NOVV_STRNV
ID NOVV_STRNV Reviewed; 297 AA.
AC Q9L9E6;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Glucose-1-phosphate thymidylyltransferase;
DE EC=2.7.7.24;
DE AltName: Full=Novobiocin biosynthesis protein V;
DE AltName: Full=dTDP-glucose pyrophosphorylase;
DE AltName: Full=dTDP-glucose synthase;
GN Name=novV;
OS Streptomyces niveus (Streptomyces spheroides).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=193462;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 23965 / DSM 40292 / JCM 4252 / NBRC 12917 / NCIMB 11891 / NRRL
RC 2449;
RX PubMed=10770754; DOI=10.1128/aac.44.5.1214-1222.2000;
RA Steffensky M., Muhlenweg A., Wang Z.X., Li S.M., Heide L.;
RT "Identification of the novobiocin biosynthetic gene cluster of Streptomyces
RT spheroides NCIB 11891.";
RL Antimicrob. Agents Chemother. 44:1214-1222(2000).
RN [2]
RP REVIEW, AND POSSIBLE FUNCTION.
RX PubMed=16868863; DOI=10.1055/s-2006-946699;
RA Li S.M., Heide L.;
RT "The biosynthetic gene clusters of aminocoumarin antibiotics.";
RL Planta Med. 72:1093-1099(2006).
CC -!- FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and
CC glucose 1-phosphate in the novobiocin biosynthesis pathway, an
CC aminocoumarin family antibiotic that targets bacterial DNA gyrases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 1-phosphate + dTTP + H(+) = diphosphate +
CC dTDP-alpha-D-glucose; Xref=Rhea:RHEA:15225, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37568, ChEBI:CHEBI:57477,
CC ChEBI:CHEBI:58601; EC=2.7.7.24;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Antibiotic biosynthesis; novobiocin biosynthesis.
CC -!- SIMILARITY: Belongs to the glucose-1-phosphate thymidylyltransferase
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF170880; AAF67515.1; -; Genomic_DNA.
DR RefSeq; WP_069626150.1; NZ_MDCR01000039.1.
DR AlphaFoldDB; Q9L9E6; -.
DR SMR; Q9L9E6; -.
DR PRIDE; Q9L9E6; -.
DR KEGG; ag:AAF67515; -.
DR BioCyc; MetaCyc:MON-18086; -.
DR UniPathway; UPA01035; -.
DR GO; GO:0008879; F:glucose-1-phosphate thymidylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; IEA:InterPro.
DR CDD; cd02538; G1P_TT_short; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR005907; G1P_thy_trans_s.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR43532; PTHR43532; 1.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR TIGRFAMs; TIGR01207; rmlA; 1.
PE 3: Inferred from homology;
KW Antibiotic biosynthesis; Magnesium; Metal-binding; Nucleotidyltransferase;
KW Transferase.
FT CHAIN 1..297
FT /note="Glucose-1-phosphate thymidylyltransferase"
FT /id="PRO_0000424008"
FT BINDING 108
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 297 AA; 33096 MW; 9D84E40B40385FF0 CRC64;
MRGILLAGGT GSRLWPVTRA ISKQLIPVFD KPMIYYPLTT LMMAGVREIL VITRPDDQRQ
FRHLLGDGSQ LGLRLEYAVQ ERPEGIAQAF VLGAEFIGDQ SVALVLGDNI FHGAGLGTRL
RQYNDPAGAR IFAYVVADPK AYGVVEFDEA GRAVSIEEKP ARPKSRYAVP GLYFYDNRVL
DVVHGLVPSR RGELEITAVN ETYLKWGQLR VTTLDRGTAW LDTGTFASLV QASEYVRVVE
ERQGLKIGCV EEVAWRCGFI GNDQLRDLSR PLLKSGYGRY LLDLLADHEE LKEVKPS
