HLDE_ECOLI
ID HLDE_ECOLI Reviewed; 477 AA.
AC P76658; Q2M9F3; Q6J1J5;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Bifunctional protein HldE;
DE Includes:
DE RecName: Full=D-beta-D-heptose 7-phosphate kinase;
DE EC=2.7.1.167;
DE AltName: Full=D-beta-D-heptose 7-phosphotransferase;
DE AltName: Full=D-glycero-beta-D-manno-heptose-7-phosphate kinase;
DE Includes:
DE RecName: Full=D-beta-D-heptose 1-phosphate adenylyltransferase;
DE EC=2.7.7.70;
DE AltName: Full=D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase;
GN Name=hldE; Synonyms=rfaE, waaE, yqiF; OrderedLocusNames=b3052, JW3024;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 461-477.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Perna N.T.;
RT "Escherichia coli K-12 MG1655 genomic sequence correction.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP DOMAINS.
RC STRAIN=K12 / ATCC 12435 / DSM 5695 / NBRC 3302 / NCIMB 9481 / W1485;
RX PubMed=10629197; DOI=10.1128/jb.182.2.488-497.2000;
RA Valvano M.A., Marolda C.L., Bittner M., Glaskin-Clay M., Simon T.L.,
RA Klena J.D.;
RT "The rfaE gene from Escherichia coli encodes a bifunctional protein
RT involved in the biosynthesis of the lipopolysaccharide core precursor ADP-
RT L-glycero-D-manno-heptose.";
RL J. Bacteriol. 182:488-497(2000).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND ADP-L-BETA-D-HEPTOSE BIOSYNTHESIS
RP PATHWAY.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=11751812; DOI=10.1128/jb.184.2.363-369.2002;
RA Kneidinger B., Marolda C., Graninger M., Zamyatina A., McArthur F.,
RA Kosma P., Valvano M.A., Messner P.;
RT "Biosynthesis pathway of ADP-L-glycero-beta-D-manno-heptose in Escherichia
RT coli.";
RL J. Bacteriol. 184:363-369(2002).
RN [6]
RP MUTAGENESIS OF ASN-195; GLU-198 AND ASP-264, AND SUBUNIT.
RX PubMed=16030223; DOI=10.1128/jb.187.15.5292-5300.2005;
RA McArthur F., Andersson C.E., Loutet S., Mowbray S.L., Valvano M.A.;
RT "Functional analysis of the glycero-manno-heptose 7-phosphate kinase domain
RT from the bifunctional HldE protein, which is involved in ADP-L-glycero-D-
RT manno-heptose biosynthesis.";
RL J. Bacteriol. 187:5292-5300(2005).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-179, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200;
RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA Grishin N.V., Zhao Y.;
RT "Lysine acetylation is a highly abundant and evolutionarily conserved
RT modification in Escherichia coli.";
RL Mol. Cell. Proteomics 8:215-225(2009).
CC -!- FUNCTION: Catalyzes the phosphorylation of D-glycero-D-manno-heptose 7-
CC phosphate at the C-1 position to selectively form D-glycero-beta-D-
CC manno-heptose-1,7-bisphosphate. {ECO:0000269|PubMed:11751812}.
CC -!- FUNCTION: Catalyzes the ADP transfer from ATP to D-glycero-beta-D-
CC manno-heptose 1-phosphate, yielding ADP-D-glycero-beta-D-manno-heptose.
CC {ECO:0000269|PubMed:11751812}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-glycero-beta-D-manno-heptose 7-phosphate = ADP + D-
CC glycero-beta-D-manno-heptose 1,7-bisphosphate + H(+);
CC Xref=Rhea:RHEA:27473, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:60204, ChEBI:CHEBI:60208, ChEBI:CHEBI:456216;
CC EC=2.7.1.167; Evidence={ECO:0000269|PubMed:11751812};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-glycero-beta-D-manno-heptose 1-phosphate + H(+) = ADP-
CC D-glycero-beta-D-manno-heptose + diphosphate; Xref=Rhea:RHEA:27465,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:59967, ChEBI:CHEBI:61593; EC=2.7.7.70;
CC Evidence={ECO:0000269|PubMed:11751812};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-
CC heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-
CC glycero-beta-D-manno-heptose 7-phosphate: step 1/4.
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-
CC heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-
CC glycero-beta-D-manno-heptose 7-phosphate: step 3/4.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16030223}.
CC -!- MISCELLANEOUS: In both reactions the enzyme functions only with beta
CC anomers.
CC -!- MISCELLANEOUS: The function of the domain II is independent from the
CC activity mediated by domain I.
CC -!- SIMILARITY: In the N-terminal section; belongs to the carbohydrate
CC kinase PfkB family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the
CC cytidylyltransferase family. {ECO:0000305}.
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DR EMBL; U00096; AAC76088.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77103.1; -; Genomic_DNA.
DR EMBL; AY605712; AAT28329.1; -; Genomic_DNA.
DR PIR; B65093; B65093.
DR RefSeq; NP_417524.1; NC_000913.3.
DR RefSeq; WP_000869178.1; NZ_STEB01000001.1.
DR AlphaFoldDB; P76658; -.
DR SMR; P76658; -.
DR BioGRID; 4261504; 430.
DR DIP; DIP-10666N; -.
DR IntAct; P76658; 6.
DR STRING; 511145.b3052; -.
DR iPTMnet; P76658; -.
DR jPOST; P76658; -.
DR PaxDb; P76658; -.
DR PRIDE; P76658; -.
DR EnsemblBacteria; AAC76088; AAC76088; b3052.
DR EnsemblBacteria; BAE77103; BAE77103; BAE77103.
DR GeneID; 66673049; -.
DR GeneID; 947548; -.
DR KEGG; ecj:JW3024; -.
DR KEGG; eco:b3052; -.
DR PATRIC; fig|1411691.4.peg.3679; -.
DR EchoBASE; EB3192; -.
DR eggNOG; COG0615; Bacteria.
DR eggNOG; COG2870; Bacteria.
DR HOGENOM; CLU_021150_2_1_6; -.
DR InParanoid; P76658; -.
DR OMA; CEFANAA; -.
DR PhylomeDB; P76658; -.
DR BioCyc; EcoCyc:G7590-MON; -.
DR BioCyc; MetaCyc:G7590-MON; -.
DR BRENDA; 2.7.1.167; 2026.
DR BRENDA; 2.7.7.70; 2026.
DR UniPathway; UPA00356; UER00437.
DR UniPathway; UPA00356; UER00439.
DR UniPathway; UPA00958; -.
DR PRO; PR:P76658; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0033785; F:heptose 7-phosphate kinase activity; IDA:EcoCyc.
DR GO; GO:0033786; F:heptose-1-phosphate adenylyltransferase activity; IDA:EcoCyc.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:InterPro.
DR GO; GO:0097171; P:ADP-L-glycero-beta-D-manno-heptose biosynthetic process; IMP:EcoCyc.
DR GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IMP:EcoCyc.
DR CDD; cd01172; RfaE_like; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_01603; HldE; 1.
DR InterPro; IPR023030; Bifunc_HldE.
DR InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR011611; PfkB_dom.
DR InterPro; IPR011913; RfaE_dom_I.
DR InterPro; IPR011914; RfaE_dom_II.
DR InterPro; IPR029056; Ribokinase-like.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF01467; CTP_transf_like; 1.
DR Pfam; PF00294; PfkB; 1.
DR SUPFAM; SSF53613; SSF53613; 1.
DR TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
DR TIGRFAMs; TIGR02198; rfaE_dom_I; 1.
DR TIGRFAMs; TIGR02199; rfaE_dom_II; 1.
DR PROSITE; PS00583; PFKB_KINASES_1; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Carbohydrate metabolism; Kinase;
KW Lipopolysaccharide biosynthesis; Multifunctional enzyme;
KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..477
FT /note="Bifunctional protein HldE"
FT /id="PRO_0000080107"
FT REGION 1..318
FT /note="Ribokinase"
FT REGION 344..477
FT /note="Cytidylyltransferase"
FT ACT_SITE 264
FT /evidence="ECO:0000255"
FT BINDING 195..198
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 179
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT MUTAGEN 195
FT /note="N->D: Loss of activity."
FT /evidence="ECO:0000269|PubMed:16030223"
FT MUTAGEN 198
FT /note="E->D: Loss of activity."
FT /evidence="ECO:0000269|PubMed:16030223"
FT MUTAGEN 264
FT /note="D->E: Loss of activity."
FT /evidence="ECO:0000269|PubMed:16030223"
FT MUTAGEN 264
FT /note="D->N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:16030223"
SQ SEQUENCE 477 AA; 51051 MW; 0F03CBE160B95389 CRC64;
MKVTLPEFER AGVMVVGDVM LDRYWYGPTS RISPEAPVPV VKVNTIEERP GGAANVAMNI
ASLGANARLV GLTGIDDAAR ALSKSLADVN VKCDFVSVPT HPTITKLRVL SRNQQLIRLD
FEEGFEGVDP QPLHERINQA LSSIGALVLS DYAKGALASV QQMIQLARKA GVPVLIDPKG
TDFERYRGAT LLTPNLSEFE AVVGKCKTEE EIVERGMKLI ADYELSALLV TRSEQGMSLL
QPGKAPLHMP TQAQEVYDVT GAGDTVIGVL AATLAAGNSL EEACFFANAA AGVVVGKLGT
STVSPIELEN AVRGRADTGF GVMTEEELKL AVAAARKRGE KVVMTNGVFD ILHAGHVSYL
ANARKLGDRL IVAVNSDAST KRLKGDSRPV NPLEQRMIVL GALEAVDWVV SFEEDTPQRL
IAGILPDLLV KGGDYKPEEI AGSKEVWANG GEVLVLNFED GCSTTNIIKK IQQDKKG
