ID A0A1D9FL96_9CLOT Unreviewed; 105 AA.
AC A0A1D9FL96;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Thioredoxin {ECO:0000256|PIRNR:PIRNR000077};
GN ORFNames=BJL90_09780 {ECO:0000313|EMBL:AOY76166.1};
OS Clostridium formicaceticum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1497 {ECO:0000313|EMBL:AOY76166.1, ECO:0000313|Proteomes:UP000177894};
RN [1] {ECO:0000313|EMBL:AOY76166.1, ECO:0000313|Proteomes:UP000177894}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27076 {ECO:0000313|EMBL:AOY76166.1,
RC ECO:0000313|Proteomes:UP000177894};
RA Bao T., Cheng C., Zhao J., Yang S.-T., Wang J., Wang M.;
RT "Complete Genome Sequence of Acetogen Clostridium formicoaceticum ATCC
RT 27076.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the thioredoxin family.
CC {ECO:0000256|ARBA:ARBA00008987, ECO:0000256|PIRNR:PIRNR000077}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP017603; AOY76166.1; -; Genomic_DNA.
DR RefSeq; WP_070967215.1; NZ_CP020559.1.
DR AlphaFoldDB; A0A1D9FL96; -.
DR STRING; 1497.BJL90_09780; -.
DR KEGG; cfm:BJL90_09780; -.
DR OrthoDB; 9790390at2; -.
DR Proteomes; UP000177894; Chromosome.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR CDD; cd02947; TRX_family; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR005746; Thioredoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR45663; GEO12009P1; 1.
DR PANTHER; PTHR45663:SF11; GEO12009P1; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR PIRSF; PIRSF000077; Thioredoxin; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR000077-4};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|PIRSR:PIRSR000077-4};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 1..105
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 29
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT ACT_SITE 32
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT SITE 23
FT /note="Deprotonates C-terminal active site Cys"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT SITE 30
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT SITE 31
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT DISULFID 29..32
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-4"
SQ SEQUENCE 105 AA; 11959 MW; 75F03EE45ECBCC3A CRC64;
MLAVDKDTFQ TEVLEAQGYV LVDYWSESCE PCKALMPSVM ELSEKYNNSI KFCKLDTTKA
RRLAIKEKVL GLPTIAVYKD GKKIDEVTKE DATIENIETM IKKYA
//