UniProtKB - P37744 (RMLA1_ECOLI)

BLAST

>sp|P37744|RMLA1_ECOLI Glucose-1-phosphate thymidylyltransferase 1 OS=Escherichia coli (strain K12) OX=83333 GN=rfbA PE=1 SV=2
MKMRKGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQD
TPRFQQLLGDGSQWGLNLQYKVQPSPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLP
KLMEAAVNKESGATVFAYHVNDPERYGVVEFDKNGTAISLEEKPLEPKSNYAVTGLYFYD
NDVVQMAKNLKPSARGELEITDINRIYLEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFI
ATIEERQGLKVSCPEEIAFRKGFIDVEQVRKLAVPLIKNNYGQYLYKMTKDSN

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History
Entry version 147 (28 Mar 2018)
Sequence version 2 (01 Nov 1997)
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Protein

Glucose-1-phosphate thymidylyltransferase 1

Gene

rfbA

Organism

Escherichia coli (strain K12)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis.1 Publication

Miscellaneous

Both catalyzed reactions, i.e. dTDP-glucose biosynthesis and pyrophosphorolysis, follow a sequential ordered bi-bi catalytic mechanism.1 Publication

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.Curated

Catalytic activityⁱ

dTTP + alpha-D-glucose 1-phosphate = diphosphate + dTDP-alpha-D-glucose.1 Publication

Cofactorⁱ

Mg²⁺1 PublicationNote: Binds 1 Mg²⁺ ion per subunit.1 Publication

Kineticsⁱ

pH dependenceⁱ

Optimum pH is 8.0-8.5. Active from pH 6.0 to 10.0.1 Publication

Pathwayⁱ: dTDP-L-rhamnose biosynthesis

This protein is involved in the pathway dTDP-L-rhamnose biosynthesis, which is part of Carbohydrate biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway dTDP-L-rhamnose biosynthesis and in Carbohydrate biosynthesis.

Pathwayⁱ: LPS O-antigen biosynthesis

This protein is involved in the pathway LPS O-antigen biosynthesis, which is part of Bacterial outer membrane biogenesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway LPS O-antigen biosynthesis and in Bacterial outer membrane biogenesis.

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Metal bindingⁱ	111	MagnesiumBy similarity		1
Metal bindingⁱ	226	MagnesiumBy similarity		1

GO - Molecular functionⁱ

glucose-1-phosphate thymidylyltransferase activity
Source: EcoCyc
Inferred from direct assayⁱ
- 11697907
identical protein binding
Source: EcoCyc
Inferred from direct assayⁱ
- 11697907
metal ion binding
Source: EcoCyc
Inferred from direct assayⁱ
- 11697907

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

dTDP-rhamnose biosynthetic process Source: UniProtKB-UniPathway
extracellular polysaccharide biosynthetic process Source: InterPro
O antigen biosynthetic process Source: UniProtKB-UniPathway

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Nucleotidyltransferase, Transferase
Biological process	Lipopolysaccharide biosynthesis
Ligand	Magnesium, Metal-binding

Enzyme and pathway databases

BioCycⁱ	EcoCyc:DTDPGLUCOSEPP-MONOMER MetaCyc:DTDPGLUCOSEPP-MONOMER
UniPathwayⁱ	UPA00124 UPA00281

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Glucose-1-phosphate thymidylyltransferase 1 (EC:2.7.7.241 Publication) Short name: G1P-TT 1 Alternative name(s): dTDP-glucose pyrophosphorylase 1 dTDP-glucose synthase 1
Gene namesⁱ	Name:rfbA Synonyms:rmlA, rmlA1 Ordered Locus Names:b2039, JW2024
Organismⁱ	Escherichia coli (strain K12)
Taxonomic identifierⁱ	83333 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli
Proteomesⁱ	UP000000318 Componentⁱ: Chromosome UP000000625 Componentⁱ: Chromosome

Organism-specific databases

EcoGeneⁱ	EG11978 rfbA

EcoGeneⁱ

EG11978 rfbA

Subcellular locationⁱ

GO - Cellular componentⁱ

cytosol
Source: EcoCyc
Inferred from direct assayⁱ
- 18304323

View the complete GO annotation on QuickGO ...

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000207991	1 – 293	Glucose-1-phosphate thymidylyltransferase 1Add BLAST		293

Proteomic databases

EPDⁱ	P37744
PaxDbⁱ	P37744
PRIDEⁱ	P37744

2D gel databases

SWISS-2DPAGEⁱ	P37744

SWISS-2DPAGEⁱ

P37744

Interactionⁱ

Subunit structureⁱ

Homotetramer.1 Publication

GO - Molecular functionⁱ

identical protein binding
Source: EcoCyc
Inferred from direct assayⁱ
- 11697907

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	4259680, 190 interactors
IntActⁱ	P37744, 9 interactors
STRINGⁱ	316385.ECDH10B_2189

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	4 – 9	Combined sources	6
Helixⁱ	15 – 17	Combined sources	3
Turnⁱ	18 – 22	Combined sources	5
Helixⁱ	26 – 28	Combined sources	3
Beta strandⁱ	29 – 31	Combined sources	3
Helixⁱ	38 – 46	Combined sources	9
Beta strandⁱ	49 – 56	Combined sources	8
Turnⁱ	58 – 60	Combined sources	3
Helixⁱ	61 – 68	Combined sources	8
Helixⁱ	72 – 74	Combined sources	3
Beta strandⁱ	77 – 82	Combined sources	6
Helixⁱ	91 – 95	Combined sources	5
Helixⁱ	97 – 100	Combined sources	4
Beta strandⁱ	105 – 109	Combined sources	5
Beta strandⁱ	113 – 115	Combined sources	3
Helixⁱ	119 – 128	Combined sources	10
Beta strandⁱ	131 – 139	Combined sources	9
Helixⁱ	143 – 145	Combined sources	3
Beta strandⁱ	146 – 151	Combined sources	6
Beta strandⁱ	153 – 155	Combined sources	3
Beta strandⁱ	157 – 163	Combined sources	7
Beta strandⁱ	170 – 179	Combined sources	10
Helixⁱ	183 – 189	Combined sources	7
Beta strandⁱ	194 – 197	Combined sources	4
Helixⁱ	200 – 209	Combined sources	10
Beta strandⁱ	213 – 217	Combined sources	5
Beta strandⁱ	222 – 225	Combined sources	4
Helixⁱ	230 – 247	Combined sources	18
Helixⁱ	254 – 260	Combined sources	7
Helixⁱ	266 – 273	Combined sources	8
Helixⁱ	274 – 276	Combined sources	3
Helixⁱ	280 – 288	Combined sources	9

Show more details

3D structure databases

ProteinModelPortalⁱ	P37744
SMRⁱ	P37744
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P37744

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the glucose-1-phosphate thymidylyltransferase family.Curated

Phylogenomic databases

eggNOGⁱ	ENOG4108I19 Bacteria COG1209 LUCA
HOGENOMⁱ	HOG000283473
InParanoidⁱ	P37744
KEGG Orthology (KO) More...KOⁱ	K00973
OMAⁱ	GPYPMIY
PhylomeDBⁱ	P37744

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd02538 G1P_TT_short, 1 hit
Gene3Dⁱ	3.90.550.10, 1 hit
InterProⁱ	View protein in InterPro IPR005907 G1P_thy_trans_s IPR005835 NTP_transferase_dom IPR029044 Nucleotide-diphossugar_trans
PANTHERⁱ	PTHR43532 PTHR43532, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00483 NTP_transferase, 1 hit
SUPFAMⁱ	SSF53448 SSF53448, 1 hit
TIGRFAMsⁱ	TIGR01207 rmlA, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P37744-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MKMRKGIILA GGSGTRLYPV TMAVSKQLLP IYDKPMIYYP LSTLMLAGIR 
        60         70         80         90        100
DILIISTPQD TPRFQQLLGD GSQWGLNLQY KVQPSPDGLA QAFIIGEEFI 
       110        120        130        140        150
GGDDCALVLG DNIFYGHDLP KLMEAAVNKE SGATVFAYHV NDPERYGVVE 
       160        170        180        190        200
FDKNGTAISL EEKPLEPKSN YAVTGLYFYD NDVVQMAKNL KPSARGELEI 
       210        220        230        240        250
TDINRIYLEQ GRLSVAMMGR GYAWLDTGTH QSLIEASNFI ATIEERQGLK 
       260        270        280        290 
VSCPEEIAFR KGFIDVEQVR KLAVPLIKNN YGQYLYKMTK DSN

Length:293

Mass (Da):32,694

Last modified:November 1, 1997 - v2

Checksum:ⁱBA895362D1C5CA55

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	247	Q → P in AAC31629 (PubMed:7517390).Curated		1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U09876 Genomic DNA Translation: AAB88400.1 U00096 Genomic DNA Translation: AAC75100.1 AP009048 Genomic DNA Translation: BAA15881.1 U03041 Genomic DNA Translation: AAC31629.1
PIRⁱ	F64969
NCBI Reference Sequences More...RefSeqⁱ	NP_416543.1, NC_000913.3 WP_000783975.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC75100; AAC75100; b2039 BAA15881; BAA15881; BAA15881
GeneIDⁱ	945154
KEGGⁱ	ecj:JW2024 eco:b2039
PATRICⁱ	fig\|1411691.4.peg.212

Protein	Similar proteins		Species	Score	Length	Source
P37744	Glucose-1-phosphate thymidylyltransferase		ECOLX		293	UniRef100_P37744
Glucose-1-phosphate thymidylyltransferase		Escherichia coli 3-373-03_S4_C2		293
Glucose-1-phosphate thymidylyltransferase		Escherichia coli HVH 70 (4-2963531)		293
Glucose-1-phosphate thymidylyltransferase (Fragment)		ACINO		81
UPI000BA952A6		ECOLX		284
+1

Protein	Similar proteins		Species	Score	Length	Source
P37744	Glucose-1-phosphate thymidylyltransferase	)	SALTY		292	UniRef90_P37744
Glucose-1-phosphate thymidylyltransferase		ECOLX		293
Glucose-1-phosphate thymidylyltransferase		Escherichia coli 3-373-03_S4_C2		293
Glucose-1-phosphate thymidylyltransferase		Escherichia coli HVH 70 (4-2963531)		293
Glucose-1-phosphate thymidylyltransferase (Fragment)		ACINO		81
+220

Protein	Similar proteins		Species	Score	Length	Source
P37744	Glucose-1-phosphate thymidylyltransferase	)	SALTY		292	UniRef50_P37744
Glucose-1-phosphate thymidylyltransferase		STRMU		289
Glucose-1-phosphate thymidylyltransferase 2	)	ECOLI		293
Glucose-1-phosphate thymidylyltransferase 2		SHIFL		293
Glucose-1-phosphate thymidylyltransferase		ECOLX		293
+6559

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U09876 Genomic DNA Translation: AAB88400.1 U00096 Genomic DNA Translation: AAC75100.1 AP009048 Genomic DNA Translation: BAA15881.1 U03041 Genomic DNA Translation: AAC31629.1
PIRⁱ	F64969
RefSeqⁱ	NP_416543.1, NC_000913.3 WP_000783975.1, NZ_LN832404.1

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB 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	[»]
ProteinModelPortalⁱ	P37744
SMRⁱ	P37744
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4259680, 190 interactors
IntActⁱ	P37744, 9 interactors
STRINGⁱ	316385.ECDH10B_2189

2D gel databases

SWISS-2DPAGEⁱ	P37744

SWISS-2DPAGEⁱ

P37744

Proteomic databases

EPDⁱ	P37744
PaxDbⁱ	P37744
PRIDEⁱ	P37744

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAC75100; AAC75100; b2039 BAA15881; BAA15881; BAA15881
GeneIDⁱ	945154
KEGGⁱ	ecj:JW2024 eco:b2039
PATRICⁱ	fig\|1411691.4.peg.212

Organism-specific databases

EchoBASEⁱ	EB1921
EcoGeneⁱ	EG11978 rfbA

Phylogenomic databases

eggNOGⁱ	ENOG4108I19 Bacteria COG1209 LUCA
HOGENOMⁱ	HOG000283473
InParanoidⁱ	P37744
KOⁱ	K00973
OMAⁱ	GPYPMIY
PhylomeDBⁱ	P37744

Enzyme and pathway databases

UniPathwayⁱ	UPA00124 UPA00281
BioCycⁱ	EcoCyc:DTDPGLUCOSEPP-MONOMER MetaCyc:DTDPGLUCOSEPP-MONOMER

Miscellaneous databases

EvolutionaryTraceⁱ	P37744
Protein Ontology More...PROⁱ	PR:P37744

Family and domain databases

CDDⁱ	cd02538 G1P_TT_short, 1 hit
Gene3Dⁱ	3.90.550.10, 1 hit
InterProⁱ	View protein in InterPro IPR005907 G1P_thy_trans_s IPR005835 NTP_transferase_dom IPR029044 Nucleotide-diphossugar_trans
PANTHERⁱ	PTHR43532 PTHR43532, 1 hit
Pfamⁱ	View protein in Pfam PF00483 NTP_transferase, 1 hit
SUPFAMⁱ	SSF53448 SSF53448, 1 hit
TIGRFAMsⁱ	TIGR01207 rmlA, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	RMLA1_ECOLI
Accessionⁱ	P37744Primary (citable) accession number: P37744 Secondary accession number(s): P78081
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
	Last sequence update:	November 1, 1997
	Last modified:	March 28, 2018
	This is version 147 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

PDB cross-references
Index of Protein Data Bank (PDB) cross-references
SIMILARITY comments
Index of protein domains and families
PATHWAY comments
Index of metabolic and biosynthesis pathways
Escherichia coli
Escherichia coli (strain K12): entries and cross-references to EcoGene

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P37744 (RMLA1_ECOLI)

Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the ‘basket’ to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>

Glucose-1-phosphate thymidylyltransferase 1

rfbA

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

Caution

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

pH dependencei

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: dTDP-L-rhamnose biosynthesis

Pathwayi: LPS O-antigen biosynthesis

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

2D gel databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Experimental Info

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

Kineticsⁱ

pH dependenceⁱ

Pathwayⁱ: dTDP-L-rhamnose biosynthesis

Pathwayⁱ: LPS O-antigen biosynthesis

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

PTM / Processingⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ