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Database: UniProt
Entry: A0A0F4QHF7_9GAMM
LinkDB: A0A0F4QHF7_9GAMM
Original site: A0A0F4QHF7_9GAMM 
ID   A0A0F4QHF7_9GAMM        Unreviewed;       315 AA.
AC   A0A0F4QHF7;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
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=TW77_18110 {ECO:0000313|EMBL:KJZ06720.1};
OS   Pseudoalteromonas rubra.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=43658 {ECO:0000313|EMBL:KJZ06720.1, ECO:0000313|Proteomes:UP000033452};
RN   [1] {ECO:0000313|EMBL:KJZ06720.1, ECO:0000313|Proteomes:UP000033452}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2471 {ECO:0000313|EMBL:KJZ06720.1,
RC   ECO:0000313|Proteomes:UP000033452};
RX   PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA   Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT   "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT   bacteria.";
RL   BMC Genomics 16:158-158(2015).
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:KJZ06720.1}.
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DR   EMBL; JXYA01000045; KJZ06720.1; -; Genomic_DNA.
DR   RefSeq; WP_046006389.1; NZ_JXYA01000045.1.
DR   AlphaFoldDB; A0A0F4QHF7; -.
DR   PATRIC; fig|43658.5.peg.3825; -.
DR   OrthoDB; 5289281at2; -.
DR   Proteomes; UP000033452; 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|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_02043};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_02043}; Reference proteome {ECO:0000313|Proteomes:UP000033452};
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};
KW   tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP-
KW   Rule:MF_02043}.
FT   DOMAIN          5..306
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            283
FT                   /note="Interacts with tRNA"
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   315 AA;  35441 MW;  8458A8294566EEDC CRC64;
     MKLFLAPMEG VVDFKMRELL TDLGGFDMCV TEFIRVVDLT LPRRVFIRYC PELLNGGLTR
     AGTPVRIQLL GQVPHVLAAN ARKAVKLGSH GVDLNFGCPA KTVNKSKGGA VLLKEPEQIY
     QIIRAVREAV PQEHEVSAKI RLGFDDDSNS TEIVDAVQSA GASSLVIHAR TKRDGYKPPA
     YWEKIPPLLE RLTIPVVANG EIWQVEDAMR CRQRSGCNNL MLGRGALATP DLAAKIKAHV
     AGEDYQPLVW QKVVYHILHS SMHQDESMSE KYFSSRTKQW LGYLKLQYPQ AHELFEKVKR
     LKRTHEVVDV LHQEL
//
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