ID HLDE_RHOPA Reviewed; 490 AA. AC Q6N2R5; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 07-JUN-2017, entry version 74. 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}; Synonyms=rfaE; GN OrderedLocusNames=RPA3984; OS Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Rhodopseudomonas. OX NCBI_TaxID=258594; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-98 / CGA009; RX PubMed=14704707; DOI=10.1038/nbt923; RA Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L., RA Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R., RA Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C., RA Harrison F.H., Gibson J., Harwood C.S.; RT "Complete genome sequence of the metabolically versatile RT photosynthetic bacterium Rhodopseudomonas palustris."; RL Nat. Biotechnol. 22:55-61(2004). CC -!- FUNCTION: Catalyzes the phosphorylation of D-glycero-D-manno- CC heptose 7-phosphate at the C-1 position to selectively form D- CC glycero-beta-D-manno-heptose-1,7-bisphosphate. {ECO:0000255|HAMAP- CC 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- CC heptose. {ECO:0000255|HAMAP-Rule:MF_01603}. CC -!- CATALYTIC ACTIVITY: D-glycero-beta-D-manno-heptose 7-phosphate + CC ATP = D-glycero-beta-D-manno-heptose 1,7-bisphosphate + ADP. CC {ECO:0000255|HAMAP-Rule:MF_01603}. CC -!- CATALYTIC ACTIVITY: D-glycero-beta-D-manno-heptose 1-phosphate + CC ATP = ADP-D-glycero-beta-D-manno-heptose + diphosphate. CC {ECO:0000255|HAMAP-Rule:MF_01603}. CC -!- PATHWAY: Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D- CC manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose CC from D-glycero-beta-D-manno-heptose 7-phosphate: step 1/4. CC {ECO:0000255|HAMAP-Rule:MF_01603}. CC -!- PATHWAY: Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D- CC manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose CC from D-glycero-beta-D-manno-heptose 7-phosphate: step 3/4. CC {ECO:0000255|HAMAP-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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BX572605; CAE29425.1; -; Genomic_DNA. DR RefSeq; WP_011159520.1; NC_005296.1. DR ProteinModelPortal; Q6N2R5; -. DR SMR; Q6N2R5; -. DR STRING; 258594.RPA3984; -. DR EnsemblBacteria; CAE29425; CAE29425; RPA3984. DR KEGG; rpa:RPA3984; -. DR eggNOG; ENOG4105DW0; Bacteria. DR eggNOG; COG2870; LUCA. DR HOGENOM; HOG000237584; -. DR KO; K03272; -. DR OMA; CDPKGKD; -. DR OrthoDB; POG091H01Y4; -. DR PhylomeDB; Q6N2R5; -. DR UniPathway; UPA00356; UER00437. DR UniPathway; UPA00356; UER00439. DR Proteomes; UP000001426; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW. 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:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW. 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; Complete proteome; Kinase; KW Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase; KW Reference proteome; Transferase. FT CHAIN 1 490 Bifunctional protein HldE. FT /FTId=PRO_0000080123. FT NP_BIND 205 208 ATP. {ECO:0000255|HAMAP-Rule:MF_01603}. FT REGION 1 330 Ribokinase. FT REGION 358 490 Cytidylyltransferase. FT ACT_SITE 275 275 {ECO:0000255|HAMAP-Rule:MF_01603}. SQ SEQUENCE 490 AA; 52131 MW; E9E281E226F4FF60 CRC64; MFSFDALLQA IARQTVLCVG DLMLDEFVYG EVSRISPEAP APVIAVQRSE TNIGGAGNVA RNIAAIGARC IFVGLIGDDA TGRFLESELG SESRIEPVLV CDGSRPTTRK VRFVSEHFST HMLRADWETA SPAAADIEQR LLDAILPQLA RADIVLLSDY AKGVLTARVI RDTIDAAKKL GKRVIVDPKS ANFAIYRGAT LLTPNRKEFT AATRSAAATD DEIAAAAQDA MALAECEAML VTKSEHGMTL VPRGGEPIHV PALPVKVRDV SGAGDTVAAV LAVVLASGAN WATAMRAASA AAAVAVSKNG TAVVTPAELR RRILPHASLA AEEKIIGSDE ELDERLKQWR REGLRVGFTN GCFDILHPGH VKVLTAARGA CDRLIVGLNS DASVRRLKGE SRPVQHERAR AEVLAALEAV DLVAIFEEDT PLRLITRIEP SVLVKGGDYT REQVVGHEIV AAKGGDVLLV DVLPGFSTTS LVARAREGQS //