ID B3PRM9_RHIE6 Unreviewed; 132 AA.
AC B3PRM9;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=phosphoenolpyruvate--glycerone phosphotransferase {ECO:0000256|ARBA:ARBA00012095};
DE EC=2.7.1.121 {ECO:0000256|ARBA:ARBA00012095};
GN OrderedLocusNames=RHECIAT_CH0002637 {ECO:0000313|EMBL:ACE91589.1};
OS Rhizobium etli (strain CIAT 652).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=491916 {ECO:0000313|EMBL:ACE91589.1, ECO:0000313|Proteomes:UP000008817};
RN [1] {ECO:0000313|EMBL:ACE91589.1, ECO:0000313|Proteomes:UP000008817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIAT 652 {ECO:0000313|EMBL:ACE91589.1,
RC ECO:0000313|Proteomes:UP000008817};
RA Gonzalez V., Acosta J.L., Santamaria R.I., Bustos P.,
RA Hernandez-Gonzalez I.L., Fernandez J.L., Diaz R., Flores M., Mora J.,
RA Palacios R., Davila G.;
RT "Genome diversity and DNA divergence of Rhizobium etli.";
RL Submitted (APR-2008) 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; CP001074; ACE91589.1; -; Genomic_DNA.
DR AlphaFoldDB; B3PRM9; -.
DR KEGG; rec:RHECIAT_CH0002637; -.
DR eggNOG; COG3412; Bacteria.
DR HOGENOM; CLU_045361_2_1_5; -.
DR Proteomes; UP000008817; Chromosome.
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:ACE91589.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ACE91589.1}.
FT DOMAIN 7..132
FT /note="PTS EIIA type-4"
FT /evidence="ECO:0000259|PROSITE:PS51096"
SQ SEQUENCE 132 AA; 13101 MW; B2F95921CFA15CA6 CRC64;
MTGKTANVGI VIVSHSPLVA RGIADMVRQM VGDCVPLSWS GGNVDGELGT NAGGILRAIE
AAWSDAGVAV FVDLGGAETN SEMAIEMLGL PRSALVSICN APLVEGAVIA AAEASGGASL
ARVVATAEEL SP
//