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Database: UniProt
Entry: B3PRM9_RHIE6
LinkDB: B3PRM9_RHIE6
Original site: B3PRM9_RHIE6 
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};
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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
//
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