ID A0A058ZQM0_9RHOB Unreviewed; 299 AA.
AC A0A058ZQM0;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=tRNA-dihydrouridine synthase {ECO:0000256|PIRNR:PIRNR006621};
DE EC=1.3.1.- {ECO:0000256|PIRNR:PIRNR006621};
GN ORFNames=ATO10_03770 {ECO:0000313|EMBL:KCV83848.1};
OS Actibacterium atlanticum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Actibacterium.
OX NCBI_TaxID=1461693 {ECO:0000313|EMBL:KCV83848.1, ECO:0000313|Proteomes:UP000024836};
RN [1] {ECO:0000313|EMBL:KCV83848.1, ECO:0000313|Proteomes:UP000024836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22II-S11-Z10 {ECO:0000313|Proteomes:UP000024836};
RA Lai Q., Li G., Shao Z.;
RT "Shimia sp. 22II-S11-Z10 Genome Sequencing.";
RL Submitted (APR-2013) 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}.
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:KCV83848.1}.
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DR EMBL; AQQY01000001; KCV83848.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A058ZQM0; -.
DR STRING; 1461693.ATO10_03770; -.
DR PATRIC; fig|1461693.3.peg.775; -.
DR eggNOG; COG0042; Bacteria.
DR Proteomes; UP000024836; Unassembled WGS sequence.
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; 1.20.120.1460; -; 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; IPR004653; DusA.
DR InterPro; IPR018517; tRNA_hU_synthase_CS.
DR PANTHER; PTHR42907; FMN-LINKED OXIDOREDUCTASES SUPERFAMILY PROTEIN; 1.
DR PANTHER; PTHR42907:SF1; FMN-LINKED OXIDOREDUCTASES SUPERFAMILY PROTEIN; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR006621};
KW Reference proteome {ECO:0000313|Proteomes:UP000024836};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694,
KW ECO:0000256|PIRNR:PIRNR006621}.
FT DOMAIN 2..291
FT /note="DUS-like FMN-binding"
FT /evidence="ECO:0000259|Pfam:PF01207"
FT ACT_SITE 68
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006621-1"
SQ SEQUENCE 299 AA; 32612 MW; F9BD8B7F6506601C CRC64;
MSARTLLYTE MVTAPALVRG GALHLLDYNA EEHPVAVQLG GSDPAELAEA TALCAAHGYD
EINLNVGCPS DRVQSGCFGA VLMERPALVA ECVSAMIRAS NVEVTVKCRI GVDKQDPETV
LPDFIARMRD AGVTRLAVHA RKAWLQGLSP KENRDIPPLD YDLVLRMKQQ FPDLHISVNG
GIESLEQAKG FLKDGLDGVM IGRAAYHTPC DILLRADHEI FGEAGVKTAH DVVQEMRPYI
ARHVEQGGKL AQVTRHMLGM FTGRPGARHW RRVLSEHGHR AGAGLEVLDE ALSHIPEKD
//
