ID A0A1J0ACU8_9CYAN Unreviewed; 345 AA.
AC A0A1J0ACU8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=tRNA-dihydrouridine synthase {ECO:0000256|PIRNR:PIRNR006621};
DE EC=1.3.1.- {ECO:0000256|PIRNR:PIRNR006621};
GN Name=dusB {ECO:0000313|EMBL:APB33739.1};
GN ORFNames=GlitD10_1418 {ECO:0000313|EMBL:APB33739.1};
OS Gloeomargarita lithophora Alchichica-D10.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Gloeomargaritales;
OC Gloeomargaritaceae; Gloeomargarita.
OX NCBI_TaxID=1188229 {ECO:0000313|EMBL:APB33739.1, ECO:0000313|Proteomes:UP000180235};
RN [1] {ECO:0000313|EMBL:APB33739.1, ECO:0000313|Proteomes:UP000180235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D10 {ECO:0000313|EMBL:APB33739.1,
RC ECO:0000313|Proteomes:UP000180235};
RA Moreira D., Tavera R., Benzerara K., Skouri-Panet F., Couradeau E.,
RA Gerard E., Loussert C., Novelo E., Zivanovic Y., Lopez-Garcia P.;
RT "Description of Gloeomargarita lithophora gen. nov., sp. nov., a thylakoid-
RT bearing basal-branching cyanobacterium with intracellular carbonates, and
RT proposal for Gloeomargaritales ord. nov.";
RL Submitted (OCT-2016) 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|ARBA:ARBA00001917,
CC ECO:0000256|PIRNR:PIRNR006621};
CC -!- SIMILARITY: Belongs to the dus family. {ECO:0000256|PIRNR:PIRNR006621}.
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DR EMBL; CP017675; APB33739.1; -; Genomic_DNA.
DR RefSeq; WP_071454279.1; NZ_CP017675.1.
DR AlphaFoldDB; A0A1J0ACU8; -.
DR STRING; 1188229.GlitD10_1418; -.
DR Proteomes; UP000180235; Chromosome.
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 InterPro; IPR018517; tRNA_hU_synthase_CS.
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.
DR PROSITE; PS01136; UPF0034; 1.
PE 3: Inferred from homology;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|PIRNR:PIRNR006621};
KW FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|PIRNR:PIRNR006621};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR006621};
KW Reference proteome {ECO:0000313|Proteomes:UP000180235};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694,
KW ECO:0000256|PIRNR:PIRNR006621}.
FT DOMAIN 29..330
FT /note="DUS-like FMN-binding"
FT /evidence="ECO:0000259|Pfam:PF01207"
FT ACT_SITE 115
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006621-1"
SQ SEQUENCE 345 AA; 37902 MW; 4E6E9EE61260F8F1 CRC64;
MSGLKMALPA RMSAPLRIGS LVVQSRVLQS PLSGVTDLVF RRLVRRFAPH SLLYTEMVSA
TGLHYMRQLP RLMELDPGER PVGIQLFDCR PDFLAEAAVR AVGEGADLVD INMGCPVNKI
TKNGGGSSLL RQPELAAAIV RSVVRAVPVP VTVKTRLGWN DQEINILEFA QRMEQAGAQL
LTVHGRTRAQ GYQGSARWEW IRRVKGAVRI PVIANGDIFS VQAALDCLEL TGADGVMCSR
GTLGYPFLVG EIDHFFRTGE VLAPPTPAQR LQCAREHLLA LWEYKGESGL RQARKHLAWY
AREFAGAAQL RQAVAQFQTL AEGLALLDGA LERLAYVPQE WPSCA
//