ID E4PFT4_MARAH Unreviewed; 344 AA.
AC E4PFT4;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
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 OrderedLocusNames=HP15_2240 {ECO:0000313|EMBL:ADP98004.1};
OS Marinobacter adhaerens (strain DSM 23420 / HP15).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Marinobacteraceae; Marinobacter.
OX NCBI_TaxID=225937 {ECO:0000313|EMBL:ADP98004.1, ECO:0000313|Proteomes:UP000007077};
RN [1] {ECO:0000313|EMBL:ADP98004.1, ECO:0000313|Proteomes:UP000007077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23420 / HP15 {ECO:0000313|Proteomes:UP000007077};
RX PubMed=21304739;
RA Gardes A., Kaeppel E., Shehzad A., Seebah S., Teeling H., Yarza P.,
RA Glockner F.O., Grossart H.P., Ullrich M.S.;
RT "Complete genome sequence of Marinobacter adhaerens type strain (HP15), a
RT diatom-interacting marine microorganism.";
RL Stand. Genomic Sci. 3:97-107(2010).
RN [2] {ECO:0000313|Proteomes:UP000007077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23420 / HP15 {ECO:0000313|Proteomes:UP000007077};
RA Gaerdes A.A.M., Kaeppel E., Shezad A., Seebah S., Teeling H., Yarza P.,
RA Gloeckner F.O., Ullrich M.S.;
RT "Complete genome sequence of Marinobacter adhaerens type strain (HP15).";
RL Submitted (FEB-2010) 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}.
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DR EMBL; CP001978; ADP98004.1; -; Genomic_DNA.
DR RefSeq; WP_014577561.1; NC_017506.1.
DR AlphaFoldDB; E4PFT4; -.
DR STRING; 225937.HP15_2240; -.
DR KEGG; mad:HP15_2240; -.
DR PATRIC; fig|225937.3.peg.2262; -.
DR eggNOG; COG0042; Bacteria.
DR HOGENOM; CLU_013299_2_1_6; -.
DR Proteomes; UP000007077; 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};
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 22..331
FT /note="DUS-like FMN-binding"
FT /evidence="ECO:0000259|Pfam:PF01207"
FT ACT_SITE 107
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02041,
FT ECO:0000256|PIRSR:PIRSR006621-1"
FT BINDING 24..26
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02041"
FT BINDING 77
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02041"
FT BINDING 146
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02041"
FT BINDING 178
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02041"
FT BINDING 218..220
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02041"
FT BINDING 240..241
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02041"
FT SITE 104
FT /note="Interacts with tRNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02041"
FT SITE 190
FT /note="Interacts with tRNA; defines subfamily-specific
FT binding signature"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02041"
FT SITE 193
FT /note="Interacts with tRNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02041"
FT SITE 306
FT /note="Interacts with tRNA; defines subfamily-specific
FT binding signature"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02041"
FT SITE 309
FT /note="Interacts with tRNA; defines subfamily-specific
FT binding signature"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02041"
SQ SEQUENCE 344 AA; 38465 MW; 0C1B5CFA6583114A CRC64;
MSGIPSQETM LHNSGPSRRF CVAPMMDWTT SHYRYLARQL SRHTLLYTEM VTTGALIHGD
TARFLRHDEA EYPLALQLGG SDAGELAHCA RLAQQYGFDE VNLNVGCPSD RVQNNMIGAC
LMGHPDKVAE GVRAMIEATD LPVTVKHRIG IDGRESWDDL CEFVEKVSEA GCRTFIVHAR
IAILEGLSPK ENREVPPLKY DWVYRLKAKY PHLEIIINGG IKTFGECHEH LRHTDGVMLG
REAYHNPWLL AGVDPEFFGQ AAPVETRHQA LRAMLPFIGS ELERGVFLTH MSRHLLGLFH
GQPGGRQFRR YISENAHKSG AGLEVIETAL EKVREPAAPE IAEA
//
