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MetaCyc Enzyme: fused heptose 7-phosphate kinase/heptose 1-phosphate adenyltransferase

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

Synonyms: yqiF, hldE, gmhC, waaE

Species: Escherichia coli K-12 substr. MG1655

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]

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

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 [UniProtGOA11, GOA01]
GO:0008152 - metabolic process Inferred by computational analysis [UniProtGOA11]
GO:0009058 - biosynthetic process Inferred by computational analysis [GOA01]
GO:0009103 - lipopolysaccharide biosynthetic process Inferred by computational analysis [UniProtGOA11]
GO:0009244 - lipopolysaccharide core region biosynthetic process Inferred by computational analysis [UniProtGOA12]
GO:0016310 - phosphorylation Inferred by computational analysis [UniProtGOA11]
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 [UniProtGOA11]
GO:0003824 - catalytic activity Inferred by computational analysis [UniProtGOA11, GOA01]
GO:0005524 - ATP binding Inferred by computational analysis [UniProtGOA11, GOA06]
GO:0016301 - kinase activity Inferred by computational analysis [UniProtGOA11]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11]
GO:0016773 - phosphotransferase activity, alcohol group as acceptor Inferred by computational analysis [GOA01]
GO:0016779 - nucleotidyltransferase activity Inferred by computational analysis [UniProtGOA11, GOA01]
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

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


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

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


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

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Sequence Features

Feature Class Location Citations Comment
Protein-Segment 1 -> 318
[UniProt10a]
UniProt: Ribokinase; Sequence Annotation Type: region of interest;
Acetylation-Modification 179
[Zhang09, UniProt11a]
UniProt: N6-acetyllysine.
Mutagenesis-Variant 195
[McArthur05, UniProt11a]
Alternate sequence: D; UniProt: Loss of activity.
Nucleotide-Phosphate-Binding-Region 195 -> 198
[UniProt10a]
UniProt: ATP; Non-Experimental Qualifier: potential;
Mutagenesis-Variant 198
[McArthur05, UniProt11a]
Alternate sequence: D; UniProt: Loss of activity.
Mutagenesis-Variant 264
[McArthur05, UniProt11a]
Alternate sequence: N; UniProt: Loss of activity.
Alternate sequence: E; UniProt: Loss of activity.
Active-Site 264
[UniProt10a]
UniProt: Non-Experimental Qualifier: potential;
Protein-Segment 344 -> 477
[UniProt10a]
UniProt: Cytidylyltransferase; Sequence Annotation Type: region of interest;

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


References

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

GOA01: 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

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

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProt11a: UniProt Consortium (2011). "UniProt version 2011-06 released on 2011-06-30 00:00:00." Database.

UniProtGOA11: 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 MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Thu Nov 20, 2014, BIOCYC14A.