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Database: UniProt
Entry: V2UVC9_9GAMM
LinkDB: V2UVC9_9GAMM
Original site: V2UVC9_9GAMM 
ID   V2UVC9_9GAMM            Unreviewed;       208 AA.
AC   V2UVC9;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   16-JAN-2019, entry version 21.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=P255_00769 {ECO:0000313|EMBL:ESK52610.1};
OS   Acinetobacter brisouii CIP 110357.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter.
OX   NCBI_TaxID=1341683 {ECO:0000313|EMBL:ESK52610.1, ECO:0000313|Proteomes:UP000018418};
RN   [1] {ECO:0000313|EMBL:ESK52610.1, ECO:0000313|Proteomes:UP000018418}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 110357 {ECO:0000313|EMBL:ESK52610.1,
RC   ECO:0000313|Proteomes:UP000018418};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Cerqueira G., Feldgarden M., Courvalin P., Grillot-Courvalin C.,
RA   Clermont D., Rocha E., Yoon E.-J., Nemec A., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Berlin A.M.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Gnerre S., Griggs A.,
RA   Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A., Larimer J.,
RA   McCowan C., Murphy C., Pearson M., Poon T.W., Priest M., Roberts A.,
RA   Saif S., Shea T., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Acinetobacter brisouii CIP 110357.";
RL   Submitted (OCT-2013) 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:ESK52610.1}.
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DR   EMBL; AYEU01000003; ESK52610.1; -; Genomic_DNA.
DR   RefSeq; WP_004903735.1; NZ_KI530762.1.
DR   EnsemblBacteria; ESK52610; ESK52610; P255_00769.
DR   PATRIC; fig|1341683.3.peg.760; -.
DR   OrthoDB; 1440645at2; -.
DR   Proteomes; UP000018418; 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:UP000018418};
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:UP000018418}.
FT   DOMAIN        5     87       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;  22690 MW;  DBEF3D51367841D6 CRC64;
     MTTITLPALP YGYDALEPHI SKETLEFHHD KHHQTYVTNL NNLIKGTDLE GKSLEEIILA
     SAGDASKAGI FNNAAQVWNH TFYWNSIAPN GGGKPTGAIA AKIDEAFGSY EKFAEQFATA
     AATQFGSGWA WLVADKVNGN LSIVKTSNAD TPLAHGQVAV LTIDVWEHAY YIDYRNARPK
     YISTFLESLV NWDYANAKLA GQAAGVEK
//
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