ID C1BCX1_RHOOB Unreviewed; 208 AA.
AC C1BCX1;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Putative thiol-disulfide oxidoreductase {ECO:0000313|EMBL:BAH55715.1};
DE EC=1.8.-.- {ECO:0000313|EMBL:BAH55715.1};
GN OrderedLocusNames=ROP_pROB01-02160 {ECO:0000313|EMBL:BAH55715.1};
OS Rhodococcus opacus (strain B4).
OG Plasmid pROB01 {ECO:0000313|EMBL:BAH55715.1,
OG ECO:0000313|Proteomes:UP000002212}.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH55715.1, ECO:0000313|Proteomes:UP000002212};
RN [1] {ECO:0000313|EMBL:BAH55715.1, ECO:0000313|Proteomes:UP000002212}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4 {ECO:0000313|EMBL:BAH55715.1,
RC ECO:0000313|Proteomes:UP000002212};
RC PLASMID=pROB01 {ECO:0000313|EMBL:BAH55715.1,
RC ECO:0000313|Proteomes:UP000002212};
RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT PR4 and Rhodococcus opacus B4.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; AP011116; BAH55715.1; -; Genomic_DNA.
DR AlphaFoldDB; C1BCX1; -.
DR KEGG; rop:ROP_pROB01-02160; -.
DR PATRIC; fig|632772.20.peg.7942; -.
DR HOGENOM; CLU_042529_11_1_11; -.
DR Proteomes; UP000002212; Plasmid pROB01.
DR GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd02966; TlpA_like_family; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR42852; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBE; 1.
DR PANTHER; PTHR42852:SF6; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBE; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000313|EMBL:BAH55715.1};
KW Plasmid {ECO:0000313|EMBL:BAH55715.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..208
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039726113"
FT DOMAIN 45..202
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 208 AA; 22273 MW; CC08806B82EDDB06 CRC64;
MTTPTPQRLL RRRVVLAAVC AALLTAPACA TGADAVAQGG TFDFVAPGGQ TDIFYDPPQA
RGSIGALTGP DLMTDRPVSL ADYAGHVVVI NLWGQWCAPC RSEADDLERA YTATADRGVR
FLGINVRDPG RDKAQDFVVD NAVTYPSIYD PPMRTLLALG GSYPTSVIPS TLVLDRQHRV
AAVFLRALLT EDLQPVIERV AAEPGDPR
//
