HLDE_CAMJE
ID HLDE_CAMJE Reviewed; 461 AA.
AC Q6TG09; Q0P9A6; Q7BPS3; Q9PNE5;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 2.
DT 03-AUG-2022, entry version 99.
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=waaE; OrderedLocusNames=Cj1150c;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43446 / MK104 / Serotype O:19;
RA Gilbert M.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=GB11;
RX PubMed=14742567; DOI=10.1128/iai.72.2.1162-1165.2004;
RA Gilbert M., Godschalk P.C., Karwaski M.-F., Ang C.W., Van Belkum A., Li J.,
RA Wakarchuk W.W., Endtz H.P.;
RT "Evidence for acquisition of the lipooligosaccharide biosynthesis locus in
RT Campylobacter jejuni GB11, a strain isolated from a patient with Guillain-
RT Barre syndrome, by horizontal exchange.";
RL Infect. Immun. 72:1162-1165(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
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:0000250}.
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:0000250}.
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;
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 -!- 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; LOS core biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
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; AF167344; AAR99165.1; -; Genomic_DNA.
DR EMBL; AY422197; AAR82883.1; -; Genomic_DNA.
DR EMBL; AL111168; CAL35265.1; -; Genomic_DNA.
DR PIR; H81319; H81319.
DR RefSeq; WP_002858114.1; NC_002163.1.
DR RefSeq; YP_002344541.1; NC_002163.1.
DR AlphaFoldDB; Q6TG09; -.
DR SMR; Q6TG09; -.
DR STRING; 192222.Cj1150c; -.
DR PaxDb; Q6TG09; -.
DR PRIDE; Q6TG09; -.
DR DNASU; 905440; -.
DR EnsemblBacteria; CAL35265; CAL35265; Cj1150c.
DR GeneID; 905440; -.
DR KEGG; cje:Cj1150c; -.
DR PATRIC; fig|192222.6.peg.1131; -.
DR eggNOG; COG0615; Bacteria.
DR eggNOG; COG2870; Bacteria.
DR HOGENOM; CLU_021150_2_1_7; -.
DR OMA; CEFANAA; -.
DR UniPathway; UPA00356; UER00437.
DR UniPathway; UPA00356; UER00439.
DR UniPathway; UPA00976; -.
DR Proteomes; UP000000799; 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 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; 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.
PE 3: Inferred from homology;
KW ATP-binding; Carbohydrate metabolism; Kinase; Multifunctional enzyme;
KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..461
FT /note="Bifunctional protein HldE"
FT /id="PRO_0000080103"
FT REGION 1..312
FT /note="Ribokinase"
FT REGION 334..461
FT /note="Cytidylyltransferase"
FT ACT_SITE 259
FT /evidence="ECO:0000255"
FT BINDING 191..194
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 39
FT /note="I -> V (in Ref. 1; AAR99165 and 2; AAR82883)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="A -> T (in Ref. 2; AAR82883)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="S -> N (in Ref. 1; AAR99165)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="E -> K (in Ref. 2; AAR82883)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="E -> A (in Ref. 1; AAR99165 and 2; AAR82883)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="V -> I (in Ref. 1; AAR99165)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="E -> K (in Ref. 2; AAR82883)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="V -> A (in Ref. 1; AAR99165 and 2; AAR82883)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="N -> S (in Ref. 1; AAR99165 and 2; AAR82883)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="K -> KEAL (in Ref. 1; AAR99165)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="S -> A (in Ref. 1; AAR99165 and 2; AAR82883)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="E -> G (in Ref. 1; AAR99165)"
FT /evidence="ECO:0000305"
FT CONFLICT 305..307
FT /note="SFK -> NFN (in Ref. 2; AAR82883)"
FT /evidence="ECO:0000305"
FT CONFLICT 317
FT /note="S -> N (in Ref. 1; AAR99165)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="V -> M (in Ref. 1; AAR99165)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="V -> T (in Ref. 2; AAR82883)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="N -> D (in Ref. 1; AAR99165 and 2; AAR82883)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="D -> E (in Ref. 1; AAR99165 and 2; AAR82883)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="I -> V (in Ref. 1; AAR99165)"
FT /evidence="ECO:0000305"
FT CONFLICT 401
FT /note="I -> V (in Ref. 1; AAR99165)"
FT /evidence="ECO:0000305"
FT CONFLICT 429
FT /note="L -> I (in Ref. 2; AAR82883)"
FT /evidence="ECO:0000305"
FT CONFLICT 438
FT /note="R -> K (in Ref. 2; AAR82883)"
FT /evidence="ECO:0000305"
FT CONFLICT 438
FT /note="R -> N (in Ref. 1; AAR99165)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 461 AA; 51238 MW; 490D9FDB4EB58322 CRC64;
MLEFLSQQKP KILIIGDFMV DNYTWCDCSR ISPEAPVLIA KTLKEDKRLG GAANVYANLK
SLGADVFALG VVGDDESGKF LQENLKGEFL IQKGRKTPFK NRIMAHNQQV LRLDEEDISE
ILLENELIAL FDEKIKDFKA VVLSDYAKGV LTPKVCKAVI EKAKVLNIPV LVDPKGSDFN
KYSGATLLTP NKKEALEALK FENLEGENLE KGIKKLKEDF SLRYSIITLS EAGIALFDEG
LKIAPAKALE VYDVTGAGDS VIAVLAFCLA NEIEIFKACE LANEAAAVVV SKIGSVSVSF
DEIKSFKRVD FEKKIKSKEE LLVLLKQNNK KIVFTNGCFD IVHFGHIKYL DKAKRLGDVL
IVGLNSDASV KRLKGESRPV NSEFQRACML AAFYFVDFVV IFDEDTPLEL ISFLKPDILV
KGADYKDKLV VGADIVSRVE LIDFEEGFST SKIIEKIKDK K
