GenomeNet

Database: UniProt
Entry: A0A1E7RMA7_9GAMM
LinkDB: A0A1E7RMA7_9GAMM
Original site: A0A1E7RMA7_9GAMM 
ID   A0A1E7RMA7_9GAMM        Unreviewed;       212 AA.
AC   A0A1E7RMA7;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   13-FEB-2019, entry version 10.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=BIY45_11885 {ECO:0000313|EMBL:OEZ00366.1};
OS   Stenotrophomonas sp. BIIR7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas.
OX   NCBI_TaxID=1904462 {ECO:0000313|EMBL:OEZ00366.1, ECO:0000313|Proteomes:UP000175905};
RN   [1] {ECO:0000313|EMBL:OEZ00366.1, ECO:0000313|Proteomes:UP000175905}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BIIR7 {ECO:0000313|EMBL:OEZ00366.1,
RC   ECO:0000313|Proteomes:UP000175905};
RA   Sanchez-Castro I., Ruiz-Fresneda M.A., Bakkali M., Kampfer P.,
RA   Busse H.J., Lopez-Fernandez M., Martinez-Rodriguez P., Merroun M.L.;
RT   "Stenotrophomonas bentonitica sp. nov., isolated from bentonite
RT   formations.";
RL   Submitted (SEP-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: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:OEZ00366.1}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; MKCZ01000051; OEZ00366.1; -; Genomic_DNA.
DR   RefSeq; WP_070208276.1; NZ_MKCZ01000051.1.
DR   EnsemblBacteria; OEZ00366; OEZ00366; BIY45_11885.
DR   Proteomes; UP000175905; 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; PS00087; SOD_CU_ZN_1; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000175905};
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     24       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        25    212       Superoxide dismutase [Cu-Zn].
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5009201851.
FT   DOMAIN       72    208       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   212 AA;  21396 MW;  EF0D14C3268BF82B CRC64;
     MRLIHTALFA AVAAVGLTAC NKPAETTTPE PTPATDTAPA AAAAAAANDA PPAMTSEAHA
     NHTAMAELAP TQGNNVKGNV TFSVVDGKVH VKGDISGLRP NSEHGFHIHE KGDCSAPNGD
     SAGGHFNPSK EDHGNLATTP HHGGDIPNIK ADAQGNAVVD ADVSTNVNIG EGNDFDIIGR
     GLIVHADADD YKTQPTGNAG ARLACAVIKA AP
//
DBGET integrated database retrieval system