ID A0A222FM68_9GAMM Unreviewed; 354 AA.
AC A0A222FM68;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=CHH28_14250 {ECO:0000313|EMBL:ASP39762.1};
OS Bacterioplanes sanyensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Bacterioplanes.
OX NCBI_TaxID=1249553 {ECO:0000313|EMBL:ASP39762.1, ECO:0000313|Proteomes:UP000202440};
RN [1] {ECO:0000313|EMBL:ASP39762.1, ECO:0000313|Proteomes:UP000202440}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NV9 {ECO:0000313|EMBL:ASP39762.1,
RC ECO:0000313|Proteomes:UP000202440};
RA Rehman Z.U.;
RT "Annotated genome sequence of Bacterioplanes sanyensis isolated from Red
RT Sea.";
RL Submitted (JUL-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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP022530; ASP39762.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A222FM68; -.
DR KEGG; bsan:CHH28_14250; -.
DR OrthoDB; 9783413at2; -.
DR Proteomes; UP000202440; Chromosome.
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}; Reference proteome {ECO:0000313|Proteomes:UP000202440};
KW RNA-binding {ECO:0000256|HAMAP-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 29..334
FT /note="DUS-like FMN-binding"
FT /evidence="ECO:0000259|Pfam:PF01207"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 114
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02041,
FT ECO:0000256|PIRSR:PIRSR006621-1"
FT BINDING 31..33
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02041"
FT BINDING 84
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02041"
FT BINDING 153
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02041"
FT BINDING 185
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02041"
FT BINDING 225..227
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02041"
FT BINDING 247..248
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02041"
FT SITE 111
FT /note="Interacts with tRNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02041"
FT SITE 197
FT /note="Interacts with tRNA; defines subfamily-specific
FT binding signature"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02041"
FT SITE 200
FT /note="Interacts with tRNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02041"
FT SITE 317
FT /note="Interacts with tRNA; defines subfamily-specific
FT binding signature"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02041"
FT SITE 320
FT /note="Interacts with tRNA; defines subfamily-specific
FT binding signature"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02041"
SQ SEQUENCE 354 AA; 39608 MW; B0D83CA697EB38C3 CRC64;
MTAHSTASLT DTSSDKPSPL KAGARRFSTA PMMDWSDRHC RRFWRTLTRH SLLYSEMVTT
GALIHGDRQR FLQYSDEEHP IALQLGGSDP QQLAQCAAFA QQFGYDEVNL NVGCPSDRVQ
NNMIGACLMA HPELVRDGLQ AMRDACGIDV TVKHRIGIDD QDSYEHLRDF VGIVKDSGVT
TFIVHARTAI LQGLSPKENR EVPPLRYELV YRLKQEFPEL EIILNGGIET HAACETHLGH
LDGVMLGREA YHNPSVLMAA DHLYFGEPAP PDTSIEARKH AIRSLYPYIE QELSRGAVLH
HISRHMLGLF NGAKGARLFR RHLSEQAHKR TSGVDVMEQA LEFVQPAVFA EAAH
//
