ID A0A1H0W2F6_9CLOT Unreviewed; 321 AA.
AC A0A1H0W2F6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=tRNA-dihydrouridine synthase {ECO:0000256|PIRNR:PIRNR006621};
DE EC=1.3.1.- {ECO:0000256|PIRNR:PIRNR006621};
GN ORFNames=SAMN04488529_1287 {ECO:0000313|EMBL:SDP84892.1};
OS Clostridium gasigenes.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=94869 {ECO:0000313|EMBL:SDP84892.1, ECO:0000313|Proteomes:UP000198597};
RN [1] {ECO:0000313|EMBL:SDP84892.1, ECO:0000313|Proteomes:UP000198597}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12272 {ECO:0000313|EMBL:SDP84892.1,
RC ECO:0000313|Proteomes:UP000198597};
RA de Groot N.N.;
RL Submitted (OCT-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; FNJM01000028; SDP84892.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0W2F6; -.
DR STRING; 94869.SAMN04488529_1287; -.
DR OrthoDB; 9764501at2; -.
DR Proteomes; UP000198597; 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 InterPro; IPR018517; tRNA_hU_synthase_CS.
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 Reference proteome {ECO:0000313|Proteomes:UP000198597};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694,
KW ECO:0000256|PIRNR:PIRNR006621}.
FT DOMAIN 5..304
FT /note="DUS-like FMN-binding"
FT /evidence="ECO:0000259|Pfam:PF01207"
FT ACT_SITE 94
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006621-1"
SQ SEQUENCE 321 AA; 37364 MW; 8AB45CCB1B7E5BDA CRC64;
MKYYLAPMEG ITGYIYRTSY EKYFGNIDKY FTPFIVTNQS RSLKTKELRD VFPENNEGMN
IVPQILTNDS EGFINISRKL QQLGYNEVNL NLGCPAGTVV SKNRGSGFLA KREELDMFLD
EIFKIDDMKI SIKTRIGKDS PEEFYELIKI YNKYPLEELI IHPRTQKDFY GNKPNLEVFK
DGLSLSTNPV CYNGDIFTVD DHNKLIKAFP KVDTVMLGRG ILANPGLMNE IKNNTFIDKE
VLKDFHDEIL YKYIELFNED RNAIFRMKEL WGYMSCIFSD NKKYAKKIKK SQNLSDYNEA
VLSLFREQEI IQGAGLFNKP Y
//
