ID A0A198FIA1_9GAMM Unreviewed; 310 AA.
AC A0A198FIA1;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=M983_2677 {ECO:0000313|EMBL:OAT24164.1};
OS Proteus myxofaciens ATCC 19692.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Proteus.
OX NCBI_TaxID=1354337 {ECO:0000313|EMBL:OAT24164.1, ECO:0000313|Proteomes:UP000094023};
RN [1] {ECO:0000313|EMBL:OAT24164.1, ECO:0000313|Proteomes:UP000094023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19692 {ECO:0000313|EMBL:OAT24164.1,
RC ECO:0000313|Proteomes:UP000094023};
RA Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.;
RT "ATOL: Assembling a taxonomically balanced genome-scale reconstruction of
RT the evolutionary history of the Enterobacteriaceae.";
RL Submitted (APR-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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAT24164.1}.
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DR EMBL; LXEN01000132; OAT24164.1; -; Genomic_DNA.
DR RefSeq; WP_066751934.1; NZ_LXEN01000132.1.
DR AlphaFoldDB; A0A198FIA1; -.
DR STRING; 1354337.M983_2677; -.
DR PATRIC; fig|1354337.4.peg.2744; -.
DR OrthoDB; 9764501at2; -.
DR Proteomes; UP000094023; 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}; Reference proteome {ECO:0000313|Proteomes:UP000094023};
KW RNA-binding {ECO:0000256|HAMAP-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 4..288
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 200..202
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02043"
FT BINDING 224..225
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 272
FT /note="Interacts with tRNA; defines subfamily-specific
FT binding signature"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02043"
FT SITE 274
FT /note="Interacts with tRNA; defines subfamily-specific
FT binding signature"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02043"
FT SITE 279
FT /note="Interacts with tRNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02043"
FT SITE 295
FT /note="Interacts with tRNA; defines subfamily-specific
FT binding signature"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02043"
SQ SEQUENCE 310 AA; 34579 MW; 0A1D3F74A1A70E3A CRC64;
MRVLLAPMEG VLDPLVRDLL TSINHYDLCI TEFIRVVDSL LPPKAFYRLC PELQTQSRTQ
SGTLVRIQLL GQNPQWLAEN AFRAVSLGSF GVDLNCGCPS KTVNGNGGGA SLLKQPEMIY
QATKAMRSAV PSDLPVSVKV RLGWDSTEKC YEIADAVAQG GATEITIHGR TKEDGYRAEK
INWQAIGDIR KKLAIPVIAN GEIWSREDAL SCLALTGCDA VMIGRGAMHT PNLSRVVKGI
ENRMSWNDVI LLLKRYIRLE KKDDTTYYHA SRIKQWLGYL RKEYQEAEIL FSQIRTLKTS
PEIAQVIDAL
//
