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Database: UniProt/TrEMBL
Entry: A0A0D6I3S8_ALCXX
LinkDB: A0A0D6I3S8_ALCXX
Original site: A0A0D6I3S8_ALCXX 
ID   A0A0D6I3S8_ALCXX        Unreviewed;       192 AA.
AC   A0A0D6I3S8; A0A0M7CF22;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   18-JUL-2018, entry version 27.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   Name=sodB_1 {ECO:0000313|EMBL:CKH78489.1};
GN   ORFNames=AL504_30195 {ECO:0000313|EMBL:AMG39891.1}, BIZ92_30830
GN   {ECO:0000313|EMBL:OMG81597.1}, ERS369984_00532
GN   {ECO:0000313|EMBL:CUI39374.1}, ERS451415_03925
GN   {ECO:0000313|EMBL:CKH78489.1};
OS   Alcaligenes xylosoxydans xylosoxydans (Achromobacter xylosoxidans).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Achromobacter.
OX   NCBI_TaxID=85698 {ECO:0000313|EMBL:CKH78489.1, ECO:0000313|Proteomes:UP000059657};
RN   [1] {ECO:0000313|EMBL:CKH78489.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NCTC10807 {ECO:0000313|EMBL:CKH78489.1};
RA   Informatics Pathogen;
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CUI39374.1, ECO:0000313|Proteomes:UP000040179}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2789STDY5608609 {ECO:0000313|EMBL:CUI39374.1,
RC   ECO:0000313|Proteomes:UP000040179};
RA   Jackson K.R., Lunt B.L., Fisher J.N.B., Gardner A.V., Bailey M.E.,
RA   Deus L.M., Earl A.S., Gibby P.D., Hartmann K.A., Liu J.E., Manci A.M.,
RA   Nielsen D.A., Solomon M.B., Breakwell D.P., Burnett S.H., Grose J.H.;
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000060602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FDAARGOS_147 {ECO:0000313|Proteomes:UP000060602};
RA   Case J., Tallon L., Sadzewicz L., Sengamalay N., Ott S., Godinez A.,
RA   Nagaraj S., Nadendla S., Sichtig H.;
RT   "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT   Supporting development and validation of Infectious Disease Dx
RT   tests.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:OMG81597.1, ECO:0000313|Proteomes:UP000187251}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AUS488 {ECO:0000313|EMBL:OMG81597.1,
RC   ECO:0000313|Proteomes:UP000187251};
RA   Jeukens J., Freschi L., Vincent A.T., Emond-Rheault J.-G.,
RA   Kukavica-Ibrulj I., Charette S.J., Levesque R.C.;
RT   "Phylogenomics of Achromobacter.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EMBL:AMG39891.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FDAARGOS_147 {ECO:0000313|EMBL:AMG39891.1};
RA   Kerrigan L., Tallon L., Sadzewicz L., Sengamalay N., Ott S.,
RA   Godinez A., Nagaraj S., Vavikolanu K., Aluvathingal J., Nadendla S.,
RA   Sichtig H.;
RT   "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT   Supporting development and validation of Infectious Disease Dx
RT   tests.";
RL   Submitted (JAN-2018) 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; CP014060; AMG39891.1; -; Genomic_DNA.
DR   EMBL; LN831029; CKH78489.1; -; Genomic_DNA.
DR   EMBL; CYTP01000001; CUI39374.1; -; Genomic_DNA.
DR   EMBL; MJMN01000029; OMG81597.1; -; Genomic_DNA.
DR   RefSeq; WP_006383994.1; NZ_PHGT01000001.1.
DR   EnsemblBacteria; AMG39891; AMG39891; AL504_30195.
DR   EnsemblBacteria; CKH78489; CKH78489; ERS451415_03925.
DR   EnsemblBacteria; CUI39374; CUI39374; ERS369984_00532.
DR   GeneID; 29505334; -.
DR   KEGG; axx:ERS451415_03925; -.
DR   PATRIC; fig|85698.15.peg.946; -.
DR   KO; K04564; -.
DR   Proteomes; UP000040179; Unassembled WGS sequence.
DR   Proteomes; UP000059657; Chromosome 1.
DR   Proteomes; UP000060602; Chromosome.
DR   Proteomes; UP000187251; 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:UP000040179,
KW   ECO:0000313|Proteomes:UP000059657, ECO:0000313|Proteomes:UP000060602,
KW   ECO:0000313|Proteomes:UP000187251};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:CKH78489.1}.
FT   DOMAIN        3     81       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       89    189       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        74     74       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       157    157       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       161    161       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   192 AA;  21383 MW;  A85C1F9D2586935E CRC64;
     MAHTLPPLPY ELDALAPHIS KETLEFHYGK HHQTYVTNLN NLIPGTEFEN LSLEDIVKKS
     SGGIFNNAAQ IWNHTFYWNS LAPKAGGAPT GKLADAINAK WGSFDAFKEA FNKSAAGNFG
     SGWTWLVKKA DGSVDIVNTS NAATPLTTAD KPLLTCDVWE HAYYIDYRNA RPKYLENFWA
     LVNWDFAAKN FA
//
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