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Database: UniProt
Entry: U4KQ42_9MOLU
LinkDB: U4KQ42_9MOLU
Original site: U4KQ42_9MOLU 
ID   U4KQ42_9MOLU            Unreviewed;       327 AA.
AC   U4KQ42;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=tRNA-dihydrouridine synthase {ECO:0000256|PIRNR:PIRNR006621};
DE            EC=1.3.1.- {ECO:0000256|PIRNR:PIRNR006621};
GN   Name=duS {ECO:0000313|EMBL:CCV66647.1};
GN   ORFNames=BN85316260 {ECO:0000313|EMBL:CCV66647.1};
OS   Paracholeplasma brassicae.
OC   Bacteria; Mycoplasmatota; Mollicutes; Acholeplasmatales;
OC   Acholeplasmataceae; Paracholeplasma.
OX   NCBI_TaxID=61635 {ECO:0000313|EMBL:CCV66647.1, ECO:0000313|Proteomes:UP000032737};
RN   [1] {ECO:0000313|EMBL:CCV66647.1, ECO:0000313|Proteomes:UP000032737}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0502 {ECO:0000313|Proteomes:UP000032737};
RX   PubMed=24158107; DOI=10.1159/000354322;
RA   Kube M., Siewert C., Migdoll A.M., Duduk B., Holz S., Rabus R.,
RA   Seemuller E., Mitrovic J., Muller I., Buttner C., Reinhardt R.;
RT   "Analysis of the Complete Genomes of Acholeplasma brassicae , A. palmae and
RT   A. laidlawii and Their Comparison to the Obligate Parasites from '
RT   Candidatus Phytoplasma'.";
RL   J. Mol. Microbiol. Biotechnol. 24:19-36(2013).
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; FO681348; CCV66647.1; -; Genomic_DNA.
DR   AlphaFoldDB; U4KQ42; -.
DR   STRING; 61635.BN85316260; -.
DR   KEGG; abra:BN85316260; -.
DR   HOGENOM; CLU_013299_0_3_14; -.
DR   Proteomes; UP000032737; Chromosome Acholeplasma brassicae.
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:UP000032737};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694,
KW   ECO:0000256|PIRNR:PIRNR006621}.
FT   DOMAIN          16..321
FT                   /note="DUS-like FMN-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01207"
FT   ACT_SITE        103
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006621-1"
SQ   SEQUENCE   327 AA;  36138 MW;  7C9E01ECCF5610AC CRC64;
     MAFKIGTIEI DSNVVLAPMA GVSNAAFRVI SRELGAGVVF AEMVSDKGLM YDNEKTKDLL
     KSLSSEHPYA QQIFGSDKES MVKAAIYIDQ HTDCDIIDIN MGCPVPKVAA RAQAGAALLK
     DPDKIYEIVK AIQEAVTKPV TVKIRTGWDD ASINAVEVAK KIEQAGAKAI TVHGRTRAQM
     YSGRANLDVI KAVKEAVSIP VIANGDVTNG KEARYVLDYT KADAVMVGRA ALGNPWVFKE
     IDRYLKYQEE TPKPSYKEIK DMILRHADIL MELKGEHLAM LQMRGQSTWY FKGLPHASHT
     KSLLSKVSDY DTFRSIVDDY FNLIMTS
//
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