ID Q2GE34_NEOSM Unreviewed; 331 AA.
AC Q2GE34;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE RecName: Full=tRNA-dihydrouridine synthase {ECO:0000256|PIRNR:PIRNR006621};
DE EC=1.3.1.- {ECO:0000256|PIRNR:PIRNR006621};
GN OrderedLocusNames=NSE_0373 {ECO:0000313|EMBL:ABD45936.1};
OS Neorickettsia sennetsu (strain ATCC VR-367 / Miyayama) (Ehrlichia
OS sennetsu).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Neorickettsia.
OX NCBI_TaxID=222891 {ECO:0000313|EMBL:ABD45936.1, ECO:0000313|Proteomes:UP000001942};
RN [1] {ECO:0000313|EMBL:ABD45936.1, ECO:0000313|Proteomes:UP000001942}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-367 / Miyayama {ECO:0000313|Proteomes:UP000001942};
RX PubMed=16482227; DOI=10.1371/journal.pgen.0020021;
RA Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V.,
RA Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M.,
RA Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N., Nelson W.,
RA Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J., Daugherty S.C.,
RA Davidsen T., Durkin A.S., Gwinn M., Haft D.H., Selengut J.D.,
RA Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R.,
RA Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H.;
RT "Comparative genomics of emerging human ehrlichiosis agents.";
RL PLoS Genet. 2:208-222(2006).
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|ARBA:ARBA00001917,
CC ECO:0000256|PIRNR:PIRNR006621};
CC -!- SIMILARITY: Belongs to the dus family. {ECO:0000256|PIRNR:PIRNR006621}.
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DR EMBL; CP000237; ABD45936.1; -; Genomic_DNA.
DR RefSeq; WP_011451768.1; NC_007798.1.
DR AlphaFoldDB; Q2GE34; -.
DR STRING; 222891.NSE_0373; -.
DR KEGG; nse:NSE_0373; -.
DR eggNOG; COG0042; Bacteria.
DR HOGENOM; CLU_013299_0_3_5; -.
DR OrthoDB; 9764501at2; -.
DR Proteomes; UP000001942; 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; 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; IPR004652; DusB-like.
DR InterPro; IPR024036; tRNA-dHydroUridine_Synthase_C.
DR InterPro; IPR018517; tRNA_hU_synthase_CS.
DR NCBIfam; TIGR00737; nifR3_yhdG; 1.
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.
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 NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR006621};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694,
KW ECO:0000256|PIRNR:PIRNR006621}.
FT DOMAIN 15..321
FT /note="DUS-like FMN-binding"
FT /evidence="ECO:0000259|Pfam:PF01207"
FT ACT_SITE 102
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006621-1"
SQ SEQUENCE 331 AA; 36987 MW; 5DEC660267F66AD1 CRC64;
MKLNLANNIS IDNVILAPMS GVTDMPYRDL VKSFGAGLVV SEMIASRAMI LKTKDTMKKV
SLSPREDITA IQLAGFEPDV MAEAAKINED MGAKIIDINF GCPVKKVVNG YAGSYLMKDE
CHAAKILEAT VKAVKIPVTL KMRTGWDENH RNAPKLAKIA EDLGIKMITI HGRTRAQMYK
GKSDWQFIRT VKNTVKIPVI ANGDIKTYED AERALVESGA DGIMIGRGAY GKPWSIRNML
HFLRTGKKLQ EPTPQEKLPI ILQHISSIFS HYGTEMGIGI ARKHILWYSA NYKNSAEFRQ
QICQETCVEK LLERVEEFFH SACCTTKLPQ Q
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