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Database: UniProt/TrEMBL
Entry: A0A1L6KNQ3_ACIHA
LinkDB: A0A1L6KNQ3_ACIHA
Original site: A0A1L6KNQ3_ACIHA 
ID   A0A1L6KNQ3_ACIHA        Unreviewed;       208 AA.
AC   A0A1L6KNQ3;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   25-OCT-2017, entry version 6.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=AHTJS_10155 {ECO:0000313|EMBL:APR70702.1};
OS   Acinetobacter haemolyticus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter.
OX   NCBI_TaxID=29430 {ECO:0000313|EMBL:APR70702.1, ECO:0000313|Proteomes:UP000185439};
RN   [1] {ECO:0000313|EMBL:APR70702.1, ECO:0000313|Proteomes:UP000185439}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TJS01 {ECO:0000313|EMBL:APR70702.1,
RC   ECO:0000313|Proteomes:UP000185439};
RA   Deng Y., Zhang S.-C., Song C.-C., Dong Y., Gao F., Huang H.;
RT   "Complete genome sequence of Acinetobacter haemolyticus strain TJS01
RT   isolated from a respiratory patient in china.";
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}.
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DR   EMBL; CP018871; APR70702.1; -; Genomic_DNA.
DR   RefSeq; WP_075315805.1; NZ_CP018871.1.
DR   KEGG; ahl:AHTJS_10155; -.
DR   KO; K04564; -.
DR   Proteomes; UP000185439; 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:UP000185439};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN        5     88       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       95    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;  22891 MW;  90E7D65032306EB5 CRC64;
     MTTITLPALP YGYDDLAPHI TRETLEYHHD KHHNTYVVNL NNLIKGTDLE GKSLEEIIKA
     SAGDASKAGI FNNAAQVWNH TFYWNSMKPN GGGKPTGAIA AKIDEAFGSY EKFAEEFTAA
     ATTQFGSGWA WLVADEVNGK LSITKTANAD TPLAHGQIAV LTIDVWEHAY YIDFRNLRPK
     YIATFLESLV NWDYANAKLA GQPAGVEK
//
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