ID   A0A421BGI8_9LACT        Unreviewed;       105 AA.
AC   A0A421BGI8;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   RecName: Full=Thioredoxin {ECO:0000256|PIRNR:PIRNR000077};
GN   ORFNames=D3H64_04325 {ECO:0000313|EMBL:RLK63466.1};
OS   Atopobacter sp. AH10.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC   Atopobacter.
OX   NCBI_TaxID=2315861 {ECO:0000313|EMBL:RLK63466.1, ECO:0000313|Proteomes:UP000283681};
RN   [1] {ECO:0000313|EMBL:RLK63466.1, ECO:0000313|Proteomes:UP000283681}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AH10 {ECO:0000313|EMBL:RLK63466.1,
RC   ECO:0000313|Proteomes:UP000283681};
RA   Jeong H., Chang D.-H., Kim B.-C.;
RT   "Genome sequence of Atopobacter sp. AH10.";
RL   Submitted (SEP-2018) 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:RLK63466.1}.
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DR   EMBL; QXPZ01000019; RLK63466.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A421BGI8; -.
DR   Proteomes; UP000283681; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000283681};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          1..104
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;  12105 MW;  0DA50DA0D82456A6 CRC64;
     MMIKEIKQEE FKEAIAEGFV LLDVYGPHCG PCRMLDKTLH ILEREYPDMT ILKLDSSLNE
     QFCEENHIVG VPTLFFFFNG ELKERLTGAL SEDELMEIAG PYLYA
//