[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=LT2; DOI=10.1111/j.1365-2958.1991.tb00741.x; PubMed=1710759 [NCBI, ExPASy, EBI, Israel, Japan] Jiang X.-M., Neal B., Santiago F., Lee S.J., Romana L.K., Reeves P.R.; "Structure and sequence of the rfb (O antigen) gene cluster of Salmonella serovar typhimurium (strain LT2)."; Mol. Microbiol. 5:695-713(1991).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=LT2 / SGSC1412 / ATCC 700720; DOI=10.1038/35101614; PubMed=11677609 [NCBI, ExPASy, EBI, Israel, Japan] McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E., Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.; "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."; Nature 413:852-856(2001).
[3]	PROTEIN SEQUENCE OF 1-22, AND FUNCTION. STRAIN=LT2; PubMed=8382158 [NCBI, ExPASy, EBI, Israel, Japan] Lindquist L., Kaiser R., Reeves P.R., Lindberg A.A.; "Purification, characterization and HPLC assay of Salmonella glucose-1-phosphate thymidylyltransferase from the cloned rfbA gene."; Eur. J. Biochem. 211:763-770(1993).
[4]	CHARACTERIZATION, MUTAGENESIS OF THR-201 AND TRP-224, AND X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF COMPLEXES WITH UDP-GLC AND DTTP. STRAIN=LT2; DOI=10.1038/88618; PubMed=11373625 [NCBI, ExPASy, EBI, Israel, Japan] Barton W.A., Lesniak J., Biggins J.B., Jeffrey P.D., Jiang J., Rajashankar K.R., Thorson J.S., Nikolov D.B.; "Structure, mechanism and engineering of a nucleotidylyltransferase as a first step toward glycorandomization."; Nat. Struct. Biol. 8:545-551(2001).

Comments

FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis. Is also able to convert non natural substrates such as a wide array of alpha-D-hexopyranosyl, deoxy-alpha-D-glucopyranosyl, aminodeoxy-alpha-D-hexopyranosyl and acetamidodeoxy-alpha-D-hexopyranosyl phosphates to their corresponding dTDP- and UDP-nucleotide sugars.
CATALYTIC ACTIVITY: dTTP + alpha-D-glucose 1-phosphate = diphosphate + dTDP-glucose.
COFACTOR: Binds 1 magnesium ion per subunit (Probable).
BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters: K_M=0.7 mM for dTTP;
K_M=0.3 mM for G1P;
PATHWAY: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis .
PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen biosynthesis .
SUBUNIT: Homotetramer.
SIMILARITY: Belongs to the glucose-1-phosphate thymidylyltransferase family.
CAUTION: The position of the magnesium ion observed in the crystallographic structure is different from that observed in the structure of E.coli rmlA2 (rffH) and does not seem to correspond to the binding site for the catalytically essential magnesium ion. Therefore, we choose to propagate in the feature lines the positions found in the E.coli structure.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X56793; CAA40117.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE008792; AAL20999.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S15301; S15301.

RefSeq

NP_461040.1; -.

3D structure databases

PDB

1IIM; X-ray; 2.10 A; A/B=1-291.	[ExPASy / RCSB / EBI]
1IIN; X-ray; 2.10 A; A/B/C/D=1-291.	[ExPASy / RCSB / EBI]
1MP3; X-ray; 2.20 A; A/B=1-292.	[ExPASy / RCSB / EBI]
1MP4; X-ray; 2.20 A; A/B=1-292.	[ExPASy / RCSB / EBI]
1MP5; X-ray; 2.75 A; A=1-292.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1IIM; -.
1IIN; -.
1MP3; -.
1MP4; -.
1MP5; -.

ModBase

P26393.

Enzyme and pathway databases

BioCyc

STYP99287:STM2095-MON; -.

Organism-specific databases

StyGene

SG10449; rmlA.

Ontologies

GO:0008879;	Molecular function: glucose-1-phosphate thymidylyltransferase activity (inferred from electronic annotation from InterPro).
GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0045226;	Biological process: extracellular polysaccharide biosynthetic process (inferred from electronic annotation from InterPro).
GO:0009103;	Biological process: lipopolysaccharide biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR005907; G1P_thy_trans_l.
IPR005835; NTP_transferase.
Graphical view of domain structure.

Pfam

PF00483; NTP_transferase; 1.
Pfam graphical view of domain structure.

TIGR01207; rmlA; 1.

Genome annotation databases

GeneID

1253616; -.

GenomeReviews

AE006468_GR; STM2095.

KEGG

stm:STM2095; -.

NMPDR

fig|99287.1.peg.2020; -.

Phylogenomic databases

HOGENOM

P26393; -.

Genome annotation databases

CMR

P26393; STM2095.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Complete proteome; Direct protein sequencing; Lipopolysaccharide biosynthesis; Magnesium; Metal-binding; Nucleotidyltransferase; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 292`	`292`	`Glucose-1-phosphate thymidylyltransferase.`	`PRO_0000207995`
`METAL`	`111 111`		`Magnesium (By similarity).`
`METAL`	`226 226`		`Magnesium (By similarity).`
`MUTAGEN`	`201 201`		`T->A: Two-fold increase in the conversion of 2-acetamido-2-deoxy-alpha-D-glucopyranosyl phosphate.`
`MUTAGEN`	`224 224`		`W->H: Is able to convert both 6-acetamido-6-deoxy-alpha-D-glucopyranosyl phosphate and alpha-D-glucopyranuronic acid 1-(dihydrogen phosphate), which are not accepted by the wild-type.`
`STRAND`	`5 9`	`5`
`HELIX`	`15 17`	`3`
`TURN`	`18 22`	`5`
`HELIX`	`26 28`	`3`
`STRAND`	`29 35`	`7`
`HELIX`	`38 46`	`9`
`STRAND`	`51 56`	`6`
`TURN`	`58 60`	`3`
`HELIX`	`61 68`	`8`
`HELIX`	`72 74`	`3`
`STRAND`	`77 82`	`6`
`HELIX`	`89 91`	`3`
`HELIX`	`92 95`	`4`
`HELIX`	`97 100`	`4`
`STRAND`	`105 109`	`5`
`STRAND`	`112 115`	`4`
`HELIX`	`119 128`	`10`
`STRAND`	`130 139`	`10`
`HELIX`	`143 145`	`3`
`STRAND`	`146 151`	`6`
`STRAND`	`157 163`	`7`
`STRAND`	`168 179`	`12`
`HELIX`	`183 189`	`7`
`HELIX`	`200 209`	`10`
`STRAND`	`213 217`	`5`
`STRAND`	`222 226`	`5`
`HELIX`	`230 247`	`18`
`HELIX`	`254 260`	`7`
`HELIX`	`266 273`	`8`
`HELIX`	`274 276`	`3`
`HELIX`	`280 288`	`9`

Sequence information

Length: 292 AA [This is the length of the unprocessed precursor]

Molecular weight: 32453 Da [This is the MW of the unprocessed precursor]

CRC64: 11065BA9DF2B0268 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKTRKGIILA GGSGTRLYPV TMAVSKQLLP IYDKPMIYYP LSTLMLAGIR DILIISTPQD 

        70         80         90        100        110        120 
TPRFQQLLGD GSQWGLNLQY KVQPSPDGLA QAFIIGEEFI GHDDCALVLG DNIFYGHDLP 

       130        140        150        160        170        180 
KLMEAAVNKE SGATVFAYHV NDPERYGVVE FDQKGTAVSL EEKPLQPKSN YAVTGLYFYD 

       190        200        210        220        230        240 
NSVVEMAKNL KPSARGELEI TDINRIYMEQ GRLSVAMMGR GYAWLDTGTH QSLIEASNFI 

       250        260        270        280        290 
ATIEERQGLK VSCPEEIAFR KNFINAQQVI ELAGPLSKND YGKYLLKMVK GL

P26393 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools