ID A0A290QP34_9BACT Unreviewed; 340 AA.
AC A0A290QP34;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=tRNA-dihydrouridine synthase {ECO:0000256|PIRNR:PIRNR006621};
DE EC=1.3.1.- {ECO:0000256|PIRNR:PIRNR006621};
GN ORFNames=CMV30_18445 {ECO:0000313|EMBL:ATC66232.1};
OS Nibricoccus aquaticus.
OC Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae;
OC Nibricoccus.
OX NCBI_TaxID=2576891 {ECO:0000313|EMBL:ATC66232.1, ECO:0000313|Proteomes:UP000217265};
RN [1] {ECO:0000313|EMBL:ATC66232.1, ECO:0000313|Proteomes:UP000217265}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HZ-65 {ECO:0000313|EMBL:ATC66232.1,
RC ECO:0000313|Proteomes:UP000217265};
RA Choi A.;
RT "Complete genome sequence of Verrucomicrobial strain HZ-65, isolated from
RT freshwater.";
RL Submitted (SEP-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|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; CP023344; ATC66232.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A290QP34; -.
DR KEGG; vbh:CMV30_18445; -.
DR OrthoDB; 9764501at2; -.
DR Proteomes; UP000217265; 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 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:UP000217265};
KW tRNA processing {ECO:0000256|PIRNR:PIRNR006621}.
FT DOMAIN 1..288
FT /note="DUS-like FMN-binding"
FT /evidence="ECO:0000259|Pfam:PF01207"
FT ACT_SITE 85
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006621-1"
SQ SEQUENCE 340 AA; 38073 MW; 4D93F6D9F28AD70A CRC64;
MQDVTDLAFM RVIAHYGAPD YFVTEFFRVH SQSRPEKHII RSIDENQTGR PVFAQLIGEN
IHDLTRTTEE LLRHPVAGID LNLGCPAPKV YKKNVGGGLL REPAKIAEIL TALRATVPGL
FTVKMRIGFE DTRHFDEILS IVNDNNVDLL SVHGRTVKEM YRSDVHYDWI AHAVSRVRCP
VLANGNVTSA VKAADVVATT KAAGVMIGRH AIRNPWIFRQ CRERFSGQPI SRITLSDVRE
YIERLFHATK HDGIPERAHV NKMKKYLNFV GQSVDATGAF LHDMRRTETP VELFAACDRH
LLAEPAKEFP SEPYPGVIAR PNCETPDSAS NGCSLENVTA
//
