ID A0A1H6T0Z2_9PSED Unreviewed; 319 AA.
AC A0A1H6T0Z2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=tRNA-dihydrouridine(16) synthase {ECO:0000256|HAMAP-Rule:MF_02043};
DE EC=1.3.1.- {ECO:0000256|HAMAP-Rule:MF_02043};
DE AltName: Full=U16-specific dihydrouridine synthase {ECO:0000256|HAMAP-Rule:MF_02043};
DE Short=U16-specific Dus {ECO:0000256|HAMAP-Rule:MF_02043};
DE AltName: Full=tRNA-dihydrouridine synthase C {ECO:0000256|HAMAP-Rule:MF_02043};
GN Name=dusC {ECO:0000256|HAMAP-Rule:MF_02043};
GN ORFNames=SAMN03159495_1511 {ECO:0000313|EMBL:SEI73789.1};
OS Pseudomonas sp. NFR16.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1566248 {ECO:0000313|EMBL:SEI73789.1, ECO:0000313|Proteomes:UP000199219};
RN [1] {ECO:0000313|EMBL:SEI73789.1, ECO:0000313|Proteomes:UP000199219}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NFR16 {ECO:0000313|EMBL:SEI73789.1,
RC ECO:0000313|Proteomes:UP000199219};
RA de Groot N.N.;
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. Specifically modifies U16 in tRNAs.
CC {ECO:0000256|HAMAP-Rule:MF_02043}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouridine(16) in tRNA + NAD(+) = H(+) + NADH +
CC uridine(16) in tRNA; Xref=Rhea:RHEA:53380, Rhea:RHEA-COMP:13543,
CC Rhea:RHEA-COMP:13544, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02043};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouridine(16) in tRNA + NADP(+) = H(+) + NADPH +
CC uridine(16) in tRNA; Xref=Rhea:RHEA:53376, Rhea:RHEA-COMP:13543,
CC Rhea:RHEA-COMP:13544, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02043};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917,
CC ECO:0000256|HAMAP-Rule:MF_02043, ECO:0000256|PIRNR:PIRNR006621};
CC -!- SIMILARITY: Belongs to the Dus family. DusC subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_02043}.
CC -!- SIMILARITY: Belongs to the dus family. {ECO:0000256|PIRNR:PIRNR006621}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02043}.
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DR EMBL; FNYJ01000001; SEI73789.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6T0Z2; -.
DR STRING; 1566248.SAMN03159495_1511; -.
DR OrthoDB; 5289281at2; -.
DR Proteomes; UP000199219; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0010181; F:FMN binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0102262; F:tRNA-dihydrouridine16 synthase activity; IEA:RHEA.
DR CDD; cd02801; DUS_like_FMN; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 1.20.225.30; Dihydrouridine synthase, C-terminal recognition domain; 1.
DR HAMAP; MF_02043; DusC_subfam; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR035587; DUS-like_FMN-bd.
DR InterPro; IPR001269; DUS_fam.
DR InterPro; IPR032886; DusC.
DR InterPro; IPR042270; DusC_C.
DR InterPro; IPR018517; tRNA_hU_synthase_CS.
DR PANTHER; PTHR11082; TRNA-DIHYDROURIDINE SYNTHASE; 1.
DR PANTHER; PTHR11082:SF26; TRNA-DIHYDROURIDINE(16) SYNTHASE; 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, ECO:0000256|HAMAP-
KW Rule:MF_02043};
KW FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|HAMAP-Rule:MF_02043};
KW NADP {ECO:0000256|HAMAP-Rule:MF_02043};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_02043};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_02043};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_02043}; tRNA-binding {ECO:0000256|HAMAP-Rule:MF_02043}.
FT DOMAIN 5..252
FT /note="DUS-like FMN-binding"
FT /evidence="ECO:0000259|Pfam:PF01207"
FT ACT_SITE 98
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02043,
FT ECO:0000256|PIRSR:PIRSR006621-1"
FT BINDING 68
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02043"
FT BINDING 139
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02043"
FT BINDING 199..201
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02043"
FT BINDING 223..224
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02043"
FT SITE 35
FT /note="Interacts with tRNA; defines subfamily-specific
FT binding signature"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02043"
FT SITE 95
FT /note="Interacts with tRNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02043"
FT SITE 176
FT /note="Interacts with tRNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02043"
FT SITE 276
FT /note="Interacts with tRNA; defines subfamily-specific
FT binding signature"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02043"
FT SITE 278
FT /note="Interacts with tRNA; defines subfamily-specific
FT binding signature"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02043"
FT SITE 299
FT /note="Interacts with tRNA; defines subfamily-specific
FT binding signature"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02043"
SQ SEQUENCE 319 AA; 35309 MW; C58B7E4A0B7532FE CRC64;
MQIALAPMEG LVDDILRDVL TQVGGIDWCV TEFIRVTERL LPAHYFHKFA SELLTDAKTR
AGVPLRVQLL GSDPVCLAEN AAFAAELGAP VIDLNFGCPA KTVNKSRGGA VLLKEPELLH
SILSHVRRAV PAHIPVTAKM RLGYDSTEPA LDCARALEAG GAEHIVVHAR TKVDGYKPPA
HWEWIGKIQD VVGIPIIANG EIWTVDDWRR CREICGARDI MIGRGLVARP DLGRQIAAAQ
AGRDVVAMTW QELQPLLREF WLQAMAKMTR IQAPGRLKQW VVLLTKSYPE AVVLFDALRR
ETNCERISRM LGIVEQEVA
//
