PT1_CUPNH
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 03-AUG-2022, entry version 139.
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; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC 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 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}.
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DR EMBL; M69036; AAA21978.1; -; Genomic_DNA.
DR EMBL; AM260479; CAJ91477.1; -; Genomic_DNA.
DR PIR; B38120; B38120.
DR RefSeq; WP_011614460.1; NZ_CP039287.1.
DR AlphaFoldDB; P23536; -.
DR SMR; P23536; -.
DR STRING; 381666.H16_A0326; -.
DR EnsemblBacteria; CAJ91477; CAJ91477; H16_A0326.
DR GeneID; 57642423; -.
DR KEGG; reh:H16_A0326; -.
DR PATRIC; fig|381666.6.peg.689; -.
DR eggNOG; COG1080; Bacteria.
DR HOGENOM; CLU_007308_7_0_4; -.
DR OMA; CNAEWAL; -.
DR OrthoDB; 467393at2; -.
DR Proteomes; UP000008210; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008965; F:phosphoenolpyruvate-protein phosphotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.274.10; -; 1.
DR Gene3D; 3.20.20.60; -; 1.
DR InterPro; IPR008279; PEP-util_enz_mobile_dom.
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 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 SUPFAM; SSF47831; SSF47831; 1.
DR SUPFAM; SSF51621; SSF51621; 1.
DR SUPFAM; SSF52009; SSF52009; 1.
DR TIGRFAMs; TIGR01417; PTS_I_fam; 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
