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Database: UniProt/TrEMBL
Entry: A0A0M4GLG2_9GAMM
LinkDB: A0A0M4GLG2_9GAMM
Original site: A0A0M4GLG2_9GAMM 
ID   A0A0M4GLG2_9GAMM        Unreviewed;       208 AA.
AC   A0A0M4GLG2;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   25-OCT-2017, entry version 10.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=AMQ28_12820 {ECO:0000313|EMBL:ALD03142.1};
OS   Acinetobacter sp. TTH0-4.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter.
OX   NCBI_TaxID=1646498 {ECO:0000313|EMBL:ALD03142.1, ECO:0000313|Proteomes:UP000055186};
RN   [1] {ECO:0000313|EMBL:ALD03142.1, ECO:0000313|Proteomes:UP000055186}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TTH0-4 {ECO:0000313|EMBL:ALD03142.1,
RC   ECO:0000313|Proteomes:UP000055186};
RA   Zhang G.;
RT   "Acinetobacter qinghaiensis sp. nov., isolated from active layer of
RT   permafrost region.";
RL   Submitted (SEP-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}.
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DR   EMBL; CP012608; ALD03142.1; -; Genomic_DNA.
DR   RefSeq; WP_053579936.1; NZ_CP012608.1.
DR   EnsemblBacteria; ALD03142; ALD03142; AMQ28_12820.
DR   KEGG; att:AMQ28_12820; -.
DR   PATRIC; fig|1646498.3.peg.2574; -.
DR   KO; K04564; -.
DR   Proteomes; UP000055186; 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   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:UP000055186};
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:UP000055186}.
FT   DOMAIN        5     88       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       96    197       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        28     28       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        80     80       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   208 AA;  22870 MW;  474805EC56F8F45C CRC64;
     MTTITLPALP YGYEDLAPHI SKETLEYHHD KHHNTYVVNI NNLIKGTDLE GKTLEEIITA
     TAGDAAKAGI FNNAAQVWNH TFYWNCMAKN GGGKATGTLA AKIDEAFGSY EKFAEEFAAA
     ATTQFGSGWA WLVADEVNGN LSILKTANAD TPMAHGKVAV LTIDVWEHAY YIDFRNARPK
     YISTFLESLV NWDYANAKYA GQEAGVEK
//
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