ID A0A2T5I8D4_9PROT Unreviewed; 491 AA. AC A0A2T5I8D4; DT 18-JUL-2018, integrated into UniProtKB/TrEMBL. DT 18-JUL-2018, sequence version 1. DT 13-SEP-2023, entry version 19. DE RecName: Full=Bifunctional protein HldE {ECO:0000256|HAMAP-Rule:MF_01603}; DE Includes: DE RecName: Full=D-beta-D-heptose 7-phosphate kinase {ECO:0000256|HAMAP-Rule:MF_01603}; DE EC=2.7.1.167 {ECO:0000256|HAMAP-Rule:MF_01603}; DE AltName: Full=D-beta-D-heptose 7-phosphotransferase {ECO:0000256|HAMAP-Rule:MF_01603}; DE AltName: Full=D-glycero-beta-D-manno-heptose-7-phosphate kinase {ECO:0000256|HAMAP-Rule:MF_01603}; DE Includes: DE RecName: Full=D-beta-D-heptose 1-phosphate adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_01603}; DE EC=2.7.7.70 {ECO:0000256|HAMAP-Rule:MF_01603}; DE AltName: Full=D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_01603}; GN Name=hldE {ECO:0000256|HAMAP-Rule:MF_01603}; GN ORFNames=C8R21_11914 {ECO:0000313|EMBL:PTQ80077.1}; OS Nitrosospira multiformis. OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales; OC Nitrosomonadaceae; Nitrosospira. OX NCBI_TaxID=1231 {ECO:0000313|EMBL:PTQ80077.1, ECO:0000313|Proteomes:UP000244152}; RN [1] {ECO:0000313|EMBL:PTQ80077.1, ECO:0000313|Proteomes:UP000244152} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Nl12 {ECO:0000313|EMBL:PTQ80077.1, RC ECO:0000313|Proteomes:UP000244152}; RA Wagner M.; RT "Active sludge and wastewater microbial communities from Klosterneuburg, RT Austria."; RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases. 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:0000256|HAMAP-Rule:MF_01603}. 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:0000256|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:0000256|ARBA:ARBA00000534, ECO:0000256|HAMAP- CC 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:0000256|HAMAP-Rule:MF_01603}; CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis. CC {ECO:0000256|ARBA:ARBA00004713}. 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:0000256|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:0000256|HAMAP- CC Rule:MF_01603}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01603}. CC -!- SIMILARITY: In the C-terminal section; belongs to the CC cytidylyltransferase family. {ECO:0000256|HAMAP-Rule:MF_01603}. CC -!- SIMILARITY: In the N-terminal section; belongs to the carbohydrate CC kinase PfkB family. {ECO:0000256|HAMAP-Rule:MF_01603}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:PTQ80077.1}. 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; QAOK01000019; PTQ80077.1; -; Genomic_DNA. DR AlphaFoldDB; A0A2T5I8D4; -. DR EnsemblBacteria; PTQ80077; PTQ80077; C8R21_11914. DR UniPathway; UPA00356; UER00437. DR UniPathway; UPA00958; -. DR Proteomes; UP000244152; Unassembled WGS sequence. 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 Gene3D; 3.40.1190.20; -; 1. DR Gene3D; 3.40.50.620; HUPs; 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; IPR011914; RfaE_dom_II. DR InterPro; IPR029056; Ribokinase-like. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR NCBIfam; TIGR00125; cyt_tran_rel; 1. DR NCBIfam; TIGR02199; rfaE_dom_II; 1. DR PANTHER; PTHR46969; BIFUNCTIONAL PROTEIN HLDE; 1. DR PANTHER; PTHR46969:SF1; BIFUNCTIONAL PROTEIN HLDE; 1. DR Pfam; PF01467; CTP_transf_like; 1. DR Pfam; PF00294; PfkB; 1. DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1. DR SUPFAM; SSF53613; Ribokinase-like; 1. DR PROSITE; PS00583; PFKB_KINASES_1; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_01603}; KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP- KW Rule:MF_01603}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_01603}; KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP- KW Rule:MF_01603}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_01603}; Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01603}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01603}. FT DOMAIN 16..319 FT /note="Carbohydrate kinase PfkB" FT /evidence="ECO:0000259|Pfam:PF00294" FT DOMAIN 357..450 FT /note="Cytidyltransferase-like" FT /evidence="ECO:0000259|Pfam:PF01467" FT REGION 1..332 FT /note="Ribokinase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01603" FT REGION 356..491 FT /note="Cytidylyltransferase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01603" FT ACT_SITE 279 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01603" FT BINDING 204..207 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01603" SQ SEQUENCE 491 AA; 53733 MW; 92507CE74897C1A8 CRC64; MNSSYLATID RFSGLNVLVI GDAMLDVYLD GSANRICREA PVPIVDIRDV KAVPGGAANT AVNLAQLGAR VHYLSVVGCD HEAELLKESL VSHSLDISLV ICDPTRRTLT KQRVAAGAQL LVRFDAGTTE QVCNQHEQQM IDTLNEKFHE MDAVVVSDYG YGILTDPVID ALRVLQKKKE NTLVIDAKSL DKYSRLGATV AKPNYQELVT LLAITEPAPV GQRSEQIRLH GQKLLKKSGT KYVAATIDVE GALLFQHGKE PYRTFSKPVE NTRAAGAGDT YVSALTLALA SGASIEVAGE IAKSAAMVIL QKSHTATCTQ NELRHYLGSS SKYIADWQGL NNRLATFRKE GKRIVFTNGC FDLLHSGHVS YLEQARDLGD ILVLGLNSDA SIKRLKGSNR PINNLYERIR ILSGLESVTF MTSFEEDTPI DLLQVVQPDL YVKGGDYTIE TLPEAPVVRA YGGKVEIMPF VQDRSTTNII SRIKSMDKQV A //