GenomeNet

Database: UniProt
Entry: A0A0A1VAD9_9BURK
LinkDB: A0A0A1VAD9_9BURK
Original site: A0A0A1VAD9_9BURK 
ID   A0A0A1VAD9_9BURK        Unreviewed;       143 AA.
AC   A0A0A1VAD9;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   SubName: Full=Thiol-disulfide isomerase and thioredoxins {ECO:0000313|EMBL:GAD20463.1};
GN   ORFNames=AVS7_00224 {ECO:0000313|EMBL:GAD20463.1};
OS   Acidovorax sp. MR-S7.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=1268622 {ECO:0000313|EMBL:GAD20463.1};
RN   [1] {ECO:0000313|EMBL:GAD20463.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-S7 {ECO:0000313|EMBL:GAD20463.1};
RX   DOI=10.1128/genomeA.00412-13;
RA   Miura T., Kusada H., Kamagata Y., Hanada S., Kimura N.;
RT   "Genome Sequence of the Multiple-beta-Lactam-Antibiotic-Resistant Bacterium
RT   Acidovorax sp. Strain MR-S7.";
RL   Genome Announc. 1:e00412-13(2013).
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; DF238892; GAD20463.1; -; Genomic_DNA.
DR   RefSeq; WP_024000747.1; NZ_DF238892.1.
DR   AlphaFoldDB; A0A0A1VAD9; -.
DR   STRING; 1268622.AVS7_00224; -.
DR   eggNOG; COG3118; Bacteria.
DR   OrthoDB; 9790390at2; -.
DR   Proteomes; UP000030646; Unassembled WGS sequence.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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; IPR049299; Thio2_N.
DR   InterPro; IPR005746; Thioredoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   InterPro; IPR013137; Znf_TFIIB.
DR   NCBIfam; TIGR01068; thioredoxin; 1.
DR   PANTHER; PTHR45663; GEO12009P1; 1.
DR   PANTHER; PTHR45663:SF11; GEO12009P1; 1.
DR   Pfam; PF21352; Thio2_N; 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.
DR   PROSITE; PS51134; ZF_TFIIB; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Isomerase {ECO:0000313|EMBL:GAD20463.1};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030646};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          1..140
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DOMAIN          1..33
FT                   /note="TFIIB-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51134"
SQ   SEQUENCE   143 AA;  15443 MW;  0C70490AE6A0621B CRC64;
     MHVGCPACGT INRVPDERPS GEPVCGRCGA ELMAATPASL SDATFERYIT RTDPPVLVDF
     WASWCGPCKM MAPHFDDAAA KLPDVRFAKL DIDANPQAVA ASAIRSVPTL ILYRAGKELA
     RHSGAMVAGD LVRWVRKYLT QKG
//
DBGET integrated database retrieval system