ID   A0A257ENJ3_9PROT        Unreviewed;       303 AA.
AC   A0A257ENJ3;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Thioredoxin {ECO:0000313|EMBL:OYU15433.1};
GN   Name=trxA {ECO:0000313|EMBL:OYU15433.1};
GN   ORFNames=CFE37_05770 {ECO:0000313|EMBL:OYU15433.1};
OS   Alphaproteobacteria bacterium PA4.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria.
OX   NCBI_TaxID=2015572 {ECO:0000313|EMBL:OYU15433.1, ECO:0000313|Proteomes:UP000215773};
RN   [1] {ECO:0000313|EMBL:OYU15433.1, ECO:0000313|Proteomes:UP000215773}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PA4 {ECO:0000313|EMBL:OYU15433.1};
RA   Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA   Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT   "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT   formosa and its bacterial cohort.";
RL   Submitted (JUN-2017) 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:OYU15433.1}.
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DR   EMBL; NKIQ01000009; OYU15433.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A257ENJ3; -.
DR   Proteomes; UP000215773; Unassembled WGS sequence.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR   CDD; cd02956; ybbN; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR   InterPro; IPR005746; Thioredoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   NCBIfam; TIGR01068; thioredoxin; 1.
DR   PANTHER; PTHR45663; GEO12009P1; 1.
DR   PANTHER; PTHR45663:SF11; GEO12009P1; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   Pfam; PF14559; TPR_19; 1.
DR   Pfam; PF14561; TPR_20; 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   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW   Reference proteome {ECO:0000313|Proteomes:UP000215773};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          1..117
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   303 AA;  31878 MW;  AC8C0025F14F27FA CRC64;
     MTLASLATAA SDKASFDAFR RDVIDASKDA LVLVDFWAEW CGPCKTLGPL LERVTAANAP
     RVKLVKIDVD KNQALASQFR IQSIPTVYAF LKGQPVDGFQ GSLGERELKA FVERLLAGAP
     LPPDAADAEA QIAALIESAE AASAEGEHAE AAAILRALVQ ELPERDNLVG KYALVLIAAG
     DVSGANDALM TVAGDSKDPD VVRARAALAV ARDAVPVDDL AGLMAQVAAD PDNHALRFEL
     AGGLLARGDR DAAADALLTI IGADRGWNDS AAQQTLLKMF EATGLADPWS IKTRARLRSI
     LFA
//