ID PT1_CUPNH Reviewed; 586 AA. AC P23536; Q0KEU4; DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 02-SEP-2026, entry version 152. DE RecName: Full=Phosphoenolpyruvate-protein phosphotransferase {ECO:0000303|PubMed:1653223}; DE EC=2.7.3.9 {ECO:0000250|UniProtKB:P08839}; DE AltName: Full=Phosphotransferase system, enzyme I {ECO:0000303|PubMed:1653223}; GN Name=phbI {ECO:0000303|PubMed:1653223}; Synonyms=ptsI; GN OrderedLocusNames=H16_A0326; OS Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 OS / H16 / Stanier 337) (Ralstonia eutropha). OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria; OC Burkholderiales; Burkholderiaceae; Cupriavidus. OX NCBI_TaxID=381666; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION. RX PubMed=1653223; DOI=10.1128/jb.173.18.5843-5853.1991; RA Pries A., Priefert H., Krueger N., Steinbuechel A.; RT "Identification and characterization of two Alcaligenes eutrophus gene loci RT relevant to the poly(beta-hydroxybutyric acid)-leaky phenotype which RT exhibit homology to ptsH and ptsI of Escherichia coli."; RL J. Bacteriol. 173:5843-5853(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier RC 337; RX PubMed=16964242; DOI=10.1038/nbt1244; RA Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R., RA Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I., RA Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.; RT "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia RT eutropha H16."; RL Nat. Biotechnol. 24:1257-1262(2006). CC -!- FUNCTION: General (non sugar-specific) component of the CC phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar CC PTS). This major carbohydrate active-transport system catalyzes the CC phosphorylation of incoming sugar substrates concomitantly with their CC translocation across the cell membrane. Enzyme I transfers the CC phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl CC carrier protein (HPr). {ECO:0000250|UniProtKB:P08839, CC ECO:0000305|PubMed:1653223}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-histidyl-[protein] + phosphoenolpyruvate = N(pros)-phospho- CC L-histidyl-[protein] + pyruvate; Xref=Rhea:RHEA:23880, Rhea:RHEA- CC COMP:9745, Rhea:RHEA-COMP:9746, ChEBI:CHEBI:15361, ChEBI:CHEBI:29979, CC ChEBI:CHEBI:58702, ChEBI:CHEBI:64837; EC=2.7.3.9; CC Evidence={ECO:0000250|UniProtKB:P08839}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P08839}; CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P08839}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- DOMAIN: The N-terminal domain contains the HPr binding site, the CC central domain the pyrophosphate/phosphate carrier histidine, and the CC C-terminal domain the pyruvate binding site. CC {ECO:0000250|UniProtKB:P08839}. CC -!- MISCELLANEOUS: The reaction takes place in three steps, mediated by a CC phosphocarrier histidine residue located on the surface of the central CC domain. The two first partial reactions are catalyzed at an active site CC located on the N-terminal domain, and the third partial reaction is CC catalyzed at an active site located on the C-terminal domain. For CC catalytic turnover, the central domain swivels from the concave surface CC of the N-terminal domain to that of the C-terminal domain. CC {ECO:0000250|UniProtKB:P08839}. CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family. {ECO:0000305}. 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; M69036; AAA21978.1; -; Genomic_DNA. DR EMBL; AM260479; CAJ91477.1; -; Genomic_DNA. DR PIR; B38120; B38120. DR RefSeq; WP_011614460.1; NC_008313.1. DR AlphaFoldDB; P23536; -. DR SMR; P23536; -. DR STRING; 381666.H16_A0326; -. DR PaxDb; 381666-H16_A0326; -. DR KEGG; reh:H16_A0326; -. DR PATRIC; fig|381666.6.peg.689; -. DR eggNOG; COG1080; Bacteria. DR HOGENOM; CLU_007308_7_0_4; -. DR OrthoDB; 9765468at2; -. DR Proteomes; UP000008210; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008965; F:phosphoenolpyruvate-protein phosphotransferase activity; ISS:UniProtKB. DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:InterPro. DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1. DR Gene3D; 3.50.30.10; Phosphohistidine domain; 1. DR Gene3D; 1.10.274.10; PtsI, HPr-binding domain; 1. DR InterPro; IPR008279; PEP-util_enz_mobile_dom. DR InterPro; IPR050499; PEP-utilizing_PTS_enzyme. DR InterPro; IPR018274; PEP_util_AS. DR InterPro; IPR000121; PEP_util_C. DR InterPro; IPR023151; PEP_util_CS. DR InterPro; IPR036637; Phosphohistidine_dom_sf. DR InterPro; IPR024692; PTS_EI. DR InterPro; IPR006318; PTS_EI-like. DR InterPro; IPR008731; PTS_EIN. DR InterPro; IPR036618; PtsI_HPr-bd_sf. DR InterPro; IPR015813; Pyrv/PenolPyrv_kinase-like_dom. DR InterPro; IPR040442; Pyrv_kinase-like_dom_sf. DR NCBIfam; TIGR01417; PTS_I_fam; 1. DR PANTHER; PTHR46244; PHOSPHOENOLPYRUVATE-PROTEIN PHOSPHOTRANSFERASE; 1. DR PANTHER; PTHR46244:SF3; PHOSPHOENOLPYRUVATE-PROTEIN PHOSPHOTRANSFERASE; 1. DR Pfam; PF05524; PEP-utilisers_N; 1. DR Pfam; PF00391; PEP-utilizers; 1. DR Pfam; PF02896; PEP-utilizers_C; 1. DR PIRSF; PIRSF000732; PTS_enzyme_I; 1. DR PRINTS; PR01736; PHPHTRNFRASE. DR SUPFAM; SSF47831; Enzyme I of the PEP:sugar phosphotransferase system HPr-binding (sub)domain; 1. DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1. DR SUPFAM; SSF52009; Phosphohistidine domain; 1. DR PROSITE; PS00742; PEP_ENZYMES_2; 1. DR PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1. PE 3: Inferred from homology; KW Cytoplasm; Kinase; Magnesium; Metal-binding; Phosphotransferase system; KW Reference proteome; Sugar transport; Transferase; Transport. FT CHAIN 1..586 FT /note="Phosphoenolpyruvate-protein phosphotransferase" FT /id="PRO_0000147053" FT ACT_SITE 201 FT /note="Tele-phosphohistidine intermediate" FT /evidence="ECO:0000250|UniProtKB:P08839" FT ACT_SITE 517 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:P08839" FT BINDING 308 FT /ligand="phosphoenolpyruvate" FT /ligand_id="ChEBI:CHEBI:58702" FT /evidence="ECO:0000250|UniProtKB:P23533" FT BINDING 345 FT /ligand="phosphoenolpyruvate" FT /ligand_id="ChEBI:CHEBI:58702" FT /evidence="ECO:0000250|UniProtKB:P08839" FT BINDING 446 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P08839" FT BINDING 469..470 FT /ligand="phosphoenolpyruvate" FT /ligand_id="ChEBI:CHEBI:58702" FT /evidence="ECO:0000250|UniProtKB:P08839" FT BINDING 470 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P08839" FT BINDING 480 FT /ligand="phosphoenolpyruvate" FT /ligand_id="ChEBI:CHEBI:58702" FT /evidence="ECO:0000250|UniProtKB:P23533" FT CONFLICT 116 FT /note="R -> H (in Ref. 1; AAA21978)" FT /evidence="ECO:0000305" FT CONFLICT 529 FT /note="L -> R (in Ref. 1; AAA21978)" FT /evidence="ECO:0000305" FT CONFLICT 578..586 FT /note="AALRQLARP -> RPLRSWHDPEAIRVF (in Ref. 1; AAA21978)" FT /evidence="ECO:0000305" SQ SEQUENCE 586 AA; 64300 MW; 1F52C8FC0A406641 CRC64; MPFALHGIPV SRGVAIGRAH LLAPAALDVS HYLVDEDQLD AEVERLRAAR AAVRAELAAL KRDLPRDAPE ELGAFLDVHA MILDDEALAR EPEALIRGRR YNAEWALTTR LEELMRQFDE IEDEYLRERK TDIRQVVERI LKALAGAPVL VPAPVPALAA DGEAATGVIV VAHDIAPADM LQFRHTVFHG FVTDMGGRTS HTAIVARSLD IPAAVGVQSA SELIRQDDWI IIDGDAGLVI VDPTAIILEE YRHRQSERAL EKKRLQRLRH TPAVTLDGLE IDLLANIEMA EDAGAALAAG AVGVGLFRSE FLFMNRRDEL PGEDEQFQAY RGAVDAMHGL PVTIRTIDIG ADKPLDARGD EFETALNPAL GLRAIRWSLS EPGMFLTQLR ALLRASAFGP VRLLVPMLAH ASEIDQTLAL IAKAKRQLDE RGEAYDPGMK VGAMIEIPAA VLLLPLFLRK MDFLSIGTND LIQYTLAIDR ADNAVAHLFD PLHPAVLQLV ARTIREANRA GVPVAVCGEM AGDPSMTRLL LGMGLREFSM HPAQLLRVKQ EILHAHCERL EPLVDQVLQA FDPEEQAAAL RQLARP //