GenomeNet

Database: UniProt
Entry: C5AJ38_BURGB
LinkDB: C5AJ38_BURGB
Original site: C5AJ38_BURGB 
ID   C5AJ38_BURGB            Unreviewed;       412 AA.
AC   C5AJ38;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   SubName: Full=Thioredoxin {ECO:0000313|EMBL:ACR31918.1};
GN   OrderedLocusNames=bglu_2g15660 {ECO:0000313|EMBL:ACR31918.1};
OS   Burkholderia glumae (strain BGR1).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=626418 {ECO:0000313|EMBL:ACR31918.1, ECO:0000313|Proteomes:UP000002187};
RN   [1] {ECO:0000313|EMBL:ACR31918.1, ECO:0000313|Proteomes:UP000002187}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGR1 {ECO:0000313|EMBL:ACR31918.1,
RC   ECO:0000313|Proteomes:UP000002187};
RX   PubMed=19329631; DOI=10.1128/JB.00349-09;
RA   Lim J., Lee T.H., Nahm B.H., Choi Y.D., Kim M., Hwang I.;
RT   "Complete genome sequence of Burkholderia glumae BGR1.";
RL   J. Bacteriol. 191:3758-3759(2009).
CC   -!- SIMILARITY: Belongs to the thioredoxin family.
CC       {ECO:0000256|ARBA:ARBA00008987}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001504; ACR31918.1; -; Genomic_DNA.
DR   RefSeq; WP_015877611.1; NC_012721.2.
DR   AlphaFoldDB; C5AJ38; -.
DR   STRING; 626418.bglu_2g15660; -.
DR   GeneID; 58139128; -.
DR   KEGG; bgl:bglu_2g15660; -.
DR   PATRIC; fig|626418.3.peg.1860; -.
DR   eggNOG; COG3118; Bacteria.
DR   HOGENOM; CLU_675562_0_0_4; -.
DR   Proteomes; UP000002187; Chromosome 2.
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; 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:UP000002187};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          1..108
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   412 AA;  43954 MW;  8B1B9B35E89920B2 CRC64;
     MSSLKSVTEA SFEADVTLNS RPVLIDFWAE WCGPCKALAP TLEKVARNFE GKVDIVKVNV
     DEHPGLRERF GVRGIPALVL MNGANEAGRI VGNRTATQLA SYLDAHLGTV TQLARPEVTL
     SAFGGDAQAK ADRIARLRDY LERKQADPNT PMWPEKVTGA LAYVAGSSDP DDCAVALGIP
     SAVVEVVNSL FTYRGTNFNA ALFVADWLES VPVGADLSKL PGQLLTSILA GPIVSETLNG
     EPRLLAIRDA LVSLHAAETN GSPVGDASWA EHKQACQAVA AGLGEGNAAR AAAVLEVAAS
     SAAKNPDMLR GFVAAVCGFV RKCRQAECNW SPEDDSRFSS IAKGIYKHAI ETGAEPPMGD
     AMRKRIAEVD PELVARFKFH YDEGWRSAQE RGTAFGDLLI ALTRQTEVAS PV
//
DBGET integrated database retrieval system