HLDE_PSEPG
ID HLDE_PSEPG Reviewed; 473 AA.
AC B0KL32;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
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};
GN OrderedLocusNames=PputGB1_4983;
OS Pseudomonas putida (strain GB-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=76869;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O., Brettin T.,
RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.;
RT "Complete sequence of Pseudomonas putida GB-1.";
RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP000926; ABZ00868.1; -; Genomic_DNA.
DR RefSeq; WP_012274494.1; NC_010322.1.
DR AlphaFoldDB; B0KL32; -.
DR SMR; B0KL32; -.
DR STRING; 76869.PputGB1_4983; -.
DR EnsemblBacteria; ABZ00868; ABZ00868; PputGB1_4983.
DR KEGG; ppg:PputGB1_4983; -.
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; UP000002157; 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; Transferase.
FT CHAIN 1..473
FT /note="Bifunctional protein HldE"
FT /id="PRO_1000088023"
FT REGION 1..318
FT /note="Ribokinase"
FT REGION 343..473
FT /note="Cytidylyltransferase"
FT ACT_SITE 263
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01603"
FT BINDING 194..197
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01603"
SQ SEQUENCE 473 AA; 50003 MW; 5825CE782CAB9305 CRC64;
MKLSMPRFDQ APVLVVGDVM LDRYWHGGTS RISPEAPVPV VKVDQIEDRP GGAANVALNI
AALGAPASLI GVTGQDEAAD SLANSLQAAG VRSVFQRIAH QPTIVKLRVM SRHQQLLRID
FEEPFATDPL SLATEVDSLL EGVKVLVLSD YGKGALKNHQ SLIQAARAKG IPVLADPKGK
DFSIYRGASL ITPNLSEFET IVGRCTDEAD LVAKGLQLLQ DLDLGALLVT RGEHGMTLLR
VGQPALHLPA RAREVFDVTG AGDTVISTLA AAIAAGEDLP HAVALANLAA GIVVGKLGTA
AISAPELRRA IQREEGSERG VLGLEQLLLA IDDARAHKEK IVFTNGCFDI LHAGHVTYLE
QARAQGDRLI VAVNDDASVS RLKGPGRPIN SVDRRMAVLA GLGAVDWVIS FPEGTPENLL
SQVKPDVLVK GGDYGIDQVV GADIVKAYGG TVKVLGLVEN SSTTAIVEKI RKN
