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Database: UniProt
Entry: A0A1J0ACU8_9CYAN
LinkDB: A0A1J0ACU8_9CYAN
Original site: A0A1J0ACU8_9CYAN 
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
//
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