ID R6S2T0_9FIRM Unreviewed; 431 AA.
AC R6S2T0;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=phosphoenolpyruvate--protein phosphotransferase {ECO:0000256|ARBA:ARBA00012232};
DE EC=2.7.3.9 {ECO:0000256|ARBA:ARBA00012232};
GN ORFNames=BN586_01107 {ECO:0000313|EMBL:CDC54280.1};
OS Dorea formicigenerans CAG:28.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Dorea.
OX NCBI_TaxID=1263073 {ECO:0000313|EMBL:CDC54280.1, ECO:0000313|Proteomes:UP000018109};
RN [1] {ECO:0000313|EMBL:CDC54280.1, ECO:0000313|Proteomes:UP000018109}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:28 {ECO:0000313|Proteomes:UP000018109};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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|ARBA:ARBA00002728}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC {ECO:0000256|ARBA:ARBA00007837}.
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:CDC54280.1}.
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DR EMBL; CBFN010000029; CDC54280.1; -; Genomic_DNA.
DR AlphaFoldDB; R6S2T0; -.
DR Proteomes; UP000018109; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:InterPro.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR Gene3D; 3.50.30.10; Phosphohistidine domain; 1.
DR InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR000121; PEP_util_C.
DR InterPro; IPR023151; PEP_util_CS.
DR InterPro; IPR036637; Phosphohistidine_dom_sf.
DR InterPro; IPR006318; PTS_EI-like.
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; PF00391; PEP-utilizers; 1.
DR Pfam; PF02896; PEP-utilizers_C; 1.
DR PRINTS; PR01736; PHPHTRNFRASE.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 1.
DR PROSITE; PS00742; PEP_ENZYMES_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphotransferase system {ECO:0000256|ARBA:ARBA00022683};
KW Pyruvate {ECO:0000313|EMBL:CDC54280.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018109};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CDC54280.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 43..114
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 142..430
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT COILED 282..313
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 431 AA; 48362 MW; 06A40AAE1E75C465 CRC64;
MIRISSHQQN NPIQGKEEDV RDVAIRVIRI LSRSWKDRML TDEPFVMAAR DIYPSEALQF
DKAKVLGFVT MYGTINSHTA VLARTKGIPA VIGLGESLKE EYDGKTIIID GYEGKIYIEP
DYATLTKMRE RKDANLRHVR NLERLKGKEN ITQSGQKIDI CANVGTREDI ENVLRSDAGG
IGLFRSEFLY MEMGSKLPSE EQLFQVYKLA AESMGANRVV VRIADFGGDK MVESVDLGEQ
ANPAIGLRGI RIMMEKEELF LPQFRAILRA SALGNVSIMF PMVTSMEEVA AAKALLEKAK
KQLKDEKTAY NENIEIGVMI ETPAAVMISG ELAREVDFFS IGTNDLLQLT LGMDRENPKL
DKYYNPYHPA LMKMIRIVAN NVHLEGKRIS ICGDLAADLS MTEFFVQIGI DELSVAPHQV
LGLRKKIREI Q
//
