ID E1IMU9_ECOLX Unreviewed; 472 AA.
AC E1IMU9;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=phosphoenolpyruvate--glycerone phosphotransferase {ECO:0000256|ARBA:ARBA00012095};
DE EC=2.7.1.121 {ECO:0000256|ARBA:ARBA00012095};
GN ORFNames=HMPREF9348_01470 {ECO:0000313|EMBL:EFO59453.1};
OS Escherichia coli MS 145-7.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=679204 {ECO:0000313|EMBL:EFO59453.1, ECO:0000313|Proteomes:UP000003691};
RN [1] {ECO:0000313|EMBL:EFO59453.1, ECO:0000313|Proteomes:UP000003691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS 145-7 {ECO:0000313|EMBL:EFO59453.1,
RC ECO:0000313|Proteomes:UP000003691};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the dihydroxyacetone kinase complex, which is
CC responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation
CC of dihydroxyacetone. DhaM serves as the phosphoryl donor. Is
CC phosphorylated by phosphoenolpyruvate in an EI- and HPr-dependent
CC reaction, and a phosphorelay system on histidine residues finally leads
CC to phosphoryl transfer to DhaL and dihydroxyacetone.
CC {ECO:0000256|ARBA:ARBA00002788}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dihydroxyacetone + phosphoenolpyruvate = dihydroxyacetone
CC phosphate + pyruvate; Xref=Rhea:RHEA:18381, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:16016, ChEBI:CHEBI:57642, ChEBI:CHEBI:58702;
CC EC=2.7.1.121; Evidence={ECO:0000256|ARBA:ARBA00001113};
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:EFO59453.1}.
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DR EMBL; ADWS01000005; EFO59453.1; -; Genomic_DNA.
DR RefSeq; WP_001297541.1; NZ_ADWS01000005.1.
DR AlphaFoldDB; E1IMU9; -.
DR Proteomes; UP000003691; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0047324; F:phosphoenolpyruvate-glycerone phosphotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0019563; P:glycerol catabolic process; IEA:InterPro.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00367; PTS-HPr_like; 1.
DR Gene3D; 3.30.1340.10; HPr-like; 1.
DR Gene3D; 3.50.30.10; Phosphohistidine domain; 1.
DR Gene3D; 3.40.50.510; Phosphotransferase system, mannose-type IIA component; 1.
DR Gene3D; 1.10.274.10; PtsI, HPr-binding domain; 1.
DR InterPro; IPR039643; DhaM.
DR InterPro; IPR012844; DhaM_N.
DR InterPro; IPR000032; HPr-like.
DR InterPro; IPR035895; HPr-like_sf.
DR InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR036637; Phosphohistidine_dom_sf.
DR InterPro; IPR004701; PTS_EIIA_man-typ.
DR InterPro; IPR036662; PTS_EIIA_man-typ_sf.
DR InterPro; IPR008731; PTS_EIN.
DR InterPro; IPR001020; PTS_HPr_His_P_site.
DR InterPro; IPR036618; PtsI_HPr-bd_sf.
DR NCBIfam; TIGR02364; dha_pts; 1.
DR NCBIfam; TIGR01003; PTS_HPr_family; 1.
DR PANTHER; PTHR38594; PEP-DEPENDENT DIHYDROXYACETONE KINASE, PHOSPHORYL DONOR SUBUNIT DHAM; 1.
DR PANTHER; PTHR38594:SF1; PEP-DEPENDENT DIHYDROXYACETONE KINASE, PHOSPHORYL DONOR SUBUNIT DHAM; 1.
DR Pfam; PF03610; EIIA-man; 1.
DR Pfam; PF05524; PEP-utilisers_N; 1.
DR Pfam; PF00391; PEP-utilizers; 1.
DR Pfam; PF00381; PTS-HPr; 1.
DR PRINTS; PR00107; PHOSPHOCPHPR.
DR SUPFAM; SSF47831; Enzyme I of the PEP:sugar phosphotransferase system HPr-binding (sub)domain; 1.
DR SUPFAM; SSF55594; HPr-like; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 1.
DR SUPFAM; SSF53062; PTS system fructose IIA component-like; 1.
DR PROSITE; PS51096; PTS_EIIA_TYPE_4; 1.
DR PROSITE; PS51350; PTS_HPR_DOM; 1.
DR PROSITE; PS00369; PTS_HPR_HIS; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:EFO59453.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..135
FT /note="PTS EIIA type-4"
FT /evidence="ECO:0000259|PROSITE:PS51096"
FT DOMAIN 155..242
FT /note="HPr"
FT /evidence="ECO:0000259|PROSITE:PS51350"
SQ SEQUENCE 472 AA; 51447 MW; 797A5FDAFA366810 CRC64;
MVNLVIVSHS SRLGEGVGEL ARQMLMSDSC KIAIAAGIDD PQNPIGTDAV KVMEAIESVA
DADHVLVMMD MGSALLSAET ALELLAPKIA AKVRLCAAPL VEGTLAATVS AASGADIDKV
IFDAMHALEA KREQLGLPSS DTKISDTCPA YDEEARSLAV VIKNRNGLHV RPASRLVYTL
STFNADMLLE KNGKCVTPES INQIALLQVR YNDTLRLIAK GPEAEEALIA FRQLAEDNFG
ETEEVAPPTL RPVPPVSGKA FYYQPVLCTV QAKSTLTVEE EQDRLRQAID FTLLDLMTLT
AKAEASGLDD IAAIFSGHHT LLDDPELLAA ASELLQHEHC TAEYAWQQVL KELSQQYQQL
DDEYLQARYI DVDDLLHRTL VHLTQTKEEL PQFNSPTILL AENIYPSTVL QLDPAVVKGI
CLSAGSPVSH SALIARELGI GWICQQGEKL YAIQPEETLT LDVKTQRFNR QG
//
