ID J6IY09_9ENTR Unreviewed; 472 AA.
AC J6IY09;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=phosphoenolpyruvate--glycerone phosphotransferase {ECO:0000256|ARBA:ARBA00012095};
DE EC=2.7.1.121 {ECO:0000256|ARBA:ARBA00012095};
GN ORFNames=HMPREF1144_2590 {ECO:0000313|EMBL:EJU35598.1};
OS Klebsiella sp. OBRC7.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=936565 {ECO:0000313|EMBL:EJU35598.1, ECO:0000313|Proteomes:UP000004118};
RN [1] {ECO:0000313|EMBL:EJU35598.1, ECO:0000313|Proteomes:UP000004118}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OBRC7 {ECO:0000313|EMBL:EJU35598.1,
RC ECO:0000313|Proteomes:UP000004118};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (JUL-2012) 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:EJU35598.1}.
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DR EMBL; ALNJ01000019; EJU35598.1; -; Genomic_DNA.
DR RefSeq; WP_009651878.1; NZ_ALNJ01000019.1.
DR AlphaFoldDB; J6IY09; -.
DR PATRIC; fig|936565.3.peg.654; -.
DR Proteomes; UP000004118; 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:EJU35598.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..135
FT /note="PTS EIIA type-4"
FT /evidence="ECO:0000259|PROSITE:PS51096"
FT DOMAIN 156..243
FT /note="HPr"
FT /evidence="ECO:0000259|PROSITE:PS51350"
SQ SEQUENCE 472 AA; 50089 MW; BE976B29B083F823 CRC64;
MVNLVIVSHS ARLGEGVGEL ARQMLMNDGC KLAIAAGIDD PASPIGTDPI KVMEAIESVA
DADHILVMMD IGSALLSAET ALDLLDPAIA AKVRLCAAPL VEGTLAATVS AAAGAGIDKV
IEDAMNALEA KRVQLGLPSQ PQHASLAAAP VDDRDARSVS VVIQNHNGLH VRPASKLVAA
LAGFNADLVL EKGGKCVTPD SLNQIALLQV RRNDTLRLLA RGPDADAALA AFQALAAENF
GEPTEAAPAR RPASADRVEG KVVLYPQPQD RVSRETSTAI GQQQLRLKRA IDRTLEDLSA
LTTLAEATFS ADIAAIFSGH HTLLDDPDLY AAACDIIRDE QCSAAWAWLQ VLSDLSQQYR
HLDDAYLQAR YIDIEDILHR TLSHLNERDE VLPQFSAPSI LVADDIFPST VLQLNAEQVK
GICLQAGSEL SHGAIIARQA GIAMLCQQSD ALTLQDGESV TLDIPGKRVI RG
//
