(data stored in ACNUC7421 zone)

SWISSPROT: HLDE_PSEPF

ID   HLDE_PSEPF              Reviewed;         474 AA.
AC   Q3KJ28;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   11-DEC-2019, entry version 97.
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=Pfl01_0484;
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1;
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(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: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}.
DR   EMBL; CP000094; ABA72228.1; -; Genomic_DNA.
DR   RefSeq; WP_011332149.1; NC_007492.2.
DR   SMR; Q3KJ28; -.
DR   STRING; 205922.Pfl01_0484; -.
DR   PRIDE; Q3KJ28; -.
DR   EnsemblBacteria; ABA72228; ABA72228; Pfl01_0484.
DR   KEGG; pfo:Pfl01_0484; -.
DR   eggNOG; ENOG4105DW0; Bacteria.
DR   eggNOG; COG2870; LUCA.
DR   HOGENOM; HOG000237584; -.
DR   KO; K03272; -.
DR   OMA; CEFANAA; -.
DR   BioCyc; PFLU205922:G1G4S-489-MONOMER; -.
DR   UniPathway; UPA00356; UER00437.
DR   UniPathway; UPA00356; UER00439.
DR   Proteomes; UP000002704; 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;
DR   PRODOM; Q3KJ28.
DR   SWISS-2DPAGE; Q3KJ28.
KW   ATP-binding; Carbohydrate metabolism; Kinase; Multifunctional enzyme;
KW   Nucleotide-binding; Nucleotidyltransferase; Transferase.
FT   CHAIN           1..474
FT                   /note="Bifunctional protein HldE"
FT                   /id="PRO_0000255774"
FT   NP_BIND         194..197
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01603"
FT   REGION          1..318
FT                   /note="Ribokinase"
FT   REGION          343..474
FT                   /note="Cytidylyltransferase"
FT   ACT_SITE        263
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01603"
SQ   SEQUENCE   474 AA;  49975 MW;  D40B10A42AB6BDFE CRC64;
     MKLSMPRFDQ APVLVVGDVM LDRYWHGGTS RISPEAPVPV VKVEQIEDRP GGAANVALNI
     AALGAPASLV GVTGDDEAAD SLSNSLKGAG VRALFQRIAH QPTIVKLRVM SRHQQLLRID
     FEEPFATDAL ALGAQVDDLL EGIKVLVLSD YGKGALKNHQ ALIQAARAKG IPVLADPKGK
     DFSIYRGASL ITPNLSEFEA IVGGCADEHE LVTKGATLMH DLDLGALLVT RGEHGMTLLR
     PDHPALHLPA RAREVFDVTG AGDTVISTLA AAIAAGEELP HAVALANLAA GIVVGKLGTA
     AISAPELRRA IQREEGSERG VLGLEQLLLA VADARAHNEK IVFTNGCFDI LHAGHVTYLE
     QARAQGDRLI VAINDDASVS RLKGPGRPIN SVDRRMAVLA GLGAVDWVIS FAEGTPENLL
     REVKPDVLVK GGDYGIDQVV GADIVKAYGG AVKVLGLVEN SSTTAIVEKI RKSE
//

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