ID A0A017H3Q6_9FUSO Unreviewed; 134 AA.
AC A0A017H3Q6;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=phosphoenolpyruvate--glycerone phosphotransferase {ECO:0000256|ARBA:ARBA00012095};
DE EC=2.7.1.121 {ECO:0000256|ARBA:ARBA00012095};
GN ORFNames=C095_02345 {ECO:0000313|EMBL:KID49987.1};
OS Fusobacterium necrophorum subsp. funduliforme B35.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC Fusobacterium.
OX NCBI_TaxID=1226633 {ECO:0000313|EMBL:KID49987.1, ECO:0000313|Proteomes:UP000031184};
RN [1] {ECO:0000313|EMBL:KID49987.1, ECO:0000313|Proteomes:UP000031184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B35 {ECO:0000313|EMBL:KID49987.1,
RC ECO:0000313|Proteomes:UP000031184};
RA Benahmed F.H., Rasmussen M., Harbottle H., Soppet D., Nagaraja T.G.,
RA Davidson M.;
RT "An opportunistic ruminal bacterium that causes liver abscesses in
RT cattle.";
RL Submitted (AUG-2013) 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 -!- 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:KID49987.1}.
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DR EMBL; AUZI01000010; KID49987.1; -; Genomic_DNA.
DR RefSeq; WP_035914665.1; NZ_AOJP01000011.1.
DR AlphaFoldDB; A0A017H3Q6; -.
DR PATRIC; fig|1226633.4.peg.466; -.
DR OrthoDB; 7065393at2; -.
DR Proteomes; UP000031184; 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 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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ SEQUENCE 134 AA; 14503 MW; C1D05C05CFA0E8A6 CRC64;
MVGFVVVSHS KALAEEAIRL ANEMKKESFP LLNGSGIEGE SFGSNPFRIK ETVEKAMTEN
GVVIFVDLGS SVLNSQIALE FLEAEGKEIS KIKIADAPLV EGLIAAVAMN DTKASVEDIL
TELKEFKQFS KINN
//
