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Database: UniProt
Entry: U1FGM5_9ACTN
LinkDB: U1FGM5_9ACTN
Original site: U1FGM5_9ACTN 
ID   U1FGM5_9ACTN            Unreviewed;       355 AA.
AC   U1FGM5;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=tRNA-dihydrouridine synthase {ECO:0000256|PIRNR:PIRNR006621};
DE            EC=1.3.1.- {ECO:0000256|PIRNR:PIRNR006621};
GN   ORFNames=H641_00507 {ECO:0000313|EMBL:ERF58431.1}, L860_05435
GN   {ECO:0000313|EMBL:OCT43196.1}, L860_10945
GN   {ECO:0000313|EMBL:OCT42306.1};
OS   Cutibacterium granulosum DSM 20700.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Cutibacterium.
OX   NCBI_TaxID=1160719 {ECO:0000313|EMBL:ERF58431.1, ECO:0000313|Proteomes:UP000016307};
RN   [1] {ECO:0000313|EMBL:ERF58431.1, ECO:0000313|Proteomes:UP000016307}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20700 {ECO:0000313|EMBL:ERF58431.1,
RC   ECO:0000313|Proteomes:UP000016307};
RX   PubMed=24053623; DOI=10.1186/1471-2164-14-640;
RA   Mak T.N., Schmid M., Brzuszkiewicz E., Zeng G., Meyer R., Sfanos K.S.,
RA   Brinkmann V., Meyer T.F., Bruggemann H.;
RT   "Comparative genomics reveals distinct host-interacting traits of three
RT   major human-associated propionibacteria.";
RL   BMC Genomics 14:640-640(2013).
RN   [2] {ECO:0000313|EMBL:OCT42306.1, ECO:0000313|Proteomes:UP000094467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20700 {ECO:0000313|EMBL:OCT42306.1,
RC   ECO:0000313|Proteomes:UP000094467};
RA   Jahns A.C., Eilers H., Alexeyev O.A.;
RL   Submitted (MAY-2014) 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|ARBA:ARBA00002790,
CC       ECO:0000256|PIRNR:PIRNR006621}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5,6-dihydrouridine in tRNA + NAD(+) = a uridine in tRNA +
CC         H(+) + NADH; Xref=Rhea:RHEA:54452, Rhea:RHEA-COMP:13339, Rhea:RHEA-
CC         COMP:13887, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:65315, ChEBI:CHEBI:74443;
CC         Evidence={ECO:0000256|ARBA:ARBA00001387};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5,6-dihydrouridine in tRNA + NADP(+) = a uridine in tRNA +
CC         H(+) + NADPH; Xref=Rhea:RHEA:23624, Rhea:RHEA-COMP:13339, Rhea:RHEA-
CC         COMP:13887, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:65315, ChEBI:CHEBI:74443;
CC         Evidence={ECO:0000256|ARBA:ARBA00001183};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={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:ERF58431.1}.
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DR   EMBL; AOSS01000017; ERF58431.1; -; Genomic_DNA.
DR   EMBL; JNBU01000029; OCT42306.1; -; Genomic_DNA.
DR   EMBL; JNBU01000003; OCT43196.1; -; Genomic_DNA.
DR   AlphaFoldDB; U1FGM5; -.
DR   PATRIC; fig|1160719.4.peg.94; -.
DR   Proteomes; UP000016307; Unassembled WGS sequence.
DR   Proteomes; UP000094467; 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; 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; IPR004652; DusB-like.
DR   InterPro; IPR024036; tRNA-dHydroUridine_Synthase_C.
DR   NCBIfam; TIGR00737; nifR3_yhdG; 1.
DR   PANTHER; PTHR45846; TRNA-DIHYDROURIDINE(47) SYNTHASE [NAD(P)(+)]-LIKE; 1.
DR   PANTHER; PTHR45846:SF1; TRNA-DIHYDROURIDINE(47) SYNTHASE [NAD(P)(+)]-LIKE; 1.
DR   Pfam; PF01207; Dus; 1.
DR   PIRSF; PIRSF006621; Dus; 1.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
PE   3: Inferred from homology;
KW   Flavoprotein {ECO:0000256|PIRNR:PIRNR006621};
KW   FMN {ECO:0000256|PIRNR:PIRNR006621};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR006621};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016307};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   tRNA processing {ECO:0000256|PIRNR:PIRNR006621}.
FT   DOMAIN          1..300
FT                   /note="DUS-like FMN-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01207"
FT   ACT_SITE        85
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006621-1"
SQ   SEQUENCE   355 AA;  38740 MW;  A602CD087BBD5DF1 CRC64;
     MAGVTNAAFR QLCAEQGAGL YVCEMITSRG LVYGDHKTKD MLAFADNEKI RSVQLYGVDP
     QMMADATRIL CTEYHVDHVD LNFGCPVPKV TRKGGGGVLP WKRDRFRSVV AAVVQAADEF
     DVPVSVKTRI GIDDDHVTFI DSAKAAEDAG AAAVCLHARS VAEAYSGHSH WQAIAELVSA
     VNIPVIGNGD IWEARDAVDM VEQTGCAGVE VGRGCLGRPW LFRDLADAFC GCQTQTLPTL
     GEVCEMVRRH AELLVKYQGM HGLVDMRKHM AWYFKGFPVG GETRHALGKI SNFDELDELL
     TSLDHDAPFP VKELGKARGR QGTPRRKVVM PMGWLDSRTL DDHDLSEAEL GISGG
//
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