Glucose-1-phosphate thymidylyltransferase 1 - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P37744 (RMLA1_ECOLI)

Last modified June 16, 2009. Version 77. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Glucose-1-phosphate thymidylyltransferase 1
      Short name=G1P-TT 1
    EC=2.7.7.24
Alternative name(s):
    dTDP-glucose synthase 1
    dTDP-glucose pyrophosphorylase 1

Gene names

Name:	rmlA1
Synonyms:	rfbA, rmlA
Ordered Locus Names:	b2039, JW2024

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	293 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis.
Catalytic activity	dTTP + alpha-D-glucose 1-phosphate = diphosphate + dTDP-glucose.
Cofactor	Binds 1 magnesium ion per subunit Probable.
Pathway	Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis. Bacterial outer membrane biogenesis; LPS O-antigen biosynthesis.
Subunit structure	Homotetramer.
Miscellaneous	Both catalyzed reactions, i.e. dTDP-glucose biosynthesis and pyrophosphorolysis, follow a sequential ordered bi-bi catalytic mechanism.
Sequence similarities	Belongs to the glucose-1-phosphate thymidylyltransferase family.
Caution	Most extant K-12 lines do not express O-antigen because of mutations in dTDP-rhamnose biosynthetic genes or in the rhamnosyltransferase gene wbbL.
biophysicochemical properties	Kinetic parameters: K_M=20.5 µM for dTTP K_M=34 µM for glucose 1-phosphate K_M=95 µM for dTDP-glucose K_M=154 µM for PPi V_max=194 µmol/min/mg enzyme for the forward reaction V_max=360 µmol/min/mg enzyme for the reverse reaction pH dependence: Optimum pH is 8.0-8.5. Active from pH 6.0 to 10.0.

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Ontologies

Keywords
Biological process	Lipopolysaccharide biosynthesis
Ligand	Magnesium Metal-binding
Molecular function	Nucleotidyltransferase Transferase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	extracellular polysaccharide biosynthetic process Inferred from electronic annotation. Source: InterPro lipopolysaccharide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB
Molecular function	glucose-1-phosphate thymidylyltransferase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 293

293

Glucose-1-phosphate thymidylyltransferase 1

PRO_0000207991

Sites

Metal binding

111

Magnesium By similarity

Metal binding

226

Magnesium By similarity

Experimental info

Sequence conflict

247

Q → P in AAC31629. Ref.6

Secondary structure

293

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P37744-1 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: BA895362D1C5CA55
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FASTA

293

32,694

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

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

       130        140        150        160        170        180 
KLMEAAVNKE SGATVFAYHV NDPERYGVVE FDKNGTAISL EEKPLEPKSN YAVTGLYFYD 

       190        200        210        220        230        240 
NDVVQMAKNL KPSARGELEI TDINRIYLEQ GRLSVAMMGR GYAWLDTGTH QSLIEASNFI 

       250        260        270        280        290 
ATIEERQGLK VSCPEEIAFR KGFIDVEQVR KLAVPLIKNN YGQYLYKMTK DSN

« Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure of the O antigen of Escherichia coli K-12 and the sequence of its rfb gene cluster." Stevenson G., Neal B., Liu D., Hobbs M., Packer N.H., Batley M., Redmond J.W., Lindquist L., Reeves P.R. J. Bacteriol. 176:4144-4156(1994) [PubMed: 7517391] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / WG1.
[2]	Stevenson G. Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 288.
[3]	"A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map." Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S. Horiuchi T. DNA Res. 3:379-392(1996) [PubMed: 9097040] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Genetic analysis of the O-specific lipopolysaccharide biosynthesis region (rfb) of Escherichia coli K-12 W3110: identification of genes that confer group 6 specificity to Shigella flexneri serotypes Y and 4a." Yao Z., Valvano M.A. J. Bacteriol. 176:4133-4143(1994) [PubMed: 7517390] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 247-293. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]	"Kinetic and crystallographic analyses support a sequential-ordered bi bi catalytic mechanism for Escherichia coli glucose-1-phosphate thymidylyltransferase." Zuccotti S., Zanardi D., Rosano C., Sturla L., Tonetti M., Bolognesi M. J. Mol. Biol. 313:831-843(2001) [PubMed: 11697907] [Abstract] Cited for: CHARACTERIZATION, X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF COMPLEXES WITH DTDP-G; DTMP AND G1P AND DEOXYTHYMIDINE AND G1P. Strain: K12.

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Cross-references

Sequence databases

U09876 Genomic DNA. Translation: AAB88400.1.
U00096 Genomic DNA. Translation: AAC75100.1.
AP009048 Genomic DNA. Translation: BAA15881.1.
U03041 Genomic DNA. Translation: AAC31629.1.

PIR

F64969.

RefSeq

AP_002639.1.
NP_416543.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1H5R	X-ray	1.90	A/C/D	1-293	[»]
			B	1-293	[»]
1H5S	X-ray	2.30	A	1-293	[»]
			B	1-293	[»]
			C	1-293	[»]
			D	1-293	[»]
1H5T	X-ray	1.90	A/C/D	1-293	[»]
			B	1-293	[»]

ModBase

Search...

2-D gel databases

SWISS-2DPAGE

P37744.

Genome annotation databases

GeneID

945154.

GenomeReviews

Gene locus JW2024 in contig AP009048_GR.
Gene locus b2039 in contig U00096_GR.

KEGG

ecj:JW2024.
eco:b2039.

Organism-specific databases

EchoBASE

EB1921.

EcoGene

EG11978. rmlA1.

CMR

Search...

Phylogenomic databases

HOGENOM

P37744.

OMA

P37744. GMNIQYA.

Enzyme and pathway databases

BioCyc

EcoCyc:DTDPGLUCOSEPP-MON.
MetaCyc:DTDPGLUCOSEPP-MON.

Family and domain databases

InterPro

IPR005907. G1P_thy_trans_l.
IPR005835. NTP_transferase.
[Graphical view]

Pfam

PF00483. NTP_transferase. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01207. rmlA. 1 hit.

ProtoNet

Search...

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Entry information

Entry name

RMLA1_ECOLI

Accession

Primary (citable) accession number: P37744
Secondary accession number(s): P78081

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	November 1, 1997
Last modified:	June 16, 2009
This is version 77 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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