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Database: UniProt
Entry: A0A0Q5QVE1_9ACTN
LinkDB: A0A0Q5QVE1_9ACTN
Original site: A0A0Q5QVE1_9ACTN 
ID   A0A0Q5QVE1_9ACTN        Unreviewed;       228 AA.
AC   A0A0Q5QVE1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   10-APR-2019, entry version 13.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=ASG12_05060 {ECO:0000313|EMBL:KQS00968.1};
OS   Williamsia sp. Leaf354.
OC   Bacteria; Actinobacteria; Corynebacteriales; Williamsiaceae;
OC   Williamsia.
OX   NCBI_TaxID=1736349 {ECO:0000313|EMBL:KQS00968.1, ECO:0000313|Proteomes:UP000051980};
RN   [1] {ECO:0000313|EMBL:KQS00968.1, ECO:0000313|Proteomes:UP000051980}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf354 {ECO:0000313|EMBL:KQS00968.1,
RC   ECO:0000313|Proteomes:UP000051980};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQS00968.1, ECO:0000313|Proteomes:UP000051980}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf354 {ECO:0000313|EMBL:KQS00968.1,
RC   ECO:0000313|Proteomes:UP000051980};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KQS00968.1}.
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DR   EMBL; LMPL01000001; KQS00968.1; -; Genomic_DNA.
DR   EnsemblBacteria; KQS00968; KQS00968; ASG12_05060.
DR   Proteomes; UP000051980; 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; 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   SUPFAM; SSF49329; SSF49329; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000051980};
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051980};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   SIGNAL        1     22       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        23    228       Superoxide dismutase [Cu-Zn].
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5006260229.
FT   DOMAIN       80    225       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   228 AA;  22420 MW;  A3256C5F5BEEEC64 CRC64;
     MRRALVLAAS TVAAGAVLTA CSPGEEPSSQ QGTTPAVVTG DQAPNNLGIN EREAGASPTE
     SGNAEPSGSG LTASLISPGG ARVGEATFST EGSAVRVDVK VTSGITPGFH GLHIHSVGKC
     ENNSVAPTGG APGAFLSAGG HFQVDGRTGH PASGDLVSIN VTGAGTGETV TTTSAFTLSQ
     IAGKSIMIHS GPDNFANIPT RYAPAPDQET LSTGDAGTRV ACGVIEQG
//
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