ID S0EYJ8_CHTCT Unreviewed; 336 AA.
AC S0EYJ8;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=tRNA-dihydrouridine synthase {ECO:0000256|PIRNR:PIRNR006621};
DE EC=1.3.1.- {ECO:0000256|PIRNR:PIRNR006621};
GN ORFNames=CCALI_01154 {ECO:0000313|EMBL:CCW34973.1};
OS Chthonomonas calidirosea (strain DSM 23976 / ICMP 18418 / T49).
OC Bacteria; Armatimonadota; Chthonomonadetes; Chthonomonadales;
OC Chthonomonadaceae; Chthonomonas.
OX NCBI_TaxID=1303518 {ECO:0000313|EMBL:CCW34973.1, ECO:0000313|Proteomes:UP000014227};
RN [1] {ECO:0000313|Proteomes:UP000014227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23976 / ICMP 18418 / T49
RC {ECO:0000313|Proteomes:UP000014227};
RA Lee K.C.Y., Morgan X.C., Dunfield P.F., Tamas I., Houghton K.M.,
RA Vyssotski M., Ryan J.L.J., Lagutin K., McDonald I.R., Stott M.B.;
RT "Genome sequence of Chthonomonas calidirosea, the first sequenced genome
RT from the Armatimonadetes phylum (formally candidate division OP10).";
RL Submitted (MAR-2013) 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}.
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DR EMBL; HF951689; CCW34973.1; -; Genomic_DNA.
DR RefSeq; WP_016482518.1; NC_021487.1.
DR AlphaFoldDB; S0EYJ8; -.
DR STRING; 454171.CP488_00004; -.
DR KEGG; ccz:CCALI_01154; -.
DR PATRIC; fig|1303518.3.peg.1176; -.
DR eggNOG; COG0042; Bacteria.
DR HOGENOM; CLU_013299_0_3_0; -.
DR InParanoid; S0EYJ8; -.
DR Proteomes; UP000014227; 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 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:UP000014227};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW tRNA processing {ECO:0000256|PIRNR:PIRNR006621}.
FT DOMAIN 21..325
FT /note="DUS-like FMN-binding"
FT /evidence="ECO:0000259|Pfam:PF01207"
FT ACT_SITE 109
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006621-1"
SQ SEQUENCE 336 AA; 36474 MW; 310F3D9213CC09C0 CRC64;
MQQRGYEGFR VGNLWISPPV ILAPMADVTN GAFRRLAKRI GGPGLVVTEF ISTTALHYGS
AKTLTMFDIT PDQRPVAVQI FGADPAIMAE AARIAVDMGA DILDINMGCW VPKVCKTGAG
AALIRDPDTA CRVVEAVVKA VSVPVTVKTR PGWQYGDFAT AKLAKRFEEL GIQALTLHAR
FAVQGHEGAV DWALIRQMKA LLSIPVIGNG DVNSPQAAAR LLEETGCDGV MVGRAAIGNP
WILRDIAHFL RTGELLPPPT LQERAEAALS HLRDLAQSMG EGPAVRHLRG QLPLYFRGFP
YASRFRERIS HANTIEEVQR LIEELFHAEL TACVPA
//
