ID   A0A0P6X0V0_9CHLR        Unreviewed;        83 AA.
AC   A0A0P6X0V0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Glutaredoxin {ECO:0000313|EMBL:KPL74464.1};
GN   ORFNames=AC812_11620 {ECO:0000313|EMBL:KPL74464.1};
OS   Bellilinea caldifistulae.
OC   Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC   Bellilinea.
OX   NCBI_TaxID=360411 {ECO:0000313|EMBL:KPL74464.1, ECO:0000313|Proteomes:UP000050514};
RN   [1] {ECO:0000313|EMBL:KPL74464.1, ECO:0000313|Proteomes:UP000050514}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GOMI-1 {ECO:0000313|EMBL:KPL74464.1,
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   -!- 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:KPL74464.1}.
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DR   EMBL; LGHJ01000017; KPL74464.1; -; Genomic_DNA.
DR   RefSeq; WP_061918658.1; NZ_LGHJ01000017.1.
DR   AlphaFoldDB; A0A0P6X0V0; -.
DR   STRING; 360411.AC812_11620; -.
DR   OrthoDB; 9800630at2; -.
DR   Proteomes; UP000050514; Unassembled WGS sequence.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR005243; THIRX-like_proc.
DR   NCBIfam; TIGR00412; redox_disulf_2; 1.
DR   PANTHER; PTHR36450; THIOREDOXIN; 1.
DR   PANTHER; PTHR36450:SF1; THIOREDOXIN; 1.
DR   Pfam; PF13192; Thioredoxin_3; 1.
DR   PIRSF; PIRSF037031; Redox_disulphide_2; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR037031-51};
KW   Redox-active center {ECO:0000256|PIRSR:PIRSR037031-51};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050514}.
FT   DOMAIN          3..77
FT                   /note="Thioredoxin-like fold"
FT                   /evidence="ECO:0000259|Pfam:PF13192"
FT   ACT_SITE        11
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037031-50"
FT   ACT_SITE        14
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037031-50"
FT   DISULFID        11..14
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037031-51"
SQ   SEQUENCE   83 AA;  9097 MW;  4236EFA07664DF57 CRC64;
     MLNIKILGVG CANCKRLEAV TREVVATLGI EAEFEKVTNH ADIMQYPILA TPGLVIEGKV
     VSYGRIPSKA EIENWLKEAV KTN
//