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Database: UniProt
Entry: A0A0W0R1G8_9GAMM
LinkDB: A0A0W0R1G8_9GAMM
Original site: A0A0W0R1G8_9GAMM 
ID   A0A0W0R1G8_9GAMM        Unreviewed;       345 AA.
AC   A0A0W0R1G8;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=tRNA-dihydrouridine(20/20a) synthase {ECO:0000256|HAMAP-Rule:MF_02041};
DE            EC=1.3.1.91 {ECO:0000256|HAMAP-Rule:MF_02041};
DE   AltName: Full=U20-specific dihydrouridine synthase {ECO:0000256|HAMAP-Rule:MF_02041};
DE            Short=U20-specific Dus {ECO:0000256|HAMAP-Rule:MF_02041};
DE   AltName: Full=tRNA-dihydrouridine synthase A {ECO:0000256|HAMAP-Rule:MF_02041};
GN   Name=dus_2 {ECO:0000313|EMBL:VEH85587.1};
GN   Synonyms=dusA {ECO:0000256|HAMAP-Rule:MF_02041};
GN   ORFNames=Lade_1711 {ECO:0000313|EMBL:KTC64904.1}, NCTC12735_01222
GN   {ECO:0000313|EMBL:VEH85587.1};
OS   Legionella adelaidensis.
OG   Plasmid 19 {ECO:0000313|EMBL:VEH85587.1,
OG   ECO:0000313|Proteomes:UP000281170}.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=45056 {ECO:0000313|EMBL:KTC64904.1, ECO:0000313|Proteomes:UP000054859};
RN   [1] {ECO:0000313|EMBL:KTC64904.1, ECO:0000313|Proteomes:UP000054859}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1762-AUS-E {ECO:0000313|EMBL:KTC64904.1,
RC   ECO:0000313|Proteomes:UP000054859};
RA   Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA   Pupko T., Shuman H.A., Segal G.;
RT   "Identification of large and diverse effector repertoires of 38 Legionella
RT   species.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:VEH85587.1, ECO:0000313|Proteomes:UP000281170}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC12735 {ECO:0000313|EMBL:VEH85587.1,
RC   ECO:0000313|Proteomes:UP000281170};
RC   PLASMID=19 {ECO:0000313|Proteomes:UP000281170};
RG   Pathogen Informatics;
RL   Submitted (DEC-2018) 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. Specifically modifies U20 and U20a in
CC       tRNAs. {ECO:0000256|HAMAP-Rule:MF_02041}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5,6-dihydrouridine(20) in tRNA + NAD(+) = H(+) + NADH +
CC         uridine(20) in tRNA; Xref=Rhea:RHEA:53340, Rhea:RHEA-COMP:13533,
CC         Rhea:RHEA-COMP:13534, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.91;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02041};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5,6-dihydrouridine(20) in tRNA + NADP(+) = H(+) + NADPH +
CC         uridine(20) in tRNA; Xref=Rhea:RHEA:53336, Rhea:RHEA-COMP:13533,
CC         Rhea:RHEA-COMP:13534, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.91;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02041};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5,6-dihydrouridine(20a) in tRNA + NAD(+) = H(+) + NADH +
CC         uridine(20a) in tRNA; Xref=Rhea:RHEA:53348, Rhea:RHEA-COMP:13535,
CC         Rhea:RHEA-COMP:13536, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02041};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5,6-dihydrouridine(20a) in tRNA + NADP(+) = H(+) + NADPH +
CC         uridine(20a) in tRNA; Xref=Rhea:RHEA:53344, Rhea:RHEA-COMP:13535,
CC         Rhea:RHEA-COMP:13536, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02041};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917,
CC         ECO:0000256|HAMAP-Rule:MF_02041, ECO:0000256|PIRNR:PIRNR006621};
CC   -!- SIMILARITY: Belongs to the Dus family. DusA subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_02041}.
CC   -!- SIMILARITY: Belongs to the dus family. {ECO:0000256|PIRNR:PIRNR006621}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_02041}.
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DR   EMBL; LNKA01000016; KTC64904.1; -; Genomic_DNA.
DR   EMBL; LR134428; VEH85587.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0W0R1G8; -.
DR   STRING; 45056.Lade_1711; -.
DR   KEGG; ladl:NCTC12735_01222; -.
DR   PATRIC; fig|45056.6.peg.1767; -.
DR   Proteomes; UP000054859; Unassembled WGS sequence.
DR   Proteomes; UP000281170; Plasmid 19.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0102264; F:tRNA-dihydrouridine20 synthase activity; IEA:UniProtKB-EC.
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   HAMAP; MF_02041; DusA_subfam; 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, ECO:0000256|HAMAP-
KW   Rule:MF_02041};
KW   FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|HAMAP-Rule:MF_02041};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_02041};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_02041}; Plasmid {ECO:0000313|EMBL:VEH85587.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054859};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_02041};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_02041}; tRNA-binding {ECO:0000256|HAMAP-Rule:MF_02041}.
FT   DOMAIN          26..326
FT                   /note="DUS-like FMN-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01207"
FT   ACT_SITE        110
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02041,
FT                   ECO:0000256|PIRSR:PIRSR006621-1"
FT   BINDING         80
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02041"
FT   BINDING         149
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02041"
FT   BINDING         181
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02041"
FT   BINDING         243..244
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02041"
FT   SITE            107
FT                   /note="Interacts with tRNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02041"
FT   SITE            193
FT                   /note="Interacts with tRNA; defines subfamily-specific
FT                   binding signature"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02041"
FT   SITE            196
FT                   /note="Interacts with tRNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02041"
SQ   SEQUENCE   345 AA;  38654 MW;  F8ED4BE40970BD31 CRC64;
     MTYNLGLYFI KNLIMTYSSL FSQIAIAPMI DWTNTHFRIF MRLLAPQALL YTDMQTPGAI
     FNNPGKALYY QPVEHPLALQ LGGSVVSELV ECAKKAEKLG FKEINLNLGC PSDRVLAGKF
     GACLMSEPNH VAECIKALKE SVSLPVTAKT RIGIDNQDSY SFFSNFVFHL VEAGCDKLIV
     HARKAWLKGL SPKQNRTIPP LHYDYVYAIK KDLPHVPVVI NGNIKTIDDI RDHLEHVDGV
     MLGRLVCDNP YAIAEIHKAI FPEDRMLTRA EVVSLYVAYI REALEKAAPL SILLKPLFNL
     MHGLANSKAW KAELLRIQQQ KDTTSLTQLP VLIKNLTQAK VSIPN
//
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