKYQNKRADY LTAIWNVTNW KEISKRYEDA IAKK
//
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