HLDE_ACTPL
ID HLDE_ACTPL Reviewed; 475 AA.
AC Q8GLU7;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 73.
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;
OS Actinobacillus pleuropneumoniae (Haemophilus pleuropneumoniae).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=715;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ROLE IN LPS BIOSYNTHESIS.
RC STRAIN=ATCC 27088 / DSM 13472 / CCM 5869 / S4074 / Serotype 1;
RX PubMed=12798993; DOI=10.1016/s0378-1097(03)00247-7;
RA Provost M., Harel J., Labrie J., Sirois M., Jacques M.;
RT "Identification, cloning and characterization of rfaE of Actinobacillus
RT pleuropneumoniae serotype 1, a gene involved in lipopolysaccharide inner-
RT core biosynthesis.";
RL FEMS Microbiol. Lett. 223:7-14(2003).
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:0000305|PubMed:12798993}.
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:0000305|PubMed:12798993}.
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; LPS 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; AY127572; AAN02283.1; -; Genomic_DNA.
DR RefSeq; WP_005596429.1; NZ_CP030753.1.
DR AlphaFoldDB; Q8GLU7; -.
DR SMR; Q8GLU7; -.
DR STRING; 228399.appser1_4400; -.
DR GeneID; 66259262; -.
DR UniPathway; UPA00356; UER00437.
DR UniPathway; UPA00356; UER00439.
DR UniPathway; UPA00958; -.
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 ATP-binding; Carbohydrate metabolism; Kinase;
KW Lipopolysaccharide biosynthesis; Multifunctional enzyme;
KW Nucleotide-binding; Nucleotidyltransferase; Transferase.
FT CHAIN 1..475
FT /note="Bifunctional protein HldE"
FT /id="PRO_0000080101"
FT REGION 1..318
FT /note="Ribokinase"
FT REGION 344..475
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"
SQ SEQUENCE 475 AA; 51581 MW; 9F5CBF478CDF1633 CRC64;
MIQYSSKFNN AKVLVLGDVM LDRYWFGATN RISPEAPVPV VKVQGIEERA GGAANVAMNI
ASLSVPVALH GLIGQDDAGR ALDKLLNSHN IQNHCVALDS HPTITKLRIL SRHQQLLRLD
FEEGFHHVAS DSLLAKLEQE ITAYGALILS DYGKGTLESV QQMIQVARKA GVPTLIDPKG
TDFERYRGAT LLTPNMSEFE AVVGHCKDDD EIVEKGLKLI ADFELTALLV TRSEKGMTLL
RPNQAPFHLP TQAKEVYDVT GAGDTVISVL ATAIADGRPY EEACYLANAA AGVVVGKLGT
STVTPTELEN AIHHREETGF GILAEDELKR AVEQAKQRGE KIVMTNGCFD ILHPGHVSYL
ENARKLGDRL IVAVNTDESV KRLKGESRPI NDLNARMAVL AGLASVDWVV PFAEDTPQRL
IGEILPNLLV KGGDYKPEEI AGSQEVWANG GEVKVLNFEN GCSTTNVIKK IQASK
