ID A0A1Y6KAI3_9CHLR Unreviewed; 323 AA.
AC A0A1Y6KAI3;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 28-JUN-2023, entry version 20.
DE RecName: Full=tRNA-dihydrouridine synthase {ECO:0000256|PIRNR:PIRNR006621};
DE EC=1.3.1.- {ECO:0000256|PIRNR:PIRNR006621};
GN ORFNames=CFX1CAM_1965 {ECO:0000313|EMBL:SMX55030.1};
OS Brevefilum fermentans.
OC Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC Brevefilum.
OX NCBI_TaxID=1986204 {ECO:0000313|EMBL:SMX55030.1, ECO:0000313|Proteomes:UP000195514};
RN [1] {ECO:0000313|Proteomes:UP000195514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kirkegaard R., Mcilroy J S.;
RL Submitted (MAY-2017) 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|ARBA:ARBA00002790,
CC ECO:0000256|PIRNR:PIRNR006621}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5,6-dihydrouridine in tRNA + NAD(+) = a uridine in tRNA +
CC H(+) + NADH; Xref=Rhea:RHEA:54452, Rhea:RHEA-COMP:13339, Rhea:RHEA-
CC COMP:13887, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74443;
CC Evidence={ECO:0000256|ARBA:ARBA00001387};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5,6-dihydrouridine in tRNA + NADP(+) = a uridine in tRNA +
CC H(+) + NADPH; Xref=Rhea:RHEA:23624, Rhea:RHEA-COMP:13339, Rhea:RHEA-
CC COMP:13887, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74443;
CC Evidence={ECO:0000256|ARBA:ARBA00001183};
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; LT859958; SMX55030.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y6KAI3; -.
DR KEGG; abat:CFX1CAM_1965; -.
DR Proteomes; UP000195514; Chromosome i.
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; 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; IPR024036; tRNA-dHydroUridine_Synthase_C.
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 ECO:0000313|EMBL:SMX55030.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000195514};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW tRNA processing {ECO:0000256|PIRNR:PIRNR006621}.
FT DOMAIN 23..291
FT /note="DUS-like FMN-binding"
FT /evidence="ECO:0000259|Pfam:PF01207"
FT ACT_SITE 111
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006621-1"
SQ SEQUENCE 323 AA; 36259 MW; 6198DB58DD446B8C CRC64;
MQDQMADKPT LMVGTVPIYG DLILAPMDGI TDLPFRGLCR RLGSAMSVTE FINALDVLEH
HPRYPKRHAF EPYHRPLSLQ LLGDQPEQIL QAALQLVPQV QPDIIDINLG CQSKNVVSRG
AGAALLKTPE TIAAIFRLMR ENFSQPITAK IRLGWDEDSL NYLEVAQAIE ENGCAMLAVH
GRTRNQAFRG QARWEPIREL KQGLTIPVIG NGDVRTVADI ERIKSITGCD AVMIGRAAVG
NPWIFSRVDR HDVPPQTVHT TILAHLQAML QFYGERGVIG FRKFLKAYLA HDNIPREALL
SLLNSQDPSF IIRWIDDYYD HRA
//
