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Database: UniProt
Entry: A0A0H3KH62_BURM1
LinkDB: A0A0H3KH62_BURM1
Original site: A0A0H3KH62_BURM1 
ID   A0A0H3KH62_BURM1        Unreviewed;       282 AA.
AC   A0A0H3KH62;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Thioredoxin {ECO:0000313|EMBL:BAG44421.1};
GN   Name=ybbN {ECO:0000313|EMBL:BAG44421.1};
GN   OrderedLocusNames=BMULJ_02530 {ECO:0000313|EMBL:BAG44421.1};
OS   Burkholderia multivorans (strain ATCC 17616 / 249).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=395019 {ECO:0000313|EMBL:BAG44421.1, ECO:0000313|Proteomes:UP000008815};
RN   [1] {ECO:0000313|EMBL:BAG44421.1, ECO:0000313|Proteomes:UP000008815}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17616 / 249 {ECO:0000313|Proteomes:UP000008815};
RA   Ohtsubo Y., Yamashita A., Kurokawa K., Takami H., Yuhara S., Nishiyama E.,
RA   Endo R., Miyazaki R., Ono A., Yano K., Ito M., Sota M., Yuji N.,
RA   Hattori M., Tsuda M.;
RT   "Complete genome sequence of Burkholderia multivorans ATCC 17616.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the thioredoxin family.
CC       {ECO:0000256|ARBA:ARBA00008987}.
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DR   EMBL; AP009385; BAG44421.1; -; Genomic_DNA.
DR   RefSeq; WP_006406435.1; NC_010804.1.
DR   AlphaFoldDB; A0A0H3KH62; -.
DR   STRING; 395019.BMULJ_02530; -.
DR   GeneID; 66527478; -.
DR   KEGG; bmj:BMULJ_02530; -.
DR   eggNOG; COG3118; Bacteria.
DR   HOGENOM; CLU_046120_1_1_4; -.
DR   Proteomes; UP000008815; Chromosome 1.
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   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   SUPFAM; SSF48452; TPR-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:UP000008815};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          1..106
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   282 AA;  31324 MW;  DA8138EBC3F1CB98 CRC64;
     MDTTLATFER DVIEASLDTP VLVDFWAPWC GPCKTLGPLL EKLERDYAGR WKLVKVNVDE
     NQELAAHFQT RSIPHVIAFA DGRPVDQFIG VLPEGQLRAF LDRLLPAPEE AERRAAQIAI
     AEARFDDGLA HLEAALALNP GFDDARLDLI ELLLASNRID DARAEAERLS PQTVQGADPR
     YQAIKTRFDA LDATADLPPT DALEARIAAN PGDLDARFDL AQSLIARRAY EGALEQLLEI
     VTRDRTYGDD LGRRTMISVF ELAADRPDLV AAWRRKLSMA LN
//
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