ID A0A0Q5PA14_9SPHN Unreviewed; 201 AA.
AC A0A0Q5PA14;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Electron transporter {ECO:0000313|EMBL:KQR83628.1};
GN ORFNames=ASG07_07980 {ECO:0000313|EMBL:KQR83628.1};
OS Sphingomonas sp. Leaf343.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736345 {ECO:0000313|EMBL:KQR83628.1, ECO:0000313|Proteomes:UP000051323};
RN [1] {ECO:0000313|EMBL:KQR83628.1, ECO:0000313|Proteomes:UP000051323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf343 {ECO:0000313|EMBL:KQR83628.1,
RC ECO:0000313|Proteomes:UP000051323};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQR83628.1, ECO:0000313|Proteomes:UP000051323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf343 {ECO:0000313|EMBL:KQR83628.1,
RC ECO:0000313|Proteomes:UP000051323};
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:KQR83628.1}.
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DR EMBL; LMPG01000011; KQR83628.1; -; Genomic_DNA.
DR RefSeq; WP_055844596.1; NZ_LMPG01000011.1.
DR AlphaFoldDB; A0A0Q5PA14; -.
DR STRING; 1736345.ASG07_07980; -.
DR Proteomes; UP000051323; 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: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; PS51257; PROKAR_LIPOPROTEIN; 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:UP000051323}.
FT DOMAIN 22..201
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT BINDING 73
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 77
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 166
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT DISULFID 73..77
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ SEQUENCE 201 AA; 21295 MW; C943D25DD478191F CRC64;
MNKLSTVGDA MKTLLLAGLV SLSACQPAPT GKPPLEGARI GGPFTLIDQN GRTVTDRSFA
GKYRIMYFGY TFCPDVCPTD VQSISAGLKL AERSAPDKAA QVVPVFVTVD PARDTVPVLK
QFVSAFHPRL VGLTGDESAI AGIKKAYAVY AAKGEATPGG GYLVDHSRTA YLMDPDGKPL
VLVPQDEGPQ AVADTIEKWV R
//
