ID K8W1B8_9GAMM Unreviewed; 481 AA.
AC K8W1B8;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=phosphoenolpyruvate--glycerone phosphotransferase {ECO:0000256|ARBA:ARBA00012095};
DE EC=2.7.1.121 {ECO:0000256|ARBA:ARBA00012095};
GN ORFNames=OO7_14008 {ECO:0000313|EMBL:EKT54249.1};
OS Providencia sneebia DSM 19967.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Providencia.
OX NCBI_TaxID=1141660 {ECO:0000313|EMBL:EKT54249.1, ECO:0000313|Proteomes:UP000010290};
RN [1] {ECO:0000313|EMBL:EKT54249.1, ECO:0000313|Proteomes:UP000010290}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19967 {ECO:0000313|EMBL:EKT54249.1,
RC ECO:0000313|Proteomes:UP000010290};
RX PubMed=23145767; DOI=10.1186/1471-2164-13-612;
RA Galac M.R., Lazzaro B.P.;
RT "Comparative genomics of bacteria in the genus Providencia isolated from
RT wild Drosophila melanogaster.";
RL BMC Genomics 13:612-612(2012).
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 -!- 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:EKT54249.1}.
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DR EMBL; AKKN01000011; EKT54249.1; -; Genomic_DNA.
DR RefSeq; WP_008916548.1; NZ_CM001773.1.
DR AlphaFoldDB; K8W1B8; -.
DR PATRIC; fig|1141660.3.peg.2797; -.
DR HOGENOM; CLU_045361_0_0_6; -.
DR OrthoDB; 7065393at2; -.
DR Proteomes; UP000010290; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
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:UniProtKB-KW.
DR CDD; cd00367; PTS-HPr_like; 1.
DR Gene3D; 3.30.1340.10; HPr-like; 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; 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; IPR001020; PTS_HPr_His_P_site.
DR InterPro; IPR036618; PtsI_HPr-bd_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; PF00381; PTS-HPr; 1.
DR PRINTS; PR00107; PHOSPHOCPHPR.
DR SUPFAM; SSF47831; Enzyme I of the PEP:sugar phosphotransferase system HPr-binding (sub)domain; 1.
DR SUPFAM; SSF55594; HPr-like; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 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 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:EKT54249.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010290};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..135
FT /note="PTS EIIA type-4"
FT /evidence="ECO:0000259|PROSITE:PS51096"
FT DOMAIN 156..243
FT /note="HPr"
FT /evidence="ECO:0000259|PROSITE:PS51350"
FT COILED 121..148
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 285..323
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 481 AA; 52601 MW; D7D388D08F3CEB15 CRC64;
MIGLIIISHS KMLADGLLQL AEQMQDKKNC QIIAAAGIDD EEHPIGTDAI KVMEAIETLS
EASHIILLMD LGSALLSAET ALDLIDPDLA QKVYLCSAPL VEGTIAITAA TSGGASIDTV
LEEARQALRS KQQQLNDEST EAASQETEQS KLSDKAIKSE WIVKNPSGLH VRPAAKLAAL
LSGFDVDVEL CKDKKYADAK SMNQIALLQV RYGDKITLIA EGPDSATAIT AFEQLAKQNF
GDDIHTNGKT VLNGKNIYTP TVSGVAYHWK STTEYSSLDK EHLDNESIEN RINKVTQAIT
LLKKQLEVRA NNLTEQLGKS IADIFRGHSL LLDDDDIIDA IKYEIKDNNS SIYDAINFVF
NEMSAQYKQL DDPYLQARYI DIDDLKNQLL MLIFAIKPQQ INLTVPSIIL SDNMGPSEIL
RCQHPMVSGV ILANGSPYSH TSIIAARLGI PMLVDIGETI NDIKEKAKLT ISIDDASLTI
E
//
