ID E6X7N4_CELAD Unreviewed; 342 AA.
AC E6X7N4;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=tRNA-dihydrouridine synthase {ECO:0000256|PIRNR:PIRNR006621};
DE EC=1.3.1.- {ECO:0000256|PIRNR:PIRNR006621};
GN OrderedLocusNames=Celal_3480 {ECO:0000313|EMBL:ADV50744.1};
OS Cellulophaga algicola (strain DSM 14237 / IC166 / ACAM 630).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Cellulophaga.
OX NCBI_TaxID=688270 {ECO:0000313|EMBL:ADV50744.1, ECO:0000313|Proteomes:UP000008634};
RN [1] {ECO:0000313|EMBL:ADV50744.1, ECO:0000313|Proteomes:UP000008634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14237 / IC166 / ACAM 630
RC {ECO:0000313|Proteomes:UP000008634};
RX PubMed=21475589; DOI=10.4056/sigs.1543845;
RA Abt B., Lu M., Misra M., Han C., Nolan M., Lucas S., Hammon N.,
RA Deshpande S., Cheng J.F., Tapia R., Goodwin L., Pitluck S., Liolios K.,
RA Pagani I., Ivanova N., Mavromatis K., Ovchinikova G., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA Brambilla E., Rohde M., Tindall B.J., Goker M., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA Lapidus A.;
RT "Complete genome sequence of Cellulophaga algicola type strain (IC166).";
RL Stand. Genomic Sci. 4:72-80(2010).
CC -!- FUNCTION: Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified
CC base found in the D-loop of most tRNAs, via the reduction of the C5-C6
CC double bond in target uridines. {ECO:0000256|PIRNR:PIRNR006621}.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|PIRNR:PIRNR006621};
CC -!- SIMILARITY: Belongs to the dus family. {ECO:0000256|PIRNR:PIRNR006621}.
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DR EMBL; CP002453; ADV50744.1; -; Genomic_DNA.
DR AlphaFoldDB; E6X7N4; -.
DR STRING; 688270.Celal_3480; -.
DR KEGG; cao:Celal_3480; -.
DR eggNOG; COG0042; Bacteria.
DR HOGENOM; CLU_013299_6_0_10; -.
DR Proteomes; UP000008634; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0017150; F:tRNA dihydrouridine synthase activity; IEA:InterPro.
DR CDD; cd02801; DUS_like_FMN; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR035587; DUS-like_FMN-bd.
DR InterPro; IPR001269; DUS_fam.
DR PANTHER; PTHR45846; TRNA-DIHYDROURIDINE(47) SYNTHASE [NAD(P)(+)]-LIKE; 1.
DR PANTHER; PTHR45846:SF1; TRNA-DIHYDROURIDINE(47) SYNTHASE [NAD(P)(+)]-LIKE; 1.
DR Pfam; PF01207; Dus; 1.
DR PIRSF; PIRSF006621; Dus; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
PE 3: Inferred from homology;
KW Flavoprotein {ECO:0000256|PIRNR:PIRNR006621};
KW FMN {ECO:0000256|PIRNR:PIRNR006621};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR006621};
KW tRNA processing {ECO:0000256|PIRNR:PIRNR006621}.
FT DOMAIN 32..287
FT /note="DUS-like FMN-binding"
FT /evidence="ECO:0000259|Pfam:PF01207"
FT ACT_SITE 120
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006621-1"
SQ SEQUENCE 342 AA; 39329 MW; 563DC19EC9EECFD5 CRC64;
MFNKVSYFTK GKGQGCIFAA NLFLMSFTLL SSPLQGFTDF RFRNAFHHFF GGIDTFYAPY
IRLDGKLVIK SSYQRDLQLE NNAALNLIPQ VMTNDADEFL FVVKYIQDLG YTELNWNLGC
PYPMVTKRGM GSGLVKEADK IDHILDRVHA ETNVTVSMKM RMGYEDSSEI LDTFPVLEKY
PIKNIAIHAR IGKQLYKGGV DLDAFQRCVE STSHKLYYNG DITTVDAFKK MQERFPSIDH
WMIGRGLIAD PFLPSMIKAN TFEYPENRWA IFSEFHDTIY QDYDAFLSGP TPIKMKMQGF
WEFFANSFSN PQKTFKAIKK ANNPRAYQST VAEILKKEMS LT
//
