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

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P37744 (RMLA1_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 101. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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 pyrophosphorylase 1
dTDP-glucose synthase 1

Gene names

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

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	293 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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.

Ontologies

Keywords
Biological process	Lipopolysaccharide biosynthesis
Ligand	Magnesium Metal-binding
Molecular function	Nucleotidyltransferase Transferase
Technical term	3D-structure Complete proteome Reference 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 metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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...

Sequences

Sequence

Length

Mass (Da)

Tools

P37744 [UniParc].

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

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

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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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

NP_416543.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

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

ProteinModelPortal

P37744.

SMR

P37744. Positions 2-291.

ModBase

Search...

Protein-protein interaction databases

IntAct

P37744. 11 interactions.

2D gel databases

SWISS-2DPAGE

P37744.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000001700; EBESCP00000001700; EBESCG00000001402.
EBESCT00000018315; EBESCP00000017606; EBESCG00000017369.

GeneID

945154.

GenomeReviews

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

KEGG

ecj:JW2024.
eco:b2039.

PATRIC

32119411. VBIEscCol129921_2116.

Organism-specific databases

EchoBASE

EB1921.

EcoGene

EG11978. rmlA1.

Phylogenomic databases

eggNOG

COG1209.

GeneTree

EBGT00050000009640.

HOGENOM

HBG688195.

OMA

YRAGWID.

PhylomeDB

P37744.

ProtClustDB

PRK15480.

Enzyme and pathway databases

BioCyc

EcoCyc:DTDPGLUCOSEPP-MONOMER.
MetaCyc:DTDPGLUCOSEPP-MONOMER.

Gene expression databases

Genevestigator

P37744.

Family and domain databases

InterPro

IPR005907. G1P_thy_trans_s.
IPR005835. NTP_transferase.
[Graphical view]

K00973.

PANTHER

PTHR22572:SF13. PTHR22572:SF13. 1 hit.

Pfam

PF00483. NTP_transferase. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01207. RmlA. 1 hit.

ProtoNet

Search...

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:	January 25, 2012
This is version 101 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents