ID A0A1H5WD30_9RHOO Unreviewed; 576 AA.
AC A0A1H5WD30;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Phosphoenolpyruvate-protein phosphotransferase {ECO:0000256|ARBA:ARBA00016544, ECO:0000256|PIRNR:PIRNR000732};
DE EC=2.7.3.9 {ECO:0000256|ARBA:ARBA00012232, ECO:0000256|PIRNR:PIRNR000732};
DE AltName: Full=Phosphotransferase system, enzyme I {ECO:0000256|ARBA:ARBA00033235, ECO:0000256|PIRNR:PIRNR000732};
GN ORFNames=SAMN05216242_11140 {ECO:0000313|EMBL:SEF96717.1}, Tchl_0348
GN {ECO:0000313|EMBL:APR03220.1};
OS Thauera chlorobenzoica.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Thauera.
OX NCBI_TaxID=96773 {ECO:0000313|EMBL:APR03220.1, ECO:0000313|Proteomes:UP000185739};
RN [1] {ECO:0000313|EMBL:SEF96717.1, ECO:0000313|Proteomes:UP000236741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3CB-1 {ECO:0000313|EMBL:SEF96717.1,
RC ECO:0000313|Proteomes:UP000236741};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:APR03220.1, ECO:0000313|Proteomes:UP000185739}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3CB1 {ECO:0000313|EMBL:APR03220.1,
RC ECO:0000313|Proteomes:UP000185739};
RA Goris T., Mergelsberg M., Boll M.;
RT "Complete genome sequence of Thauera chlorobenzoica, a Betaproteobacterium
RT degrading haloaromatics anaerobically to CO2 and halides.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|PIRNR:PIRNR000732}.
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:0000256|ARBA:ARBA00000683,
CC ECO:0000256|PIRNR:PIRNR000732};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|PIRNR:PIRNR000732, ECO:0000256|PIRSR:PIRSR000732-3};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|PIRNR:PIRNR000732}.
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC {ECO:0000256|ARBA:ARBA00007837, ECO:0000256|PIRNR:PIRNR000732}.
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DR EMBL; CP018839; APR03220.1; -; Genomic_DNA.
DR EMBL; FNVJ01000011; SEF96717.1; -; Genomic_DNA.
DR RefSeq; WP_075146865.1; NZ_FNVJ01000011.1.
DR AlphaFoldDB; A0A1H5WD30; -.
DR STRING; 96773.Tchl_0348; -.
DR KEGG; tcl:Tchl_0348; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000185739; Chromosome.
DR Proteomes; UP000236741; Unassembled WGS sequence.
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; 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; 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:SF5; 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 {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR000732};
KW Kinase {ECO:0000256|PIRNR:PIRNR000732, ECO:0000313|EMBL:APR03220.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRNR:PIRNR000732};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR000732};
KW Phosphotransferase system {ECO:0000256|ARBA:ARBA00022683,
KW ECO:0000256|PIRNR:PIRNR000732}; Pyruvate {ECO:0000313|EMBL:APR03220.1};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597,
KW ECO:0000256|PIRNR:PIRNR000732};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000732};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR000732}.
FT DOMAIN 6..130
FT /note="Phosphotransferase system enzyme I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF05524"
FT DOMAIN 161..231
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 258..545
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT ACT_SITE 195
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000732-1"
FT ACT_SITE 508
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000732-1"
FT BINDING 302
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|PIRSR:PIRSR000732-2"
FT BINDING 338
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|PIRSR:PIRSR000732-2"
FT BINDING 437
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000732-3"
FT BINDING 460..461
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|PIRSR:PIRSR000732-2"
FT BINDING 461
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000732-3"
FT BINDING 471
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|PIRSR:PIRSR000732-2"
SQ SEQUENCE 576 AA; 63430 MW; 553F0CB18EF1FB5C CRC64;
MPFTVHGLAV SQGIAIGHVH LVSRALLEVN HYHVAQKYLA EELLRLDDAV ATVQGELMGL
KAAATSGHTH SEVGAFVDLQ LMMLSDPLLI DAARELVESR RCNTEWALVQ QMELLVEQFR
QIEDPYLRER QADVVQVVER LVKVLLGHPG HLPPKRRDGL GTIIVAHDLS PADTISFRDH
NIAGFVTDVG GPTSHTAIVA RNLKIPAVVG LHRVRDLVED DELVIVDGTR GLIIVAPDER
IVEEYRLRRS ELEIERSKLN RLRDAHAATL DGETIHLLAN IEGPKDLPAA KTANADGIGL
YRTEFLFLGR DTLPDEEEQY EAYRAVVKAM PGKPVTIRSF DVGADKALNG SHSRIEPNPA
LGLRAVRYSL AEPKMFLTQL RALLRASAHG RLQIMIPMLS HAQEIDQSLA LVEKAKAELR
AEKIKFDEGI QIGGMIEVPA AALSLGMFTR RLSFLSIGTN DLIQYTLAID RSDEAVVHLY
DPLHPAVLKL IAGTIATGAR YSLPVAVCGE MAGDSKYTAL LLGMGLRSFS MHPGNILEIK
QQVLRSTLGE LAPRVQRILK MDEPARIREA VERLAT
//
