ID   A0A2U3CB09_9ACTN        Unreviewed;       152 AA.
AC   A0A2U3CB09;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Thioredoxin {ECO:0000313|EMBL:PWI46199.1};
GN   Name=trxA {ECO:0000313|EMBL:PWI46199.1};
GN   ORFNames=CK485_00115 {ECO:0000313|EMBL:PWI46199.1};
OS   Streptomyces sp. ICBB 8177.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=563922 {ECO:0000313|EMBL:PWI46199.1, ECO:0000313|Proteomes:UP000245673};
RN   [1] {ECO:0000313|EMBL:PWI46199.1, ECO:0000313|Proteomes:UP000245673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ICBB 8177 {ECO:0000313|EMBL:PWI46199.1,
RC   ECO:0000313|Proteomes:UP000245673};
RX   PubMed=29773836; DOI=10.1038/s41598-018-26179-w;
RA   Pavlikova M., Kamenik Z., Janata J., Kadlcik S., Kuzma M., Najmanova L.;
RT   "Novel pathway of 3-hydroxyanthranilic acid formation in limazepine
RT   biosynthesis reveals evolutionary relation between phenazines and
RT   pyrrolobenzodiazepines.";
RL   Sci. Rep. 8:7810-7810(2018).
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:PWI46199.1}.
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DR   EMBL; NSKH01000001; PWI46199.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U3CB09; -.
DR   OrthoDB; 9790390at2; -.
DR   Proteomes; UP000245673; 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   Gene3D; 2.30.30.380; Zn-finger domain of Sec23/24; 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   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:UP000245673};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          37..144
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   152 AA;  16126 MW;  DA563FD946312904 CRC64;
     MSTVQAANVA CPHCGRTNRV PAAAEGRPRC GACKQPLPWM ADAGDDDFTD VVEQATVPVV
     LDLWATWCGP CRMVSPALEE VATDLAGTIK LVKVDIDKSP RLARRFEVQA VPTLLVLDKG
     QTIARQSGAA PAPALRRWVE QSIAGRAPAG KG
//