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Database: UniProt
Entry: A0A270PFG9_9PSED
LinkDB: A0A270PFG9_9PSED
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ID   A0A270PFG9_9PSED        Unreviewed;       331 AA.
AC   A0A270PFG9;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=dusA {ECO:0000256|HAMAP-Rule:MF_02041};
GN   ORFNames=CES87_17540 {ECO:0000313|EMBL:PAM82670.1};
OS   Pseudomonas sp. ERMR1:02.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1805930 {ECO:0000313|EMBL:PAM82670.1, ECO:0000313|Proteomes:UP000215719};
RN   [1] {ECO:0000313|EMBL:PAM82670.1, ECO:0000313|Proteomes:UP000215719}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ERMR1:02 {ECO:0000313|EMBL:PAM82670.1,
RC   ECO:0000313|Proteomes:UP000215719};
RA   Kumar R., Acharya V., Singh D., Kumar S.;
RT   "Pseudomonas sp. ERMR1:02, Genome sequencing and assembly.";
RL   Submitted (JUN-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. 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: 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:PAM82670.1}.
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DR   EMBL; NKJI01000009; PAM82670.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A270PFG9; -.
DR   OrthoDB; 9783413at2; -.
DR   Proteomes; UP000215719; Unassembled WGS sequence.
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   GO; GO:0102266; F:tRNA-dihydrouridine20a synthase activity; IEA:RHEA.
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   NCBIfam; TIGR00742; yjbN; 1.
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};
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          17..325
FT                   /note="DUS-like FMN-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01207"
FT   ACT_SITE        102
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02041,
FT                   ECO:0000256|PIRSR:PIRSR006621-1"
FT   BINDING         19..21
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02041"
FT   BINDING         72
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02041"
FT   BINDING         141
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02041"
FT   BINDING         173
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02041"
FT   BINDING         213..215
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02041"
FT   BINDING         235..236
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02041"
FT   SITE            99
FT                   /note="Interacts with tRNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02041"
FT   SITE            185
FT                   /note="Interacts with tRNA; defines subfamily-specific
FT                   binding signature"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02041"
FT   SITE            188
FT                   /note="Interacts with tRNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02041"
FT   SITE            301
FT                   /note="Interacts with tRNA; defines subfamily-specific
FT                   binding signature"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02041"
FT   SITE            304
FT                   /note="Interacts with tRNA; defines subfamily-specific
FT                   binding signature"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02041"
SQ   SEQUENCE   331 AA;  36433 MW;  2354C7DA789F3F6F CRC64;
     MPAPIATPAP LSRRFSVAPM MDWTDRHCRF FLRLLSKNAL LYTEMVTTGA LLNGDHERFL
     RHNEAEHPLA LQLGGSVPLD LAACARMAQE HGYDEVNLNV GCPSDRVQNN MIGACLMGHP
     QLVADCVKAM RDAVSIPVTV KHRIGINGRD SYEELCDFVG TVREAGCTSF TVHARIAILE
     GLSPKENRDI PPLRYDVAAR LKADFPELEI ILNGGIKTLE ACHEHLQTFD GVMLGREAYH
     NPYVMAEVDQ QLFGSTAPVI TRAEALSQLR PYIAAHIDAG GSMHHITRHV LGLGTGFPGA
     RKFRQLLSVD IHKAKEPLAL LDQAAQLLEG R
//
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