ID A0A1R4FBX1_9ACTO Unreviewed; 253 AA.
AC A0A1R4FBX1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=phosphoenolpyruvate--glycerone phosphotransferase {ECO:0000256|ARBA:ARBA00012095};
DE EC=2.7.1.121 {ECO:0000256|ARBA:ARBA00012095};
GN ORFNames=CZ771_06330 {ECO:0000313|EMBL:SJM53386.1};
OS Actinomycetales bacterium JB111.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales.
OX NCBI_TaxID=1434822 {ECO:0000313|EMBL:SJM53386.1, ECO:0000313|Proteomes:UP000196124};
RN [1] {ECO:0000313|EMBL:SJM53386.1, ECO:0000313|Proteomes:UP000196124}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JB111 {ECO:0000313|EMBL:SJM53386.1,
RC ECO:0000313|Proteomes:UP000196124};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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; FUHX01000028; SJM53386.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R4FBX1; -.
DR Proteomes; UP000196124; 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; 3.30.1340.10; HPr-like; 1.
DR Gene3D; 3.40.50.510; Phosphotransferase system, mannose-type IIA component; 1.
DR InterPro; IPR039643; DhaM.
DR InterPro; IPR012844; DhaM_N.
DR InterPro; IPR000032; HPr-like.
DR InterPro; IPR035895; HPr-like_sf.
DR InterPro; IPR004701; PTS_EIIA_man-typ.
DR InterPro; IPR036662; PTS_EIIA_man-typ_sf.
DR InterPro; IPR001020; PTS_HPr_His_P_site.
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; PF00381; PTS-HPr; 1.
DR PRINTS; PR00107; PHOSPHOCPHPR.
DR SUPFAM; SSF55594; HPr-like; 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 4: Predicted;
KW Pyruvate {ECO:0000313|EMBL:SJM53386.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000196124};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SJM53386.1}.
FT DOMAIN 3..130
FT /note="PTS EIIA type-4"
FT /evidence="ECO:0000259|PROSITE:PS51096"
FT DOMAIN 172..253
FT /note="HPr"
FT /evidence="ECO:0000259|PROSITE:PS51350"
FT REGION 132..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 253 AA; 24736 MW; 90E52728F262E3EA CRC64;
MPRTALVVVS HSADLARGLV ALAAQMAADV RIVAAGGTDD GRIGTSFDAV DSAVESLLAD
DDVSGVVLVG DLGSAEMTID SVLEMHDDAP VRHAHGPLVE GVVTAAVAAQ GGADLHAVAA
AVGEAARAQA SAAEADGSEA DAEPAAPAAP AEQAPAARDA PVAGDEVEDP DAVVRTIVID
DPMGLHARPA AAVAAKAATF TAPVTLNGVD GRSVLALMAA NIPAGSTITV QASGEDADEA
VSAVVQIIAD AKG
//
