ID Q1IGZ3_PSEE4 Unreviewed; 210 AA.
AC Q1IGZ3;
DT 13-JUN-2006, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2006, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE SubName: Full=Putative electron transport protein, Sco1/SenC family {ECO:0000313|EMBL:CAK13059.1};
GN OrderedLocusNames=PSEEN0065 {ECO:0000313|EMBL:CAK13059.1};
OS Pseudomonas entomophila (strain L48).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=384676 {ECO:0000313|EMBL:CAK13059.1, ECO:0000313|Proteomes:UP000000658};
RN [1] {ECO:0000313|EMBL:CAK13059.1, ECO:0000313|Proteomes:UP000000658}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L48 {ECO:0000313|EMBL:CAK13059.1,
RC ECO:0000313|Proteomes:UP000000658};
RX PubMed=16699499; DOI=10.1038/nbt1212;
RA Vodovar N., Vallenet D., Cruveiller S., Rouy Z., Barbe V., Acosta C.,
RA Cattolico L., Jubin C., Lajus A., Segurens B., Vacherie B., Wincker P.,
RA Weissenbach J., Lemaitre B., Medigue C., Boccard F.;
RT "Complete genome sequence of the entomopathogenic and metabolically
RT versatile soil bacterium Pseudomonas entomophila.";
RL Nat. Biotechnol. 24:673-679(2006).
CC -!- SIMILARITY: Belongs to the SCO1/2 family.
CC {ECO:0000256|ARBA:ARBA00010996}.
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DR EMBL; CT573326; CAK13059.1; -; Genomic_DNA.
DR RefSeq; WP_011531520.1; NC_008027.1.
DR AlphaFoldDB; Q1IGZ3; -.
DR STRING; 384676.PSEEN0065; -.
DR GeneID; 32803433; -.
DR KEGG; pen:PSEEN0065; -.
DR eggNOG; COG1999; Bacteria.
DR HOGENOM; CLU_050131_3_2_6; -.
DR OrthoDB; 9790194at2; -.
DR Proteomes; UP000000658; Chromosome.
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 46..208
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; 23113 MW; 7FC37879D09BAAF3 CRC64;
MTRTQKTVFI LVALVALIMG LTVNKVLSDR GQLNPTELID AGIILLPQSR TVPDVKMTDQ
NGQPVALDQL KGKWSLLFFG YTYCPDICPT TLAQLRQVKS ELPKEAIERL QVVLVSVDPH
RDTPNQLKQY LGYFDKDFVG VAGSIEDTQK LANALSIPFI PADTSKPGYT VDHSGNLAVV
GPDGRQRGFI RAPFNNQKLV AQLPGLVERD
//
