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Escherichia coli K-12 substr. MG1655 Enzyme: fused heptose 7-phosphate kinase/heptose 1-phosphate adenyltransferase



Gene: rfaE Accession Numbers: G7590 (EcoCyc), b3052, ECK3042

Synonyms: yqiF, hldE, gmhC, waaE

Regulation Summary Diagram: ?

Subunit composition of fused heptose 7-phosphate kinase/heptose 1-phosphate adenyltransferase = [RfaE]2
         fused heptose 7-phosphate kinase/heptose 1-phosphate adenyltransferase = RfaE

Summary:
HldE is a bifunctional protein with an N-terminal ribokinase superfamily domain and a C-terminal cytidylyltransferase superfamily domain; the two domains are genetically separable [Valvano00]. Structural modelling of the ribokinase domain using E. coli ribokinase led to the identification of amino acid residues potentially essential for catalysis, and site-directed mutagenesis of potential ATP binding site residues resulted in a dominant negative mutant phenotype [McArthur05]. HldE appears to function as a dimer in vivo [McArthur05].

HldE is involved in ADP-heptose formation [Sirisena92], catalyzing two steps in the pathway [Kneidinger02]. A heptoseless mutant contains a transposon insertion in the hldE gene [Valvano00]. hldE mutations were reported to result in increased expression of gabT and induction of mucoidy [Joloba04].

Locations: cytosol

Map Position: [3,193,342 <- 3,194,775] (68.83 centisomes)
Length: 1434 bp / 477 aa

Molecular Weight of Polypeptide: 51.051 kD (from nucleotide sequence), 55 kD (experimental) [Valvano00 ]

Unification Links: ASAP:ABE-0010015 , DIP:DIP-10666N , EchoBASE:EB3192 , EcoGene:EG13416 , EcoliWiki:b3052 , ModBase:P76658 , OU-Microarray:b3052 , PortEco:rfaE , PR:PRO_000022905 , Pride:P76658 , Protein Model Portal:P76658 , RefSeq:NP_417524 , RegulonDB:G7590 , SMR:P76658 , String:511145.b3052 , UniProt:P76658

Relationship Links: InterPro:IN-FAMILY:IPR002173 , InterPro:IN-FAMILY:IPR004821 , InterPro:IN-FAMILY:IPR011611 , InterPro:IN-FAMILY:IPR011913 , InterPro:IN-FAMILY:IPR011914 , InterPro:IN-FAMILY:IPR014729 , InterPro:IN-FAMILY:IPR023030 , Pfam:IN-FAMILY:PF00294 , Pfam:IN-FAMILY:PF01467 , Prosite:IN-FAMILY:PS00583 , Prosite:IN-FAMILY:PS00584

In Paralogous Gene Group: 340 (11 members)

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0046835 - carbohydrate phosphorylation Inferred by computational analysis Inferred from experiment [Kneidinger02, GOA06]
GO:0005975 - carbohydrate metabolic process Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0008152 - metabolic process Inferred by computational analysis [UniProtGOA11a]
GO:0009058 - biosynthetic process Inferred by computational analysis [GOA01a]
GO:0009103 - lipopolysaccharide biosynthetic process Inferred by computational analysis [UniProtGOA11a]
GO:0009244 - lipopolysaccharide core region biosynthetic process Inferred by computational analysis [UniProtGOA12]
GO:0016310 - phosphorylation Inferred by computational analysis [UniProtGOA11a]
GO:0097171 - ADP-L-glycero-beta-D-manno-heptose biosynthetic process Inferred by computational analysis [UniProtGOA12]
Molecular Function: GO:0033785 - heptose 7-phosphate kinase activity Inferred from experiment Inferred by computational analysis [GOA06, Kneidinger02]
GO:0033786 - heptose-1-phosphate adenylyltransferase activity Inferred from experiment Inferred by computational analysis [GOA06, Kneidinger02]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11a]
GO:0003824 - catalytic activity Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0005524 - ATP binding Inferred by computational analysis [UniProtGOA11a, GOA06]
GO:0016301 - kinase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016773 - phosphotransferase activity, alcohol group as acceptor Inferred by computational analysis [GOA01a]
GO:0016779 - nucleotidyltransferase activity Inferred by computational analysis [UniProtGOA11a, GOA01a]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, LopezCampistrou05]

MultiFun Terms: metabolism biosynthesis of macromolecules (cellular constituents) lipopolysaccharide core region

Essentiality data for rfaE knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
Yes [Feist07, Comment 4]

Enzymatic reaction of: heptose 1-phosphate adenyltransferase

EC Number: 2.7.7.70

D-glycero-β-D-manno-heptose 1-phosphate + ATP + H+ <=> ADP-D-glycero-β-D-manno-heptose + diphosphate

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

In Pathways: ADP-L-glycero-β-D-manno-heptose biosynthesis


Enzymatic reaction of: heptose 7-phosphate kinase

EC Number: 2.7.1.167

D-glycero-D-manno-heptose 7-phosphate + ATP <=> D-glycero-β-D-manno-heptose 1,7-bisphosphate + ADP + H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

In Pathways: ADP-L-glycero-β-D-manno-heptose biosynthesis


Sequence Features

Feature Class Location Citations Comment
Protein-Segment 1 -> 318
[UniProt10]
UniProt: Ribokinase; Sequence Annotation Type: region of interest;
Acetylation-Modification 179
[Zhang09, UniProt11]
UniProt: N6-acetyllysine.
Mutagenesis-Variant 195
[McArthur05, UniProt11]
Alternate sequence: N → D; UniProt: Loss of activity.
Nucleotide-Phosphate-Binding-Region 195 -> 198
[UniProt10]
UniProt: ATP; Non-Experimental Qualifier: potential;
Mutagenesis-Variant 198
[McArthur05, UniProt11]
Alternate sequence: E → D; UniProt: Loss of activity.
Mutagenesis-Variant 264
[McArthur05, UniProt11]
Alternate sequence: D → N; UniProt: Loss of activity.
Alternate sequence: D → E; UniProt: Loss of activity.
Active-Site 264
[UniProt10]
UniProt: Non-Experimental Qualifier: potential;
Protein-Segment 344 -> 477
[UniProt10]
UniProt: Cytidylyltransferase; Sequence Annotation Type: region of interest;


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
Markus Krummenacker on Tue Oct 14, 1997:
Gene object created from Blattner lab Genbank (v. M52) entry.


References

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Feist07: Feist AM, Henry CS, Reed JL, Krummenacker M, Joyce AR, Karp PD, Broadbelt LJ, Hatzimanikatis V, Palsson BO (2007). "A genome-scale metabolic reconstruction for Escherichia coli K-12 MG1655 that accounts for 1260 ORFs and thermodynamic information." Mol Syst Biol 3;121. PMID: 17593909

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Ishihama08: Ishihama Y, Schmidt T, Rappsilber J, Mann M, Hartl FU, Kerner MJ, Frishman D (2008). "Protein abundance profiling of the Escherichia coli cytosol." BMC Genomics 9;102. PMID: 18304323

Joloba04: Joloba ML, Clemmer KM, Sledjeski DD, Rather PN (2004). "Activation of the gab operon in an RpoS-dependent manner by mutations that truncate the inner core of lipopolysaccharide in Escherichia coli." J Bacteriol 186(24);8542-6. PMID: 15576807

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Kneidinger02: Kneidinger B, Marolda C, Graninger M, Zamyatina A, McArthur F, Kosma P, Valvano MA, Messner P (2002). "Biosynthesis pathway of ADP-L-glycero-beta-D-manno-heptose in Escherichia coli." J Bacteriol 184(2);363-9. PMID: 11751812

LopezCampistrou05: Lopez-Campistrous A, Semchuk P, Burke L, Palmer-Stone T, Brokx SJ, Broderick G, Bottorff D, Bolch S, Weiner JH, Ellison MJ (2005). "Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth." Mol Cell Proteomics 4(8);1205-9. PMID: 15911532

McArthur05: McArthur F, Andersson CE, Loutet S, Mowbray SL, Valvano MA (2005). "Functional analysis of the glycero-manno-heptose 7-phosphate kinase domain from the bifunctional HldE protein, which is involved in ADP-L-glycero-D-manno-heptose biosynthesis." J Bacteriol 187(15);5292-300. PMID: 16030223

Sirisena92: Sirisena DM, Brozek KA, MacLachlan PR, Sanderson KE, Raetz CR (1992). "The rfaC gene of Salmonella typhimurium. Cloning, sequencing, and enzymatic function in heptose transfer to lipopolysaccharide." J Biol Chem 267(26);18874-84. PMID: 1527014

UniProt10: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProt11: UniProt Consortium (2011). "UniProt version 2011-06 released on 2011-06-30 00:00:00." Database.

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

UniProtGOA12: UniProt-GOA (2012). "Gene Ontology annotation based on UniPathway vocabulary mapping."

Valvano00: Valvano MA, Marolda CL, Bittner M, Glaskin-Clay M, Simon TL, Klena JD (2000). "The rfaE gene from Escherichia coli encodes a bifunctional protein involved in biosynthesis of the lipopolysaccharide core precursor ADP-L-glycero-D-manno-heptose." J Bacteriol 182(2);488-97. PMID: 10629197

Zhang09: Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y (2009). "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Mol Cell Proteomics 8(2);215-25. PMID: 18723842


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Wed Dec 17, 2014, BIOCYC14B.