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Protein

Bifunctional protein HldE

Gene

hldE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the phosphorylation of D-glycero-D-manno-heptose 7-phosphate at the C-1 position to selectively form D-glycero-beta-D-manno-heptose-1,7-bisphosphate.1 Publication
Catalyzes the ADP transfer from ATP to D-glycero-beta-D-manno-heptose 1-phosphate, yielding ADP-D-glycero-beta-D-manno-heptose.1 Publication

Catalytic activityi

D-glycero-beta-D-manno-heptose 7-phosphate + ATP = D-glycero-beta-D-manno-heptose 1,7-bisphosphate + ADP.1 Publication
D-glycero-beta-D-manno-heptose 1-phosphate + ATP = ADP-D-glycero-beta-D-manno-heptose + diphosphate.1 Publication

Pathwayi: ADP-L-glycero-beta-D-manno-heptose biosynthesis

This protein is involved in step 1 and 3 of the subpathway that synthesizes ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Bifunctional protein HldE (hldE)
  2. D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatase (gmhB)
  3. Bifunctional protein HldE (hldE)
  4. ADP-L-glycero-D-manno-heptose-6-epimerase (hldD)
This subpathway is part of the pathway ADP-L-glycero-beta-D-manno-heptose biosynthesis, which is itself part of Nucleotide-sugar biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate, the pathway ADP-L-glycero-beta-D-manno-heptose biosynthesis and in Nucleotide-sugar biosynthesis.

Pathwayi: LPS core biosynthesis

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei264 – 2641Sequence analysis

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi195 – 1984ATPSequence analysis

GO - Molecular functioni

GO - Biological processi

Keywords - Molecular functioni

Kinase, Nucleotidyltransferase, Transferase

Keywords - Biological processi

Carbohydrate metabolism, Lipopolysaccharide biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:G7590-MONOMER.
ECOL316407:JW3024-MONOMER.
MetaCyc:G7590-MONOMER.
BRENDAi2.7.1.167. 2026.
2.7.7.70. 2026.
UniPathwayiUPA00356; UER00437.
UPA00356; UER00439.
UPA00958.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional protein HldE
Including the following 2 domains:
D-beta-D-heptose 7-phosphate kinase (EC:2.7.1.167)
Alternative name(s):
D-beta-D-heptose 7-phosphotransferase
D-glycero-beta-D-manno-heptose-7-phosphate kinase
D-beta-D-heptose 1-phosphate adenylyltransferase (EC:2.7.7.70)
Alternative name(s):
D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase
Gene namesi
Name:hldE
Synonyms:rfaE, waaE, yqiF
Ordered Locus Names:b3052, JW3024
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13416. hldE.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi195 – 1951N → D: Loss of activity. 1 Publication
Mutagenesisi198 – 1981E → D: Loss of activity. 1 Publication
Mutagenesisi264 – 2641D → E: Loss of activity. 1 Publication
Mutagenesisi264 – 2641D → N: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 477477Bifunctional protein HldEPRO_0000080107Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei179 – 1791N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP76658.
PaxDbiP76658.
PRIDEiP76658.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi4261504. 425 interactions.
DIPiDIP-10666N.
STRINGi511145.b3052.

Structurei

3D structure databases

ProteinModelPortaliP76658.
SMRiP76658. Positions 7-308, 341-471.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 318318RibokinaseAdd
BLAST
Regioni344 – 477134CytidylyltransferaseAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the carbohydrate kinase PfkB family.Curated
In the C-terminal section; belongs to the cytidylyltransferase family.Curated

Phylogenomic databases

eggNOGiENOG4105DW0. Bacteria.
COG2870. LUCA.
HOGENOMiHOG000237584.
InParanoidiP76658.
KOiK03272.
OMAiEACYLAN.
OrthoDBiEOG68Q0W4.
PhylomeDBiP76658.

Family and domain databases

Gene3Di3.40.1190.20. 1 hit.
3.40.50.620. 1 hit.
HAMAPiMF_01603. HldE.
InterProiIPR023030. Bifunc_HldE.
IPR002173. Carboh/pur_kinase_PfkB_CS.
IPR004821. Cyt_trans-like.
IPR011611. PfkB_dom.
IPR011913. RfaE_dom_I.
IPR011914. RfaE_dom_II.
IPR029056. Ribokinase-like.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF01467. CTP_transf_like. 1 hit.
PF00294. PfkB. 1 hit.
[Graphical view]
SUPFAMiSSF53613. SSF53613. 1 hit.
TIGRFAMsiTIGR00125. cyt_tran_rel. 1 hit.
TIGR02198. rfaE_dom_I. 1 hit.
TIGR02199. rfaE_dom_II. 1 hit.
PROSITEiPS00583. PFKB_KINASES_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P76658-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVTLPEFER AGVMVVGDVM LDRYWYGPTS RISPEAPVPV VKVNTIEERP
60 70 80 90 100
GGAANVAMNI ASLGANARLV GLTGIDDAAR ALSKSLADVN VKCDFVSVPT
110 120 130 140 150
HPTITKLRVL SRNQQLIRLD FEEGFEGVDP QPLHERINQA LSSIGALVLS
160 170 180 190 200
DYAKGALASV QQMIQLARKA GVPVLIDPKG TDFERYRGAT LLTPNLSEFE
210 220 230 240 250
AVVGKCKTEE EIVERGMKLI ADYELSALLV TRSEQGMSLL QPGKAPLHMP
260 270 280 290 300
TQAQEVYDVT GAGDTVIGVL AATLAAGNSL EEACFFANAA AGVVVGKLGT
310 320 330 340 350
STVSPIELEN AVRGRADTGF GVMTEEELKL AVAAARKRGE KVVMTNGVFD
360 370 380 390 400
ILHAGHVSYL ANARKLGDRL IVAVNSDAST KRLKGDSRPV NPLEQRMIVL
410 420 430 440 450
GALEAVDWVV SFEEDTPQRL IAGILPDLLV KGGDYKPEEI AGSKEVWANG
460 470
GEVLVLNFED GCSTTNIIKK IQQDKKG
Length:477
Mass (Da):51,051
Last modified:February 1, 1997 - v1
Checksum:i0F03CBE160B95389
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC76088.1.
AP009048 Genomic DNA. Translation: BAE77103.1.
AY605712 Genomic DNA. Translation: AAT28329.1.
PIRiB65093.
RefSeqiNP_417524.1. NC_000913.3.
WP_000869178.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76088; AAC76088; b3052.
BAE77103; BAE77103; BAE77103.
GeneIDi947548.
KEGGiecj:JW3024.
eco:b3052.
PATRICi32121516. VBIEscCol129921_3145.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC76088.1.
AP009048 Genomic DNA. Translation: BAE77103.1.
AY605712 Genomic DNA. Translation: AAT28329.1.
PIRiB65093.
RefSeqiNP_417524.1. NC_000913.3.
WP_000869178.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP76658.
SMRiP76658. Positions 7-308, 341-471.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261504. 425 interactions.
DIPiDIP-10666N.
STRINGi511145.b3052.

Proteomic databases

EPDiP76658.
PaxDbiP76658.
PRIDEiP76658.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76088; AAC76088; b3052.
BAE77103; BAE77103; BAE77103.
GeneIDi947548.
KEGGiecj:JW3024.
eco:b3052.
PATRICi32121516. VBIEscCol129921_3145.

Organism-specific databases

EchoBASEiEB3192.
EcoGeneiEG13416. hldE.

Phylogenomic databases

eggNOGiENOG4105DW0. Bacteria.
COG2870. LUCA.
HOGENOMiHOG000237584.
InParanoidiP76658.
KOiK03272.
OMAiEACYLAN.
OrthoDBiEOG68Q0W4.
PhylomeDBiP76658.

Enzyme and pathway databases

UniPathwayiUPA00356; UER00437.
UPA00356; UER00439.
UPA00958.
BioCyciEcoCyc:G7590-MONOMER.
ECOL316407:JW3024-MONOMER.
MetaCyc:G7590-MONOMER.
BRENDAi2.7.1.167. 2026.
2.7.7.70. 2026.

Miscellaneous databases

PROiP76658.

Family and domain databases

Gene3Di3.40.1190.20. 1 hit.
3.40.50.620. 1 hit.
HAMAPiMF_01603. HldE.
InterProiIPR023030. Bifunc_HldE.
IPR002173. Carboh/pur_kinase_PfkB_CS.
IPR004821. Cyt_trans-like.
IPR011611. PfkB_dom.
IPR011913. RfaE_dom_I.
IPR011914. RfaE_dom_II.
IPR029056. Ribokinase-like.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF01467. CTP_transf_like. 1 hit.
PF00294. PfkB. 1 hit.
[Graphical view]
SUPFAMiSSF53613. SSF53613. 1 hit.
TIGRFAMsiTIGR00125. cyt_tran_rel. 1 hit.
TIGR02198. rfaE_dom_I. 1 hit.
TIGR02199. rfaE_dom_II. 1 hit.
PROSITEiPS00583. PFKB_KINASES_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  2. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. "Escherichia coli K-12 MG1655 genomic sequence correction."
    Perna N.T.
    Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 461-477.
    Strain: K12 / MG1655 / ATCC 47076.
  4. "The rfaE gene from Escherichia coli encodes a bifunctional protein involved in the biosynthesis of the lipopolysaccharide core precursor ADP-L-glycero-D-manno-heptose."
    Valvano M.A., Marolda C.L., Bittner M., Glaskin-Clay M., Simon T.L., Klena J.D.
    J. Bacteriol. 182:488-497(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAINS.
    Strain: K12 / W1485.
  5. "Biosynthesis pathway of ADP-L-glycero-beta-D-manno-heptose in Escherichia coli."
    Kneidinger B., Marolda C., Graninger M., Zamyatina A., McArthur F., Kosma P., Valvano M.A., Messner P.
    J. Bacteriol. 184:363-369(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, ADP-L-BETA-D-HEPTOSE BIOSYNTHESIS PATHWAY.
    Strain: K12 / MG1655 / ATCC 47076.
  6. "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."
    McArthur F., Andersson C.E., Loutet S., Mowbray S.L., Valvano M.A.
    J. Bacteriol. 187:5292-5300(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ASN-195; GLU-198 AND ASP-264, SUBUNIT.
  7. "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
    Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
    Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-179, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.

Entry informationi

Entry nameiHLDE_ECOLI
AccessioniPrimary (citable) accession number: P76658
Secondary accession number(s): Q2M9F3, Q6J1J5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: February 1, 1997
Last modified: March 16, 2016
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

In both reactions the enzyme functions only with beta anomers.
The function of the domain II is independent from the activity mediated by domain I.

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.