ID A0A2T5I8D4_9PROT Unreviewed; 491 AA. AC A0A2T5I8D4; DT 18-JUL-2018, integrated into UniProtKB/TrEMBL. DT 18-JUL-2018, sequence version 1. DT 16-JAN-2019, entry version 6. DE RecName: Full=Bifunctional protein HldE {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}; 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}; GN Name=hldE {ECO:0000256|HAMAP-Rule:MF_01603}; GN ORFNames=C8R21_11914 {ECO:0000313|EMBL:PTQ80077.1}; OS Nitrosospira multiformis. OC Bacteria; Proteobacteria; 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 RT Klosterneuburg, 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- CC heptose. {ECO:0000256|HAMAP-Rule:MF_01603, CC ECO:0000256|SAAS:SAAS00345055}. 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:0000256|HAMAP- CC Rule:MF_01603, ECO:0000256|SAAS:SAAS00345059}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + D-glycero-beta-D-manno-heptose 1-phosphate + H(+) = CC ADP-D-glycero-beta-D-manno-heptose + diphosphate; CC Xref=Rhea:RHEA:27465, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:59967, ChEBI:CHEBI:61593; CC EC=2.7.7.70; Evidence={ECO:0000256|HAMAP-Rule:MF_01603, CC ECO:0000256|SAAS:SAAS01118290}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + D-glycero-beta-D-manno-heptose 7-phosphate = ADP + CC D-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 ECO:0000256|SAAS:SAAS01118289}; 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:0000256|HAMAP-Rule:MF_01603, ECO:0000256|SAAS:SAAS00345035}. 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:0000256|HAMAP-Rule:MF_01603, ECO:0000256|SAAS:SAAS00054951}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01603, CC ECO:0000256|SAAS:SAAS00345050}. CC -!- SIMILARITY: In the C-terminal section; belongs to the CC cytidylyltransferase family. {ECO:0000256|HAMAP-Rule:MF_01603, CC ECO:0000256|SAAS:SAAS00540903}. CC -!- SIMILARITY: In the N-terminal section; belongs to the carbohydrate CC kinase PfkB family. {ECO:0000256|HAMAP-Rule:MF_01603, CC ECO:0000256|SAAS:SAAS00540902}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 UniPathway; UPA00356; UER00437. 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 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; 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; TIGR02199; rfaE_dom_II; 1. DR PROSITE; PS00583; PFKB_KINASES_1; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01603, KW ECO:0000256|SAAS:SAAS00054912}; KW Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_01603, KW ECO:0000256|SAAS:SAAS00015140}; KW Complete proteome {ECO:0000313|Proteomes:UP000244152}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_01603, KW ECO:0000256|SAAS:SAAS00061343, ECO:0000313|EMBL:PTQ80077.1}; KW Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01603, KW ECO:0000256|SAAS:SAAS00015125}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01603, KW ECO:0000256|SAAS:SAAS00054948}; KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01603, KW ECO:0000256|SAAS:SAAS00015117}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01603, KW ECO:0000256|SAAS:SAAS00061368, ECO:0000313|EMBL:PTQ80077.1}. FT DOMAIN 16 319 PfkB. {ECO:0000259|Pfam:PF00294}. FT DOMAIN 357 450 CTP_transf_like. {ECO:0000259|Pfam: FT PF01467}. FT NP_BIND 204 207 ATP. {ECO:0000256|HAMAP-Rule:MF_01603}. FT REGION 1 330 Ribokinase. {ECO:0000256|HAMAP-Rule: FT MF_01603}. FT REGION 356 491 Cytidylyltransferase. {ECO:0000256|HAMAP- FT Rule:MF_01603}. FT ACT_SITE 279 279 {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 //