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Database: UniProt
Entry: K0DDG6_LEUCJ
LinkDB: K0DDG6_LEUCJ
Original site: K0DDG6_LEUCJ 
ID   K0DDG6_LEUCJ            Unreviewed;       372 AA.
AC   K0DDG6;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=tRNA-dihydrouridine synthase {ECO:0000256|PIRNR:PIRNR006621};
DE            EC=1.3.1.- {ECO:0000256|PIRNR:PIRNR006621};
GN   OrderedLocusNames=C270_03395 {ECO:0000313|EMBL:AFT81592.1};
OS   Leuconostoc carnosum (strain JB16).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Leuconostoc.
OX   NCBI_TaxID=1229758 {ECO:0000313|EMBL:AFT81592.1, ECO:0000313|Proteomes:UP000006299};
RN   [1] {ECO:0000313|EMBL:AFT81592.1, ECO:0000313|Proteomes:UP000006299}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JB16 {ECO:0000313|EMBL:AFT81592.1,
RC   ECO:0000313|Proteomes:UP000006299};
RX   PubMed=23144413; DOI=10.1128/JB.01805-12;
RA   Jung J.Y., Lee S.H., Jeon C.O.;
RT   "Complete genome sequence of Leuconostoc carnosum strain JB16, isolated
RT   from Kimchi.";
RL   J. Bacteriol. 194:6672-6673(2012).
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|ARBA:ARBA00001917,
CC         ECO:0000256|PIRNR:PIRNR006621};
CC   -!- SIMILARITY: Belongs to the dus family. {ECO:0000256|PIRNR:PIRNR006621}.
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DR   EMBL; CP003851; AFT81592.1; -; Genomic_DNA.
DR   RefSeq; WP_014974204.1; NC_018673.1.
DR   AlphaFoldDB; K0DDG6; -.
DR   STRING; 1229758.C270_03395; -.
DR   KEGG; lcn:C270_03395; -.
DR   PATRIC; fig|1229758.3.peg.680; -.
DR   eggNOG; COG0042; Bacteria.
DR   HOGENOM; CLU_013299_0_3_9; -.
DR   Proteomes; UP000006299; 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   InterPro; IPR018517; tRNA_hU_synthase_CS.
DR   PANTHER; PTHR11082:SF25; DUS DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR11082; TRNA-DIHYDROURIDINE SYNTHASE; 1.
DR   Pfam; PF01207; Dus; 1.
DR   PIRSF; PIRSF006621; Dus; 1.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR   PROSITE; PS01136; UPF0034; 1.
PE   3: Inferred from homology;
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|PIRNR:PIRNR006621};
KW   FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|PIRNR:PIRNR006621};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR006621};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006299};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694,
KW   ECO:0000256|PIRNR:PIRNR006621}.
FT   DOMAIN          33..332
FT                   /note="DUS-like FMN-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01207"
FT   ACT_SITE        122
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006621-1"
SQ   SEQUENCE   372 AA;  41136 MW;  A90D336286C0FD55 CRC64;
     MTLQSPQHNF WSKVVEKAQL GSDSAEKVPF FSLAPMEAVT DTIFRRVVAQ AGGPDVYFTE
     FTNASSMVHP KAKFSVQGRL AVAEGEQQPV AQIWGSRPET IAGAAKILPT MGFQAVDINM
     GCPDNTVIKN SAGSDLIRHP ELAVSVIAAA RQSGLAVSVK TRLGFSQAEE FREWLPIIFK
     QDIALLTIHL RSRKEMSKVP AHLEYIDEIL AMRDSIAPKT LIQLNGDIKT RAEGLALAQA
     HPGVDGIMIG RGIFENPYAF EKTPTPHTLE ESIALLNLQL DLFDDVNENV TSKHFEALKR
     YFKIYLRGFA HASALRQMLM ETHATNEVRD ILKRELDRVY AAVASDQHMY RDNTAASADM
     TATTLEKNSQ SV
//
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