ID Q1ZRR0_PHOAS Unreviewed; 313 AA.
AC Q1ZRR0;
DT 02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 02-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 81.
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=VAS14_06088 {ECO:0000313|EMBL:EAS65267.1};
OS Photobacterium angustum (strain S14 / CCUG 15956) (Vibrio sp. (strain S14 /
OS CCUG 15956)).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=314292 {ECO:0000313|EMBL:EAS65267.1, ECO:0000313|Proteomes:UP000001603};
RN [1] {ECO:0000313|EMBL:EAS65267.1, ECO:0000313|Proteomes:UP000001603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S14 {ECO:0000313|EMBL:EAS65267.1,
RC ECO:0000313|Proteomes:UP000001603};
RX PubMed=19805210; DOI=10.1073/pnas.0903507106;
RA Lauro F.M., McDougald D., Thomas T., Williams T.J., Egan S., Rice S.,
RA DeMaere M.Z., Ting L., Ertan H., Johnson J., Ferriera S., Lapidus A.,
RA Anderson I., Kyrpides N., Munk A.C., Detter C., Han C.S., Brown M.V.,
RA Robb F.T., Kjelleberg S., Cavicchioli R.;
RT "The genomic basis of trophic strategy in marine bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:15527-15533(2009).
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:EAS65267.1}.
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DR EMBL; AAOJ01000002; EAS65267.1; -; Genomic_DNA.
DR RefSeq; WP_005369056.1; NZ_CH902600.1.
DR AlphaFoldDB; Q1ZRR0; -.
DR eggNOG; COG0042; Bacteria.
DR HOGENOM; CLU_013299_0_4_6; -.
DR OrthoDB; 9764501at2; -.
DR Proteomes; UP000001603; 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}; 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..260
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 313 AA; 35045 MW; 798E4F0B6E794425 CRC64;
MRVILGPMEG VLDHLMREML TEINDYDLCV TEFVRVIDSL LPSSVFYRLC PELRQGGKTR
SGTPVRVQIL GQDPNWMAEN AQRACSLGSA GVDINFGCPA KAVNKSRGGA VLLKEPERIY
QIVKACRAAV NPVKPLTAKV RLGWDDPAQC FEIADAIAQA GADEMVVHAR TKEDGYRAET
IKWDYIKQLK QSVAIPIIAN GEVWNYQDGQ ACLSTTNTDA LMVCRGALNL PNLGNVVKHN
QAHMSWEDVL ALLLVYSQFE IKGDKGLYYP NRVKQWFSYL RHEYPQAKLL FTDIRALNKA
APIIEVLQRA QQQ
//
