ID Q16DC3_ROSDO Unreviewed; 223 AA.
AC Q16DC3;
DT 25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 25-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=Thiol-disulfide oxidoreductase D, Putative {ECO:0000313|EMBL:ABG30020.1};
GN Name=bdbD {ECO:0000313|EMBL:ABG30020.1};
GN OrderedLocusNames=RD1_0295 {ECO:0000313|EMBL:ABG30020.1};
OS Roseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter sp.
OS (strain OCh 114)) (Roseobacter denitrificans).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseobacter.
OX NCBI_TaxID=375451 {ECO:0000313|EMBL:ABG30020.1, ECO:0000313|Proteomes:UP000007029};
RN [1] {ECO:0000313|EMBL:ABG30020.1, ECO:0000313|Proteomes:UP000007029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33942 / OCh 114 {ECO:0000313|Proteomes:UP000007029};
RX PubMed=17098896; DOI=10.1128/JB.01390-06;
RA Swingley W.D., Sadekar S., Mastrian S.D., Matthies H.J., Hao J., Ramos H.,
RA Acharya C.R., Conrad A.L., Taylor H.L., Dejesa L.C., Shah M.K.,
RA O'huallachain M.E., Lince M.T., Blankenship R.E., Beatty J.T.,
RA Touchman J.W.;
RT "The complete genome sequence of Roseobacter denitrificans reveals a
RT mixotrophic rather than photosynthetic metabolism.";
RL J. Bacteriol. 189:683-690(2007).
CC -!- FUNCTION: May be required for disulfide bond formation in some
CC proteins. {ECO:0000256|ARBA:ARBA00003565}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbA subfamily.
CC {ECO:0000256|ARBA:ARBA00005791}.
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DR EMBL; CP000362; ABG30020.1; -; Genomic_DNA.
DR RefSeq; WP_011566642.1; NZ_FOOO01000001.1.
DR AlphaFoldDB; Q16DC3; -.
DR STRING; 375451.RD1_0295; -.
DR KEGG; rde:RD1_0295; -.
DR eggNOG; COG1651; Bacteria.
DR HOGENOM; CLU_000288_47_5_5; -.
DR OrthoDB; 8478320at2; -.
DR Proteomes; UP000007029; Chromosome.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR13887:SF55; DISULFIDE BOND FORMATION PROTEIN D; 1.
DR PANTHER; PTHR13887; GLUTATHIONE S-TRANSFERASE KAPPA; 1.
DR Pfam; PF13462; Thioredoxin_4; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000007029}.
FT DOMAIN 32..172
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 223 AA; 24257 MW; DAB9F26D9AEA3B22 CRC64;
MSRMMIISAA VAVIGLGAYF VTSPGTNPVT PANPLGAANA QEAADIDTSS IMDMTLGNPD
APVTVIEYAS YTCPHCARFH EGPFKQLKAD YIDTGKINFV YREVYFDRYG LWASMIARCA
GTPESFFGMS DLIYQKQSEW SRAGDPAAIV DELRKVGLLA GLDRDTMEAC LQNGEKAQTL
VAWYQENATA DGIESTPSFL INGQRYSNMS YAEMAELIDA AAE
//
