HLDE_ECO57
ID HLDE_ECO57 Reviewed; 477 AA.
AC Q7AAQ7; Q8XBM4;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Bifunctional protein HldE {ECO:0000255|HAMAP-Rule:MF_01603};
DE Includes:
DE RecName: Full=D-beta-D-heptose 7-phosphate kinase {ECO:0000255|HAMAP-Rule:MF_01603};
DE EC=2.7.1.167 {ECO:0000255|HAMAP-Rule:MF_01603};
DE AltName: Full=D-beta-D-heptose 7-phosphotransferase {ECO:0000255|HAMAP-Rule:MF_01603};
DE AltName: Full=D-glycero-beta-D-manno-heptose-7-phosphate kinase {ECO:0000255|HAMAP-Rule:MF_01603};
DE Includes:
DE RecName: Full=D-beta-D-heptose 1-phosphate adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_01603};
DE EC=2.7.7.70 {ECO:0000255|HAMAP-Rule:MF_01603};
DE AltName: Full=D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_01603};
GN Name=hldE {ECO:0000255|HAMAP-Rule:MF_01603}; Synonyms=rfaE;
GN OrderedLocusNames=Z4405, ECs3935;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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:0000255|HAMAP-Rule:MF_01603}.
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:0000255|HAMAP-Rule:MF_01603}.
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:0000255|HAMAP-Rule:MF_01603};
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:0000255|HAMAP-Rule:MF_01603};
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. {ECO:0000255|HAMAP-
CC Rule:MF_01603}.
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. {ECO:0000255|HAMAP-
CC Rule:MF_01603}.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01603}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the carbohydrate
CC kinase PfkB family. {ECO:0000255|HAMAP-Rule:MF_01603}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the
CC cytidylyltransferase family. {ECO:0000255|HAMAP-Rule:MF_01603}.
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DR EMBL; AE005174; AAG58186.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB37358.1; -; Genomic_DNA.
DR PIR; F85965; F85965.
DR PIR; G91120; G91120.
DR RefSeq; NP_311962.1; NC_002695.1.
DR RefSeq; WP_000869160.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; Q7AAQ7; -.
DR SMR; Q7AAQ7; -.
DR STRING; 155864.EDL933_4272; -.
DR EnsemblBacteria; AAG58186; AAG58186; Z4405.
DR EnsemblBacteria; BAB37358; BAB37358; ECs_3935.
DR GeneID; 916240; -.
DR KEGG; ece:Z4405; -.
DR KEGG; ecs:ECs_3935; -.
DR PATRIC; fig|386585.9.peg.4103; -.
DR eggNOG; COG0615; Bacteria.
DR eggNOG; COG2870; Bacteria.
DR HOGENOM; CLU_021150_2_1_6; -.
DR OMA; CEFANAA; -.
DR UniPathway; UPA00356; UER00437.
DR UniPathway; UPA00356; UER00439.
DR UniPathway; UPA00958; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0033785; F:heptose 7-phosphate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0033786; F:heptose-1-phosphate adenylyltransferase activity; IEA:UniProtKB-UniRule.
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; IEA:UniProtKB-UniPathway.
DR GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IEA:UniProtKB-UniPathway.
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 3: Inferred from homology;
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_0000080108"
FT REGION 1..318
FT /note="Ribokinase"
FT REGION 344..477
FT /note="Cytidylyltransferase"
FT ACT_SITE 264
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01603"
FT BINDING 195..198
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01603"
FT MOD_RES 179
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01603"
SQ SEQUENCE 477 AA; 51065 MW; BB877FEF6636E67C CRC64;
MKVTLPEFER AGVMVVGDVM LDRYWYGPSS 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 AVVAARKRGE KVVMTNGVFD ILHAGHVSYL
ANARKLGDRL IVAVNSDAST KRLKGDSRPV NPLEQRMIVL GALEAVDWVV SFEEDTPQRL
IAGILPDLLV KGGDYKPEEI AGSKEVWANG GEVLVLNFED GCSTTNIIKK IQQDKKG
