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Database: UniProt
Entry: A0A0Q1BDV2_9RHOB
LinkDB: A0A0Q1BDV2_9RHOB
Original site: A0A0Q1BDV2_9RHOB 
ID   A0A0Q1BDV2_9RHOB        Unreviewed;       199 AA.
AC   A0A0Q1BDV2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   28-MAR-2018, entry version 10.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=AL073_05470 {ECO:0000313|EMBL:KQB98324.1};
OS   Loktanella sp. 1ANDIMAR09.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Loktanella.
OX   NCBI_TaxID=1700845 {ECO:0000313|EMBL:KQB98324.1, ECO:0000313|Proteomes:UP000050370};
RN   [1] {ECO:0000313|EMBL:KQB98324.1, ECO:0000313|Proteomes:UP000050370}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1ANDIMAR09 {ECO:0000313|EMBL:KQB98324.1,
RC   ECO:0000313|Proteomes:UP000050370};
RA   Mas-Llado M., Nogales B., Bosch R.;
RT   "Draft genome sequence of Loktanella sp. 1ANDIMAR09.";
RL   Submitted (AUG-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: 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   -!- 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:KQB98324.1}.
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DR   EMBL; LIGP01000001; KQB98324.1; -; Genomic_DNA.
DR   RefSeq; WP_055293094.1; NZ_LIGP01000001.1.
DR   EnsemblBacteria; KQB98324; KQB98324; AL073_05470.
DR   PATRIC; fig|1700845.4.peg.1132; -.
DR   Proteomes; UP000050370; 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:UP000050370};
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:UP000050370}.
FT   DOMAIN        3     89       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       98    198       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        28     28       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   199 AA;  22122 MW;  0444D6567171B499 CRC64;
     MAFSLPDLPY AHDALASKGM SAETLEFHHD LHHNAYVTNG NKAIEGTEWE GKSLEEIIVG
     TYDKSAVAQN GIFNNISQLW NHNQFWEMMG PNDSAMPGEL EKALVESFGS VDEFKSQFSA
     AGAGQFGSGW CWLVKNADGS LAVTKTENGV NPLCFGQTAL LGCDVWEHSY YIDYRNKRPA
     YLTNFLDNLV NWENVASRM
//
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