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Database: UniProt
Entry: A0A0Q5PTK5_9BURK
LinkDB: A0A0Q5PTK5_9BURK
Original site: A0A0Q5PTK5_9BURK 
ID   A0A0Q5PTK5_9BURK        Unreviewed;       174 AA.
AC   A0A0Q5PTK5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Superoxide dismutase {ECO:0000313|EMBL:KQR90364.1};
GN   ORFNames=ASG35_01210 {ECO:0000313|EMBL:KQR90364.1};
OS   Burkholderia sp. Leaf177.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=1736287 {ECO:0000313|EMBL:KQR90364.1, ECO:0000313|Proteomes:UP000051826};
RN   [1] {ECO:0000313|EMBL:KQR90364.1, ECO:0000313|Proteomes:UP000051826}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf177 {ECO:0000313|EMBL:KQR90364.1,
RC   ECO:0000313|Proteomes:UP000051826};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQR90364.1, ECO:0000313|Proteomes:UP000051826}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf177 {ECO:0000313|EMBL:KQR90364.1,
RC   ECO:0000313|Proteomes:UP000051826};
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000256|ARBA:ARBA00010457}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQR90364.1}.
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DR   EMBL; LMPF01000001; KQR90364.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q5PTK5; -.
DR   Proteomes; UP000051826; Unassembled WGS sequence.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0006801; P:superoxide metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.40.200; Superoxide dismutase, copper/zinc binding domain; 1.
DR   InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR   InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR   InterPro; IPR001424; SOD_Cu_Zn_dom.
DR   PANTHER; PTHR10003:SF71; SUPEROXIDE DISMUTASE; 1.
DR   PANTHER; PTHR10003; SUPEROXIDE DISMUTASE CU-ZN -RELATED; 1.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   SUPFAM; SSF49329; Cu,Zn superoxide dismutase-like; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|ARBA:ARBA00023008};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051826};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          47..172
FT                   /note="Superoxide dismutase copper/zinc binding"
FT                   /evidence="ECO:0000259|Pfam:PF00080"
SQ   SEQUENCE   174 AA;  17992 MW;  AC6B19E433702F29 CRC64;
     MARFCTRAAT GFALTAGTLL LSGCGIFFQN HEKRADATLQ STAGSSVSGS LTFIERADGV
     QVSYNLSGMP PNSEHALQIH ERGDCIVSNP SDGGPVFSPA ADRSRSSKVE GDLATIRADA
     NGSATGFIVA PDLSLDGVRS VLSRAVLLHR DTSDSYSLSP HGAGPALACG VIRQ
//
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