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HLDE_ACTP2
ID   HLDE_ACTP2              Reviewed;         475 AA.
AC   A3MZC0;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 2.
DT   03-AUG-2022, entry version 89.
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}; OrderedLocusNames=APL_0402;
OS   Actinobacillus pleuropneumoniae serotype 5b (strain L20).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=416269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L20;
RX   PubMed=18065534; DOI=10.1128/jb.01845-07;
RA   Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M.,
RA   Nash J.H.E.;
RT   "The complete genome sequence of Actinobacillus pleuropneumoniae L20
RT   (serotype 5b).";
RL   J. Bacteriol. 190:1495-1496(2008).
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   -!- 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABN73506.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000569; ABN73506.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; A3MZC0; -.
DR   SMR; A3MZC0; -.
DR   STRING; 416269.APL_0402; -.
DR   EnsemblBacteria; ABN73506; ABN73506; APL_0402.
DR   KEGG; apl:APL_0402; -.
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   Proteomes; UP000001432; 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; 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; Multifunctional enzyme;
KW   Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..475
FT                   /note="Bifunctional protein HldE"
FT                   /id="PRO_0000291666"
FT   REGION          1..318
FT                   /note="Ribokinase"
FT   REGION          344..475
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"
SQ   SEQUENCE   475 AA;  51667 MW;  FC65D9C9BF3EDE73 CRC64;
     MMQYSPKFNN AKVLVLGDVM LDRYWFGATN RISPEAPVPV VKVQDIEERA 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
 
 
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