ID A0A0X8JW19_9FUSO Unreviewed; 335 AA.
AC A0A0X8JW19;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=tRNA-dihydrouridine synthase {ECO:0000256|PIRNR:PIRNR006621};
DE EC=1.3.1.- {ECO:0000256|PIRNR:PIRNR006621};
GN ORFNames=AXF11_10105 {ECO:0000313|EMBL:AMD95892.1};
OS Leptotrichia sp. oral taxon 847.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC Leptotrichia.
OX NCBI_TaxID=1785996 {ECO:0000313|EMBL:AMD95892.1, ECO:0000313|Proteomes:UP000065271};
RN [1] {ECO:0000313|Proteomes:UP000065271}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0260 {ECO:0000313|Proteomes:UP000065271};
RA Holder M.E., Ajami N.J., Petrosino J.F.;
RL Submitted (FEB-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|ARBA:ARBA00001917,
CC ECO:0000256|PIRNR:PIRNR006621};
CC -!- SIMILARITY: Belongs to the dus family. {ECO:0000256|PIRNR:PIRNR006621}.
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DR EMBL; CP014231; AMD95892.1; -; Genomic_DNA.
DR RefSeq; WP_068157900.1; NZ_CP014231.1.
DR AlphaFoldDB; A0A0X8JW19; -.
DR STRING; 1785996.AXF11_10105; -.
DR KEGG; lot:AXF11_10105; -.
DR OrthoDB; 9764501at2; -.
DR Proteomes; UP000065271; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0017150; F:tRNA dihydrouridine synthase activity; IEA:InterPro.
DR CDD; cd02801; DUS_like_FMN; 1.
DR Gene3D; 1.20.120.1460; -; 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; IPR004653; DusA.
DR InterPro; IPR018517; tRNA_hU_synthase_CS.
DR PANTHER; PTHR42907; FMN-LINKED OXIDOREDUCTASES SUPERFAMILY PROTEIN; 1.
DR PANTHER; PTHR42907:SF1; FMN-LINKED OXIDOREDUCTASES SUPERFAMILY PROTEIN; 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 tRNA processing {ECO:0000256|ARBA:ARBA00022694,
KW ECO:0000256|PIRNR:PIRNR006621}.
FT DOMAIN 12..325
FT /note="DUS-like FMN-binding"
FT /evidence="ECO:0000259|Pfam:PF01207"
FT ACT_SITE 97
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006621-1"
SQ SEQUENCE 335 AA; 38636 MW; 28FD1032F19E0556 CRC64;
MEKDIVQNKI SVAPMVDRTD RHFRNFVRMI NKDVLMYTEM ITAQAIINGN LDYILGFDKI
ENPIVLQIAA TNPEDAYKAV KIAEKYDYDE INLNVGCPSE RVSGNMMGAS LMAYPEKVAK
ILEAMKAATK KTVSIKHRIG IDGRKILPDA LSKKVFDTYE DMKNFVEIIR KVGIKKFIIH
ARIAVLAGLD TKQNREVPPL RYDEVYKIKK EIPDLYVEIN GGIKTAEQID NHLKEVDAVM
IGRQIYDNPM ILTKFGKYYG KKIEVTREEI IERMIKYVEK MELEGIRPHL FLRHTHGLFF
GQRGSKFWKR AINDPKAGSF VLKNLLKELK NERKI
//
