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Database: UniProt
Entry: I0RBD8_9FIRM
LinkDB: I0RBD8_9FIRM
Original site: I0RBD8_9FIRM 
ID   I0RBD8_9FIRM            Unreviewed;       294 AA.
AC   I0RBD8;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=Phosphoenolpyruvate-protein phosphotransferase, N-terminal / PEP-utilizing enzyme, mobile domain multi-domain protein {ECO:0000313|EMBL:EIC96996.1};
DE   Flags: Fragment;
GN   ORFNames=HMPREF9970_0611 {ECO:0000313|EMBL:EIC96996.1};
OS   Lachnoanaerobaculum saburreum F0468.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Lachnoanaerobaculum.
OX   NCBI_TaxID=1095750 {ECO:0000313|EMBL:EIC96996.1, ECO:0000313|Proteomes:UP000005039};
RN   [1] {ECO:0000313|EMBL:EIC96996.1, ECO:0000313|Proteomes:UP000005039}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0468 {ECO:0000313|EMBL:EIC96996.1,
RC   ECO:0000313|Proteomes:UP000005039};
RA   Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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:EIC96996.1}.
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DR   EMBL; AJGH01000014; EIC96996.1; -; Genomic_DNA.
DR   AlphaFoldDB; I0RBD8; -.
DR   eggNOG; COG1080; Bacteria.
DR   Proteomes; UP000005039; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016772; F:transferase activity, transferring phosphorus-containing groups; IEA:InterPro.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:InterPro.
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   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; IPR036637; Phosphohistidine_dom_sf.
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   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   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; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE   3: Inferred from homology;
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Pyruvate {ECO:0000313|EMBL:EIC96996.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EIC96996.1}.
FT   DOMAIN          5..125
FT                   /note="Phosphotransferase system enzyme I N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05524"
FT   DOMAIN          151..224
FT                   /note="PEP-utilising enzyme mobile"
FT                   /evidence="ECO:0000259|Pfam:PF00391"
FT   DOMAIN          253..294
FT                   /note="PEP-utilising enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02896"
FT   NON_TER         294
FT                   /evidence="ECO:0000313|EMBL:EIC96996.1"
SQ   SEQUENCE   294 AA;  31974 MW;  0388E4AACC27DAC7 CRC64;
     MKIYGVGAAE GIGIGIAKVV KEQSVEVVKR TVSDTEAEVV NFTEILELTK AETEEMSKSL
     ERNASAKEAE ILVGHIMLMS DPMLIDEMVN LIKNEKVCAE YAVEGVCNQY AAVFASMDDE
     LMQQRAADMR DIKNRLIKKI LGLESNDLST LPHGSILVAK DLTPSMTAGL NPENVFGIVT
     EFGGKTSHSA ILARALEIPA VVGLSDLPQD IKDNTEILLD GESGEVIILP TEDEKKEYTG
     KKKKYDENKE FLKKYLTLPS VSKDGKKVEI AGNIGSPEDV KKVIENGGEG IGLF
//
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