ID A0A172YLZ8_9GAMM Unreviewed; 311 AA.
AC A0A172YLZ8;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=A3K93_02390 {ECO:0000313|EMBL:ANF81150.1};
OS Acinetobacter sp. NCu2D-2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1608473 {ECO:0000313|EMBL:ANF81150.1, ECO:0000313|Proteomes:UP000186584};
RN [1] {ECO:0000313|Proteomes:UP000186584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCu2D-2 {ECO:0000313|Proteomes:UP000186584};
RA Wilharm G.;
RT "Acinetobacter strain NCu2D-2 is the representative of a novel species.";
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02043}.
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DR EMBL; CP015594; ANF81150.1; -; Genomic_DNA.
DR RefSeq; WP_067728592.1; NZ_CP015594.1.
DR AlphaFoldDB; A0A172YLZ8; -.
DR STRING; 1608473.A3K93_02390; -.
DR KEGG; aciu:A3K93_02390; -.
DR Proteomes; UP000186584; Chromosome.
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}; 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 5..271
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 271
FT /note="Interacts with tRNA; defines subfamily-specific
FT binding signature"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02043"
FT SITE 273
FT /note="Interacts with tRNA; defines subfamily-specific
FT binding signature"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02043"
FT SITE 294
FT /note="Interacts with tRNA; defines subfamily-specific
FT binding signature"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02043"
SQ SEQUENCE 311 AA; 34742 MW; 1F616D87BF7F9E4A CRC64;
MKLVLAPMEG LTDPIMRDVL TSVGSFDWCV TEFIRVTDSI LPDHVYHSYC PELLNDGKTA
SGTPVHVQFL GNNPDMLAAN AVKVAEMGAP TIDMNFGCPA KTVNRHRGGS VLLDEPEVVY
QLIKAVRDAV PSHIPVSAKM RLGYMDRDFM MENAHAIEDA GAAWVTVHAR TKADGYTPPA
FWDQLAPIRE TLKINVIANG EIWNNADAKQ CQIESGCQDL MIGRGAVTTP DITQCIRANT
DQALLTWNDL LGLQIRFLNG SYKKEMNMVG RYKQWLGMMS KHYPEAKMLW DEVKRVKPLD
EIIEKLQSSK H
//
