ID A0A0P6X8F4_9CHLR Unreviewed; 119 AA.
AC A0A0P6X8F4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Thioredoxin {ECO:0000256|PIRNR:PIRNR000077};
GN ORFNames=AC812_01220 {ECO:0000313|EMBL:KPL78387.1};
OS Bellilinea caldifistulae.
OC Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC Bellilinea.
OX NCBI_TaxID=360411 {ECO:0000313|EMBL:KPL78387.1, ECO:0000313|Proteomes:UP000050514};
RN [1] {ECO:0000313|EMBL:KPL78387.1, ECO:0000313|Proteomes:UP000050514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GOMI-1 {ECO:0000313|EMBL:KPL78387.1,
RC ECO:0000313|Proteomes:UP000050514};
RA Hemp J., Ward L.M., Pace L.A., Fischer W.W.;
RT "Draft genome of Bellilinea caldifistulae DSM 17877.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the thioredoxin family.
CC {ECO:0000256|ARBA:ARBA00008987, ECO:0000256|PIRNR:PIRNR000077}.
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:KPL78387.1}.
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DR EMBL; LGHJ01000005; KPL78387.1; -; Genomic_DNA.
DR RefSeq; WP_061916307.1; NZ_LGHJ01000005.1.
DR AlphaFoldDB; A0A0P6X8F4; -.
DR STRING; 360411.AC812_01220; -.
DR PATRIC; fig|360411.5.peg.1946; -.
DR OrthoDB; 9790390at2; -.
DR Proteomes; UP000050514; 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 Reference proteome {ECO:0000313|Proteomes:UP000050514};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 2..109
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 33
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT ACT_SITE 36
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT SITE 27
FT /note="Deprotonates C-terminal active site Cys"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT SITE 34
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT SITE 35
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT DISULFID 33..36
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-4"
SQ SEQUENCE 119 AA; 13147 MW; 3B2415067882FD25 CRC64;
MIKEPVHVTD AAFEKTVLQS NLPVIVDFWA PWCGPCRMVA PILDKIAAEY AGKLIVAKVN
TDENPEWAMR YGVQGIPTML FVANGKVVHR QVGALPEGML REILDQFLEV VQSASAKNN
//