ID   RMLA_ACTS5              Reviewed;         303 AA.
AC   Q9ZAE7; G8SLW3;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 2.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Glucose-1-phosphate thymidylyltransferase;
DE            EC=2.7.7.24;
DE   AltName: Full=dTDP-glucose pyrophosphorylase;
DE   AltName: Full=dTDP-glucose synthase;
GN   Name=acbA; OrderedLocusNames=ACPL_3682;
OS   Actinoplanes sp. (strain ATCC 31044 / CBS 674.73 / SE50/110).
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Actinoplanes; unclassified Actinoplanes.
OX   NCBI_TaxID=134676;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 31044 / CBS 674.73 / SE50/110;
RX   PubMed=10196166; DOI=10.1074/jbc.274.16.10889;
RA   Stratmann A., Mahmud T., Lee S., Distler J., Floss H.G., Piepersberg W.;
RT   "The AcbC protein from Actinoplanes species is a C7-cyclitol synthase
RT   related to 3-dehydroquinate synthases and is involved in the biosynthesis
RT   of the alpha-glucosidase inhibitor acarbose.";
RL   J. Biol. Chem. 274:10889-10896(1999).
RN   [2]
RP   SEQUENCE REVISION TO 264-265.
RA   Wehmeier U.F.;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31044 / CBS 674.73 / SE50/110;
RA   Schwientek P., Szczepanowski R., Kalinowski J., Klein A., Selber K.,
RA   Wehmeier U.F., Stoye J., Puehler A.;
RT   "The complete genome sequence of the acarbose producer Actinoplanes sp.
RT   SE50/110.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and
CC       glucose 1-phosphate, as well as its pyrophosphorolysis. {ECO:0000250}.
CC   -!- FUNCTION: Probably involved in the biosynthesis of the acarviose moiety
CC       of the alpha-glucosidase inhibitor acarbose.
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   -!- SIMILARITY: Belongs to the glucose-1-phosphate thymidylyltransferase
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AEV84577.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; Y18523; CAA77210.2; -; Genomic_DNA.
DR   EMBL; CP003170; AEV84577.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_043514542.1; NZ_LT827010.1.
DR   AlphaFoldDB; Q9ZAE7; -.
DR   SMR; Q9ZAE7; -.
DR   STRING; 134676.ACPL_3682; -.
DR   EnsemblBacteria; AEV84577; AEV84577; ACPL_3682.
DR   KEGG; ase:ACPL_3682; -.
DR   PATRIC; fig|134676.3.peg.3598; -.
DR   eggNOG; COG1209; Bacteria.
DR   HOGENOM; CLU_029499_9_0_11; -.
DR   OrthoDB; 1004719at2; -.
DR   Proteomes; UP000005440; Chromosome.
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: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   Magnesium; Metal-binding; Nucleotidyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..303
FT                   /note="Glucose-1-phosphate thymidylyltransferase"
FT                   /id="PRO_0000208006"
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   303 AA;  32545 MW;  CE50E7D56038E60D CRC64;
     MRGILLAGGT GSRLRPVTWA VSKQLMPVYD KPMIYYPLAT LVSCGIREIL VITTETEAAQ
     FQRLLGDGSQ WGLRLEFAVQ QRPGGIAEAF LIGEEFLAGG PVALMLGDNL LHGVDFRPCV
     QRARETAGGH VFGVAVADPS AYGVVEFDAA GRVLSIEEKP VRPRSPYAVP GFYLYDADVV
     ETARSLRPSA RGELEITEVN QAYLRRGALS VTLLGRGAVW LDTGTLADCM RAVDYVRAID
     EGQGIKIGCV EEAAWRAGFL DTAQLRALAE PLMSSGYGQY LLALTGDGLS RTPQWPALTA
     AAG