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Database: UniProt
Entry: A5VWP3_PSEP1
LinkDB: A5VWP3_PSEP1
Original site: A5VWP3_PSEP1 
ID   A5VWP3_PSEP1            Unreviewed;       210 AA.
AC   A5VWP3;
DT   10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   10-JUL-2007, sequence version 1.
DT   24-JAN-2024, entry version 80.
DE   SubName: Full=Electron transport protein SCO1/SenC {ECO:0000313|EMBL:ABQ76303.1};
DE   Flags: Precursor;
GN   OrderedLocusNames=Pput_0128 {ECO:0000313|EMBL:ABQ76303.1};
OS   Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=351746 {ECO:0000313|EMBL:ABQ76303.1};
RN   [1] {ECO:0000313|EMBL:ABQ76303.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F1 {ECO:0000313|EMBL:ABQ76303.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., Parales R., Richardson P.;
RT   "Complete sequence of Pseudomonas putida F1.";
RL   Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the SCO1/2 family.
CC       {ECO:0000256|ARBA:ARBA00010996}.
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DR   EMBL; CP000712; ABQ76303.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5VWP3; -.
DR   KEGG; ppf:Pput_0128; -.
DR   eggNOG; COG1999; Bacteria.
DR   HOGENOM; CLU_050131_3_2_6; -.
DR   OMA; GELKGHW; -.
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; LDI DOMAIN-CONTAINING PROTEIN; 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          46..210
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   BINDING         84
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         88
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         173
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        84..88
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   210 AA;  22990 MW;  09963457036DB337 CRC64;
     MTRTQKTVFI LVALVALILG LTVNKVLNGR DQPNPAELID AGIILLPQSR AVADVTMTNQ
     DGQPVQMDDL KGKWSLLFFG YTYCPDICPT TLAQLRQVKS ELPKDTVDRL QVVLVSVDPN
     RDTPNQLKQY LGYFDKDFVG VAGSIEDTQK LANALSIPFI PADTSKPGYT VDHSGNLAIV
     GPDGRQRGFI RAPFNNQKLG AQLPGLVKRD
//
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