ID C0QKD0_DESAH Unreviewed; 320 AA.
AC C0QKD0;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=tRNA-dihydrouridine synthase {ECO:0000256|PIRNR:PIRNR006621};
DE EC=1.3.1.- {ECO:0000256|PIRNR:PIRNR006621};
GN Name=dhs1 {ECO:0000313|EMBL:ACN14001.1};
GN OrderedLocusNames=HRM2_08880 {ECO:0000313|EMBL:ACN14001.1};
OS Desulforapulum autotrophicum (strain ATCC 43914 / DSM 3382 / VKM B-1955 /
OS HRM2) (Desulfobacterium autotrophicum).
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfobacteraceae; Desulforapulum.
OX NCBI_TaxID=177437 {ECO:0000313|EMBL:ACN14001.1, ECO:0000313|Proteomes:UP000000442};
RN [1] {ECO:0000313|EMBL:ACN14001.1, ECO:0000313|Proteomes:UP000000442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43914 / DSM 3382 / HRM2
RC {ECO:0000313|Proteomes:UP000000442};
RX PubMed=19187283; DOI=10.1111/j.1462-2920.2008.01825.x;
RA Strittmatter A.W., Liesegang H., Rabus R., Decker I., Amann J., Andres S.,
RA Henne A., Fricke W.F., Martinez-Arias R., Bartels D., Goesmann A.,
RA Krause L., Puehler A., Klenk H.P., Richter M., Schuler M., Gloeckner F.O.,
RA Meyerdierks A., Gottschalk G., Amann R.;
RT "Genome sequence of Desulfobacterium autotrophicum HRM2, a marine sulfate
RT reducer oxidizing organic carbon completely to carbon dioxide.";
RL Environ. Microbiol. 11:1038-1055(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. {ECO:0000256|PIRNR:PIRNR006621}.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|PIRNR:PIRNR006621};
CC -!- SIMILARITY: Belongs to the dus family. {ECO:0000256|PIRNR:PIRNR006621}.
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DR EMBL; CP001087; ACN14001.1; -; Genomic_DNA.
DR RefSeq; WP_012663241.1; NC_012108.1.
DR AlphaFoldDB; C0QKD0; -.
DR STRING; 177437.HRM2_08880; -.
DR KEGG; dat:HRM2_08880; -.
DR eggNOG; COG0042; Bacteria.
DR HOGENOM; CLU_013299_6_0_7; -.
DR OrthoDB; 5289281at2; -.
DR Proteomes; UP000000442; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0017150; F:tRNA dihydrouridine synthase activity; IEA:InterPro.
DR CDD; cd02801; DUS_like_FMN; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR035587; DUS-like_FMN-bd.
DR InterPro; IPR001269; DUS_fam.
DR PANTHER; PTHR45846; TRNA-DIHYDROURIDINE(47) SYNTHASE [NAD(P)(+)]-LIKE; 1.
DR PANTHER; PTHR45846:SF1; TRNA-DIHYDROURIDINE(47) SYNTHASE [NAD(P)(+)]-LIKE; 1.
DR Pfam; PF01207; Dus; 1.
DR PIRSF; PIRSF006621; Dus; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
PE 3: Inferred from homology;
KW Flavoprotein {ECO:0000256|PIRNR:PIRNR006621};
KW FMN {ECO:0000256|PIRNR:PIRNR006621};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR006621,
KW ECO:0000313|EMBL:ACN14001.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000442};
KW tRNA processing {ECO:0000256|PIRNR:PIRNR006621}.
FT DOMAIN 6..243
FT /note="DUS-like FMN-binding"
FT /evidence="ECO:0000259|Pfam:PF01207"
FT ACT_SITE 96
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006621-1"
SQ SEQUENCE 320 AA; 36396 MW; 164EBD3CD077A5CB CRC64;
MEKKLILAPL QGFTDAPFRQ VYPRHFTGFD EALAPFISTM GQARLKPSRI KDVLPENNPL
LPVVPQILGN VAEDFIFLAR YLADKGYTRV NWNLGCPHSK ITKKLRGSGL LCRPDLIDAF
LEQVVPAIPC SLSVKVRLGR KTSHEIFDLL PVFDRYPLDE IIVHPRTGVQ LYTGTADIDA
FERVLAQSRH ILVYNGDITD KKGFQVLVDR FPEIRSFMIG RGVLADPFLP ATIKGEVRDR
TMDLERIKAF HDDLFTTYDG NFYGPSHIAG RMKGFWSYLG PSFPGGEKLF KQIFKSRNRE
AYLVQTRRFF DEQIPFCPAG
//
