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Database: UniProt
Entry: A0A1B9SDT0_9RHIZ
LinkDB: A0A1B9SDT0_9RHIZ
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ID   A0A1B9SDT0_9RHIZ        Unreviewed;       169 AA.
AC   A0A1B9SDT0;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   05-DEC-2018, entry version 11.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=A6U86_01960 {ECO:0000313|EMBL:OCJ11848.1};
OS   Rhizobium sp. AC27/96.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=1841653 {ECO:0000313|EMBL:OCJ11848.1, ECO:0000313|Proteomes:UP000093320};
RN   [1] {ECO:0000313|EMBL:OCJ11848.1, ECO:0000313|Proteomes:UP000093320}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AC27/96 {ECO:0000313|EMBL:OCJ11848.1,
RC   ECO:0000313|Proteomes:UP000093320};
RX   PubMed=27547538; DOI=10.7717/peerj.2222;
RA   Davis E.W.II., Weisberg A.J., Tabima J.F., Grunwald N.J., Chang J.H.;
RT   "Gall-ID: tools for genotyping gall-causing phytopathogenic
RT   bacteria.";
RL   PeerJ 4:e2222-e2222(2016).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000256|RuleBase:RU000393}.
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:RU000393};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC       Note=Binds 1 copper ion per subunit.
CC       {ECO:0000256|RuleBase:RU000393};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC       Note=Binds 1 zinc ion per subunit.
CC       {ECO:0000256|RuleBase:RU000393};
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000256|RuleBase:RU000393}.
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:OCJ11848.1}.
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DR   EMBL; LXKN01000001; OCJ11848.1; -; Genomic_DNA.
DR   RefSeq; WP_068387694.1; NZ_LXKN01000001.1.
DR   EnsemblBacteria; OCJ11848; OCJ11848; A6U86_01960.
DR   Proteomes; UP000093320; 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   CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR   Gene3D; 2.60.40.200; -; 1.
DR   InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR   InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR   InterPro; IPR018152; SOD_Cu/Zn_BS.
DR   InterPro; IPR001424; SOD_Cu_Zn_dom.
DR   PANTHER; PTHR10003; PTHR10003; 1.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   PRINTS; PR00068; CUZNDISMTASE.
DR   SUPFAM; SSF49329; SSF49329; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000093320};
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   SIGNAL        1     21       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        22    169       Superoxide dismutase [Cu-Zn].
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5008636054.
FT   DOMAIN       36    168       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   169 AA;  17673 MW;  03B3695E96B0EB16 CRC64;
     MKRTMMIAAI LALAAATPAA AQGQNTATAD FVGLDGKPAG RATLTEGKAG VLIEMEVSGL
     PTNRWVAFHI HENSNCDHAH GFESAGGHFN PTKADHGFLA ANGPHAGDMP NQHVDQDGKL
     HAQVFNGMVS LNGKNGIRGR TLMIHAESDD YRSQPVGGAG KRLACAVIQ
//
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