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Database: UniProt
Entry: A0A0Q6VXK3_9BURK
LinkDB: A0A0Q6VXK3_9BURK
Original site: A0A0Q6VXK3_9BURK 
ID   A0A0Q6VXK3_9BURK        Unreviewed;       587 AA.
AC   A0A0Q6VXK3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Thioredoxin reductase {ECO:0000313|EMBL:KQV78553.1};
GN   ORFNames=ASD15_22385 {ECO:0000313|EMBL:KQV78553.1};
OS   Massilia sp. Root351.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Massilia.
OX   NCBI_TaxID=1736522 {ECO:0000313|EMBL:KQV78553.1, ECO:0000313|Proteomes:UP000051876};
RN   [1] {ECO:0000313|EMBL:KQV78553.1, ECO:0000313|Proteomes:UP000051876}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root351 {ECO:0000313|EMBL:KQV78553.1,
RC   ECO:0000313|Proteomes:UP000051876};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQV78553.1, ECO:0000313|Proteomes:UP000051876}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root351 {ECO:0000313|EMBL:KQV78553.1,
RC   ECO:0000313|Proteomes:UP000051876};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQV78553.1}.
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DR   EMBL; LMDJ01000036; KQV78553.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q6VXK3; -.
DR   Proteomes; UP000051876; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd00038; CAP_ED; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   PANTHER; PTHR48105:SF5; BLR1248 PROTEIN; 1.
DR   PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR   Pfam; PF00027; cNMP_binding; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   SMART; SM00100; cNMP; 1.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051876}.
FT   DOMAIN          32..152
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   587 AA;  62512 MW;  1BDD8F41B7D03320 CRC64;
     MAHDDTPFQA EANANNAIEG VPSSLESRRH QMFPTLTEAE IKRMDRFGTV RHFRNGERLF
     EAGRTTFGML VILKGRVAIS RYDGLGNTSL IIEHGAGQFC AEVGQLSDRP SLVNGDAVGD
     VEVLVIPSES LRALVVAEAE LGERIVRALI LRRVGLIEAP SGGPVLVGAP SHPRLHNLQT
     WLQSNGHPYS VLDPKHDAQA RALCEHYQPT ADEMPLVVCP DGSVKKNPTN VDLGRCLGML
     PELGSDKVWD VIVVGAGPAG LATAVYAASE GLSVLALETR AFGGQAAASA RIENYLGFPT
     GISGGALAGR AYVQSQKFGV EIAIPAPAGR LICDTYPLQV EMCGSLTRLQ AKTVVLSCGA
     RYRRPSLANL KQFEGRGVYY WASPIEAKLC KTEEIVLVGG GNSAGQAAVF LSGHASKVHM
     LVRGPSLAAT MSSYLIERIQ ATPNIVLHTH SEIVALEGDD EQGLQQVRIR CSKSDTETDY
     DVCRVFLFIG ADPNTGWLSD CGVDVDSKGF IRTGFDVTKA QCRANFAKGV YPADLPARAA
     LETSVPGVFA IGDVRANSTK RVAAAVGEGA AVVSQIHAFL ANLPPEL
//
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