ID A0A1G7QDJ3_9LACT Unreviewed; 124 AA.
AC A0A1G7QDJ3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=phosphoenolpyruvate--glycerone phosphotransferase {ECO:0000256|ARBA:ARBA00012095};
DE EC=2.7.1.121 {ECO:0000256|ARBA:ARBA00012095};
GN ORFNames=SAMN05421791_10257 {ECO:0000313|EMBL:SDF96548.1};
OS Facklamia miroungae.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Facklamia.
OX NCBI_TaxID=120956 {ECO:0000313|EMBL:SDF96548.1, ECO:0000313|Proteomes:UP000199708};
RN [1] {ECO:0000313|EMBL:SDF96548.1, ECO:0000313|Proteomes:UP000199708}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-466 {ECO:0000313|EMBL:SDF96548.1,
RC ECO:0000313|Proteomes:UP000199708};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FNCK01000002; SDF96548.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7QDJ3; -.
DR STRING; 120956.SAMN05421791_10257; -.
DR OrthoDB; 7065393at2; -.
DR Proteomes; UP000199708; 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 Gene3D; 3.40.50.510; Phosphotransferase system, mannose-type IIA component; 1.
DR InterPro; IPR039643; DhaM.
DR InterPro; IPR012844; DhaM_N.
DR InterPro; IPR004701; PTS_EIIA_man-typ.
DR InterPro; IPR036662; PTS_EIIA_man-typ_sf.
DR NCBIfam; TIGR02364; dha_pts; 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 SUPFAM; SSF53062; PTS system fructose IIA component-like; 1.
DR PROSITE; PS51096; PTS_EIIA_TYPE_4; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:SDF96548.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199708};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 3..124
FT /note="PTS EIIA type-4"
FT /evidence="ECO:0000259|PROSITE:PS51096"
SQ SEQUENCE 124 AA; 13531 MW; A0DA31F9171D8CE9 CRC64;
MKKTGIVIVS HVYEIAEGIH RLLQQVAADV DIQVIGGVDQ KEVGTSYDTA LEAINNNSAE
NILAFYDLGS AKMNLEMAME MSDKTIKIYD VPVVEGAYTA ATLLQAGVDQ ESIEAQLEEM
HMVK
//