ID R7KTH5_BACT4 Unreviewed; 99 AA. AC R7KTH5; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 24-JAN-2024, entry version 31. DE SubName: Full=Thioredoxin C-2 {ECO:0000313|EMBL:CDE79704.1}; GN ORFNames=BN644_03596 {ECO:0000313|EMBL:CDE79704.1}; OS Bacteroides thetaiotaomicron CAG:40. OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=1263054 {ECO:0000313|EMBL:CDE79704.1, ECO:0000313|Proteomes:UP000018192}; RN [1] {ECO:0000313|EMBL:CDE79704.1, ECO:0000313|Proteomes:UP000018192} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:40 {ECO:0000313|Proteomes:UP000018192}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S., RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T., RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N., RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T., RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R., RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N., RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W., RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., RA Wang J., Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units of RT genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the thioredoxin family. CC {ECO:0000256|ARBA:ARBA00008987}. 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:CDE79704.1}. 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; CBJO010000163; CDE79704.1; -; Genomic_DNA. DR AlphaFoldDB; R7KTH5; -. DR Proteomes; UP000018192; Unassembled WGS sequence. 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; IPR017937; Thioredoxin_CS. DR InterPro; IPR013766; Thioredoxin_domain. DR NCBIfam; TIGR01068; thioredoxin; 1. DR PANTHER; PTHR45663; GEO12009P1; 1. DR PANTHER; PTHR45663:SF11; GEO12009P1; 1. DR Pfam; PF00085; Thioredoxin; 1. DR PIRSF; PIRSF000077; Thioredoxin; 1. DR PRINTS; PR00421; THIOREDOXIN. DR SUPFAM; SSF52833; Thioredoxin-like; 1. DR PROSITE; PS00194; THIOREDOXIN_1; 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..99 FT /note="Thioredoxin" FT /evidence="ECO:0000259|PROSITE:PS51352" FT ACT_SITE 23 FT /note="Nucleophile" FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1" FT ACT_SITE 26 FT /note="Nucleophile" FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1" FT SITE 17 FT /note="Deprotonates C-terminal active site Cys" FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1" FT SITE 24 FT /note="Contributes to redox potential value" FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1" FT SITE 25 FT /note="Contributes to redox potential value" FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1" FT DISULFID 23..26 FT /note="Redox-active" FT /evidence="ECO:0000256|PIRSR:PIRSR000077-4" SQ SEQUENCE 99 AA; 11344 MW; 2037C6E75986C413 CRC64; MEKFEDLIQS PIPVLVDFFA EWCGPCKAMK PVLEELKTMV GDKARIVKID VDQHEDLATK YRIQAVPTFI LFKNGEAVWR HSGVIHSSEL KGIIEQNYI //