ID A0A0N1EJG8_9SPHN Unreviewed; 199 AA.
AC A0A0N1EJG8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Electron transporter {ECO:0000313|EMBL:KPH62140.1};
GN ORFNames=ADT71_16190 {ECO:0000313|EMBL:KPH62140.1};
OS Novosphingobium sp. ST904.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1684385 {ECO:0000313|EMBL:KPH62140.1, ECO:0000313|Proteomes:UP000037878};
RN [1] {ECO:0000313|EMBL:KPH62140.1, ECO:0000313|Proteomes:UP000037878}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST904 {ECO:0000313|EMBL:KPH62140.1,
RC ECO:0000313|Proteomes:UP000037878};
RA Thijs S., Bottos E.M., Van Hamme J.D., Gkorezis P., Rineau F.,
RA Vangronsveld J.;
RT "Novosphingobium nitrophenolicus strain ST904 degrades p-nitrophenol and
RT stimulates plant growth.";
RL Submitted (JUL-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:KPH62140.1}.
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DR EMBL; LGJH01000150; KPH62140.1; -; Genomic_DNA.
DR RefSeq; WP_054438537.1; NZ_SLVC01000020.1.
DR AlphaFoldDB; A0A0N1EJG8; -.
DR STRING; 1684385.ADT71_16190; -.
DR PATRIC; fig|1684385.3.peg.1729; -.
DR OrthoDB; 9790194at2; -.
DR Proteomes; UP000037878; 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:UP000037878};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..199
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005870418"
FT DOMAIN 25..199
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT BINDING 72
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 76
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 164
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT DISULFID 72..76
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ SEQUENCE 199 AA; 21647 MW; C704B03327380B39 CRC64;
MTYLFRRIAP IALALSMGMS LAACQQAATE APPLEGAQIG GPFTLSDKDG KAVTWDTFKG
KWRIVYFGYT FCPDACPMDV QAMMRGFTLF EKAHAAQAAG VQPIFITIDP ERDTREIVGQ
WTAAFGPRLY GLTGTPAQVR QAADAFAVYY KKGEATPGGY LMDHSRIAYL MDPDGKPIAM
LPVDKGPEAV SAELAKWVK
//