ID A0A1G6TQ95_9BACT Unreviewed; 321 AA.
AC A0A1G6TQ95;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 11.
DE RecName: Full=tRNA-dihydrouridine synthase {ECO:0000256|PIRNR:PIRNR006621};
DE EC=1.3.1.- {ECO:0000256|PIRNR:PIRNR006621};
GN ORFNames=SAMN05216323_11283 {ECO:0000313|EMBL:SDD30495.1};
OS Williamwhitmania taraxaci.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Williamwhitmaniaceae;
OC Williamwhitmania.
OX NCBI_TaxID=1640674 {ECO:0000313|EMBL:SDD30495.1, ECO:0000313|Proteomes:UP000199452};
RN [1] {ECO:0000313|EMBL:SDD30495.1, ECO:0000313|Proteomes:UP000199452}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A7P-90m {ECO:0000313|EMBL:SDD30495.1,
RC ECO:0000313|Proteomes:UP000199452};
RA Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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; FMYP01000128; SDD30495.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6TQ95; -.
DR STRING; 1640674.SAMN05216323_11283; -.
DR OrthoDB; 9764501at2; -.
DR Proteomes; UP000199452; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000199452};
KW tRNA processing {ECO:0000256|PIRNR:PIRNR006621}.
FT DOMAIN 10..286
FT /note="DUS-like FMN-binding"
FT /evidence="ECO:0000259|Pfam:PF01207"
FT ACT_SITE 99
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006621-1"
SQ SEQUENCE 321 AA; 35937 MW; 7A613BE9E1B5F17A CRC64;
MIMAAPIFYL APLQGFTEYP FRKAMLAAGT IPSFFVAPFV DAHEYARGKA RRLKDILPEN
NEGISLIPQL LGSNPDELAV LMAWYRELGY SNVSFNLGCP YPMVALKGSG SGLIGKPEVV
RAILDKLFTT FPDIQLSVKT RLGYLDSSEI ETLIPVLNQF PLAEVVVHPR IGKQLYKGDA
DLDAFAKVLP TIKAPVCYNG DILSVTDYQE RSKRFPTVTR WMIGRAALQN PLIFNDIAGG
IESDLDEKLS AMHKLHDALF QHYVASLSGN SHLIKKMAPF WEYFSLPFPE RRKAYKKVVK
ATTADHYRNA TNEFFAKQIS V
//
