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
//