ID A0A0D6PHS8_9PROT Unreviewed; 749 AA.
AC A0A0D6PHS8;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=phosphoenolpyruvate--glycerone phosphotransferase {ECO:0000256|ARBA:ARBA00012095};
DE EC=2.7.1.121 {ECO:0000256|ARBA:ARBA00012095};
GN ORFNames=Aam_090_003 {ECO:0000313|EMBL:GAN81325.1};
OS Acidocella aminolytica 101 = DSM 11237.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acidocella.
OX NCBI_TaxID=1120923 {ECO:0000313|EMBL:GAN81325.1, ECO:0000313|Proteomes:UP000032668};
RN [1] {ECO:0000313|EMBL:GAN81325.1, ECO:0000313|Proteomes:UP000032668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=101 / DSM 11237 {ECO:0000313|Proteomes:UP000032668};
RA Azuma Y., Higashiura N., Hirakawa H., Matsushita K.;
RT "Whole genome sequence of Acidocella aminolytica 101 = DSM 11237.";
RL Submitted (NOV-2012) 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC {ECO:0000256|ARBA:ARBA00007837}.
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:GAN81325.1}.
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DR EMBL; BANC01000088; GAN81325.1; -; Genomic_DNA.
DR RefSeq; WP_048879718.1; NZ_FQVJ01000046.1.
DR AlphaFoldDB; A0A0D6PHS8; -.
DR STRING; 1120923.SAMN02746095_03472; -.
DR Proteomes; UP000032668; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0047324; F:phosphoenolpyruvate-glycerone phosphotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR CDD; cd00367; PTS-HPr_like; 1.
DR Gene3D; 3.30.1340.10; HPr-like; 1.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR Gene3D; 3.50.30.10; Phosphohistidine domain; 1.
DR Gene3D; 3.40.50.510; Phosphotransferase system, mannose-type IIA component; 1.
DR Gene3D; 1.10.274.10; PtsI, HPr-binding domain; 1.
DR InterPro; IPR012844; DhaM_N.
DR InterPro; IPR000032; HPr-like.
DR InterPro; IPR035895; HPr-like_sf.
DR InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR000121; PEP_util_C.
DR InterPro; IPR023151; PEP_util_CS.
DR InterPro; IPR036637; Phosphohistidine_dom_sf.
DR InterPro; IPR004701; PTS_EIIA_man-typ.
DR InterPro; IPR036662; PTS_EIIA_man-typ_sf.
DR InterPro; IPR008731; PTS_EIN.
DR InterPro; IPR036618; PtsI_HPr-bd_sf.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR NCBIfam; TIGR02364; dha_pts; 1.
DR NCBIfam; TIGR01003; PTS_HPr_family; 1.
DR PANTHER; PTHR46244; PHOSPHOENOLPYRUVATE-PROTEIN PHOSPHOTRANSFERASE; 1.
DR PANTHER; PTHR46244:SF3; PHOSPHOENOLPYRUVATE-PROTEIN PHOSPHOTRANSFERASE; 1.
DR Pfam; PF03610; EIIA-man; 1.
DR Pfam; PF05524; PEP-utilisers_N; 1.
DR Pfam; PF00391; PEP-utilizers; 1.
DR Pfam; PF02896; PEP-utilizers_C; 1.
DR Pfam; PF00381; PTS-HPr; 1.
DR PRINTS; PR00107; PHOSPHOCPHPR.
DR PRINTS; PR01736; PHPHTRNFRASE.
DR SUPFAM; SSF47831; Enzyme I of the PEP:sugar phosphotransferase system HPr-binding (sub)domain; 1.
DR SUPFAM; SSF55594; HPr-like; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 1.
DR SUPFAM; SSF53062; PTS system fructose IIA component-like; 1.
DR PROSITE; PS00742; PEP_ENZYMES_2; 1.
DR PROSITE; PS51096; PTS_EIIA_TYPE_4; 1.
DR PROSITE; PS51350; PTS_HPR_DOM; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000032668};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:GAN81325.1}.
FT DOMAIN 5..135
FT /note="PTS EIIA type-4"
FT /evidence="ECO:0000259|PROSITE:PS51096"
FT DOMAIN 152..242
FT /note="HPr"
FT /evidence="ECO:0000259|PROSITE:PS51350"
SQ SEQUENCE 749 AA; 77191 MW; A8C4517EDBD41257 CRC64;
MDGLPTGLLL VSHSLALAQA TEALVRQMTG ERLSIALAAG TGPDRADLGT DPLAILEAGE
ALAACQDIVV LMDIGSAVLS AEMAVDLAEE PLKTKLHLAA APFVEGALAA GVAAGAGMPV
AAVLTEAAAG LRPKLTALGG QEETTTPALQ ASLIRKVTLG DPNGLHLRPA ARCVEAASRF
EATLCLRFKN REAGLDSLTA LMALGAKGGE VVTIEAGGPQ AEQAAARLAA ILTEVPATID
KVLEAPSGAG PVPISPGRVS GRLMAVDRHQ PPIPDTATEA PEAGWIALLA AIETVRTHLG
DDDILAAQAA LLSDPAILTP AKAGVFEHRQ HPAAAWQQAF AHAAAGYEAL DDAYLRARAK
DVREVGNEVL RALLGGGGLE WPTDPAIILV ENLTAAEAAA LPAEVLGVLD RHGGRTSHAA
IMLRAAGVPC LGSVVLGSIP DTLAFDGATG EMVPNPDAAA RKAFTPAQAA STGPASIILP
DGCGLEFWAN VAGPKDAALA AQSGAFGIGL ARTEMLFLDR VDCPPEEEQT ARISAMLAPF
KGRPVTVRLL DAGADKPVPF LHLAPEENPA LGVRGVRALL KHPDFTAAHL RAILRAGQGH
DLRVMVPMVT FPKEMQTLRG WLEQACQETG LPCPSLGAMV EVPAAALTMP DLVPVCDFFS
IGTNDLTQYT LAAERGHQEL AAFANPANDA VIGLCARVVR EAGSRPVSVC GEAAGDPQAA
SRLVEEGVRK LSMGAARLGP IRALWQGRD
//
