ID   A0A160FPY6_9BURK        Unreviewed;       189 AA.
AC   A0A160FPY6;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Electron transporter {ECO:0000313|EMBL:ANB74732.1};
GN   ORFNames=AYM40_14540 {ECO:0000313|EMBL:ANB74732.1};
OS   Paraburkholderia phytofirmans OLGA172.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=1417228 {ECO:0000313|EMBL:ANB74732.1, ECO:0000313|Proteomes:UP000076852};
RN   [1] {ECO:0000313|EMBL:ANB74732.1, ECO:0000313|Proteomes:UP000076852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OLGA172 {ECO:0000313|EMBL:ANB74732.1,
RC   ECO:0000313|Proteomes:UP000076852};
RX   PubMed=27063562; DOI=10.1016/j.gene.2016.04.018;
RA   Ricker N., Shen S.Y., Goordial J., Jin S., Fulthorpe R.R.;
RT   "PacBio SMRT assembly of a complex multi-replicon genome reveals
RT   chlorocatechol degradative operon in a region of genome plasticity.";
RL   Gene 586:239-247(2016).
CC   -!- SIMILARITY: Belongs to the SCO1/2 family.
CC       {ECO:0000256|ARBA:ARBA00010996}.
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DR   EMBL; CP014578; ANB74732.1; -; Genomic_DNA.
DR   RefSeq; WP_063498028.1; NZ_CP014578.1.
DR   AlphaFoldDB; A0A160FPY6; -.
DR   STRING; 1804984.AYM40_14540; -.
DR   KEGG; buz:AYM40_14540; -.
DR   Proteomes; UP000076852; Chromosome 1.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd02968; SCO; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR003782; SCO1/SenC.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR12151:SF5; AT19154P; 1.
DR   PANTHER; PTHR12151; ELECTRON TRANSPORT PROTIN SCO1/SENC FAMILY MEMBER; 1.
DR   Pfam; PF02630; SCO1-SenC; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|PIRSR:PIRSR603782-1};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR603782-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR603782-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076852}.
FT   DOMAIN          21..189
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   BINDING         61
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         65
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         151
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        61..65
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   189 AA;  20858 MW;  5957736E4163F9ED CRC64;
     MVGVLGALAG CTHRTEPFQL TNVTGHLPDL DLTLTSDDGR AVTGDSFKGR TSLVYFGYTH
     CPDVCPETMG RLMRVLGKLG PDAQKVRILF ITVDPARDTP KALHDYIGAF DSQHAEGLTG
     TDWQIESLAK RYRVAYQMEK GDPNGNYEVT HSSAVYVFDQ QGHARLLATD HDTPDTIAQD
     LRRIIDDHS
//