RMLA_MYCS2
ID RMLA_MYCS2 Reviewed; 288 AA.
AC A0QPF9; I7FD92;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=rmlA; Synonyms=rfbA; OrderedLocusNames=MSMEG_0384, MSMEI_0377;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=16194230; DOI=10.1111/j.1365-2958.2005.04847.x;
RA Sonden B., Kocincova D., Deshayes C., Euphrasie D., Rhayat L., Laval F.,
RA Frehel C., Daffe M., Etienne G., Reyrat J.M.;
RT "Gap, a mycobacterial specific integral membrane protein, is required for
RT glycolipid transport to the cell surface.";
RL Mol. Microbiol. 58:426-440(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [5]
RP FUNCTION AS A THYMIDYLYLTRANSFERASE, AND CATALYTIC ACTIVITY.
RX PubMed=9084178; DOI=10.1099/00221287-143-3-937;
RA Ma Y., Mills J.A., Belisle J.T., Vissa V., Howell M., Bowlin K.,
RA Scherman M.S., McNeil M.;
RT "Determination of the pathway for rhamnose biosynthesis in mycobacteria:
RT cloning, sequencing and expression of the Mycobacterium tuberculosis gene
RT encoding alpha-D-glucose-1-phosphate thymidylyltransferase.";
RL Microbiology 143:937-945(1997).
CC -!- FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and
CC glucose 1-phosphate, as well as its pyrophosphorolysis. Involved in the
CC biosynthesis of the dTDP-L-rhamnose which is a component of the
CC critical linker, D-N-acetylglucosamine-L-rhamnose disaccharide, which
CC connects the galactan region of arabinogalactan to peptidoglycan via a
CC phosphodiester linkage. {ECO:0000269|PubMed:9084178}.
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 Evidence={ECO:0000269|PubMed:9084178};
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: Carbohydrate biosynthesis; dTDP-L-rhamnose 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; AY439015; ABB72064.1; -; Genomic_DNA.
DR EMBL; CP000480; ABK72771.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP36858.1; -; Genomic_DNA.
DR RefSeq; WP_011726901.1; NZ_SIJM01000018.1.
DR RefSeq; YP_884797.1; NC_008596.1.
DR AlphaFoldDB; A0QPF9; -.
DR SMR; A0QPF9; -.
DR STRING; 246196.MSMEI_0377; -.
DR EnsemblBacteria; ABK72771; ABK72771; MSMEG_0384.
DR EnsemblBacteria; AFP36858; AFP36858; MSMEI_0377.
DR GeneID; 66738571; -.
DR KEGG; msg:MSMEI_0377; -.
DR KEGG; msm:MSMEG_0384; -.
DR PATRIC; fig|246196.19.peg.381; -.
DR eggNOG; COG1209; Bacteria.
DR OMA; FTWLDTG; -.
DR OrthoDB; 1004719at2; -.
DR UniPathway; UPA00124; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0008879; F:glucose-1-phosphate thymidylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0019305; P:dTDP-rhamnose biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; IDA:UniProtKB.
DR GO; GO:0019300; P:rhamnose biosynthetic process; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Magnesium; Metal-binding; Nucleotidyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..288
FT /note="Glucose-1-phosphate thymidylyltransferase"
FT /id="PRO_0000395346"
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 288 AA; 31354 MW; 6542EE383821C0D6 CRC64;
MRGIILAGGS GTRLHPLTIG VSKQLLPVYD KPLVYYPLST LIMAGIRDIL VITTPADAPA
FRRLLGDGSD FGVNLSYAAQ NEPEGLAQAF LIGADHIGND TVALALGDNI FYGPGLGTSL
RRFEHVSGGA IFAYWVANPS AYGVVEFDAD GKAVSLEEKP KTPKSHYAVP GLYFYDNTVI
DIARSLKKSA RGEYEITEVN QIYLNRGQLS VEVLARGTAW LDTGTFDSLL DASDFVRTIE
LRQGLKVGAP EEIAWRAGFI DDDQLATRAK ELLKSGYGHY LLQLLDRE
