ID A0A0Q8EKK6_9GAMM Unreviewed; 217 AA.
AC A0A0Q8EKK6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|PROSITE:PS51352};
GN ORFNames=ASD72_13965 {ECO:0000313|EMBL:KRA42397.1};
OS Pseudoxanthomonas sp. Root630.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=1736574 {ECO:0000313|EMBL:KRA42397.1, ECO:0000313|Proteomes:UP000051081};
RN [1] {ECO:0000313|EMBL:KRA42397.1, ECO:0000313|Proteomes:UP000051081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root630 {ECO:0000313|EMBL:KRA42397.1,
RC ECO:0000313|Proteomes:UP000051081};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRA42397.1, ECO:0000313|Proteomes:UP000051081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root630 {ECO:0000313|EMBL:KRA42397.1,
RC ECO:0000313|Proteomes:UP000051081};
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 -!- SIMILARITY: Belongs to the SCO1/2 family.
CC {ECO:0000256|ARBA:ARBA00010996}.
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:KRA42397.1}.
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DR EMBL; LMGY01000018; KRA42397.1; -; Genomic_DNA.
DR RefSeq; WP_056881191.1; NZ_LMGY01000018.1.
DR AlphaFoldDB; A0A0Q8EKK6; -.
DR STRING; 1736574.ASD72_13965; -.
DR OrthoDB; 9790194at2; -.
DR Proteomes; UP000051081; Unassembled WGS sequence.
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; ELECTRON TRANSPORT PROTIN SCO1/SENC FAMILY MEMBER; 1.
DR PANTHER; PTHR12151:SF25; SCO1 PROTEIN HOMOLOG; 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}.
FT DOMAIN 45..217
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT BINDING 83
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 87
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 178
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT DISULFID 83..87
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ SEQUENCE 217 AA; 23464 MW; 7BC9F4CC3BC2149E CRC64;
MFNKKIGLIL VLALAAGLGL LAAQKFFGPV TPATQWPATE AVTLFPQARP LPPFSLRQSD
GTQLADGELK GHWTLVFLGF TFCPDVCPTT LAELAQAQAQ WKDLPDSTRP RVLFVSVDPE
RDTPTRIGEY AHAFHPDTMA ATADVPTLEN FAKSLGFVFM KVPGDGFDQN PNDYSMDHSS
AIGVLDPQGR LAGLIRPPFQ PKAIAADMRA LTEASSK
//
