ID A0A178INC0_9BACT Unreviewed; 358 AA.
AC A0A178INC0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=tRNA-dihydrouridine synthase {ECO:0000256|PIRNR:PIRNR006621};
DE EC=1.3.1.- {ECO:0000256|PIRNR:PIRNR006621};
GN ORFNames=AW736_06075 {ECO:0000313|EMBL:OAM90817.1};
OS Opitutaceae bacterium TSB47.
OC Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae.
OX NCBI_TaxID=1184151 {ECO:0000313|EMBL:OAM90817.1, ECO:0000313|Proteomes:UP000078486};
RN [1] {ECO:0000313|EMBL:OAM90817.1, ECO:0000313|Proteomes:UP000078486}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSB47 {ECO:0000313|EMBL:OAM90817.1,
RC ECO:0000313|Proteomes:UP000078486};
RA Wang Y., Shi Y., Qiu Z., Liu S., Yang H.;
RT "High potential of lignocellulose degradation of a new Verrucomicrobia
RT species.";
RL Submitted (JAN-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|PIRNR:PIRNR006621};
CC -!- SIMILARITY: Belongs to the dus family. {ECO:0000256|PIRNR:PIRNR006621}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAM90817.1}.
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DR EMBL; LRRQ01000047; OAM90817.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178INC0; -.
DR STRING; 1184151.AW736_06075; -.
DR Proteomes; UP000078486; 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 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:UP000078486};
KW tRNA processing {ECO:0000256|PIRNR:PIRNR006621}.
FT DOMAIN 18..243
FT /note="DUS-like FMN-binding"
FT /evidence="ECO:0000259|Pfam:PF01207"
FT ACT_SITE 105
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006621-1"
SQ SEQUENCE 358 AA; 39081 MW; E02C7FA1B7B5D38B CRC64;
MSAPLPAPTI PGQPLTALAP MQDVTDLAFM RVAAHYGAPD YFVTEFFRVH SQSRPEKHIL
RAIDENTTGR PVFAQLIGED IAHLARTIDE LLRHPVAGID LNLGCPAPKV YKKNVGGGLL
REPDKISKIL AAIRAAVPGL FTVKMRIGFE DTGHYDAILD LVNEHRIDLL AVHGRTVREL
YRGEVHYDAI ARAVARVRCP VMANGNITSA AKAARVLAET RAAGVMIGRH AIRNPWIFRQ
CREHFAGRPV TPVTFADVRD YIGHLFNATR QPGIPENAHV SRMKKFLNFT GQSVDPDGAF
LRDMRRATTA AGLFAVCDRH LLAEPAREFA LEPYPGVIAR PNCEMPDSAA AASGIGGG
//
