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Database: UniProt
Entry: Q0T5J7_SHIF8
LinkDB: Q0T5J7_SHIF8
Original site: Q0T5J7_SHIF8 
ID   Q0T5J7_SHIF8            Unreviewed;       449 AA.
AC   Q0T5J7;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   24-JAN-2024, entry version 108.
DE   RecName: Full=phosphoenolpyruvate--glycerone phosphotransferase {ECO:0000256|ARBA:ARBA00012095};
DE            EC=2.7.1.121 {ECO:0000256|ARBA:ARBA00012095};
GN   Name=ycgC {ECO:0000313|EMBL:ABF03418.1};
GN   OrderedLocusNames=SFV_1212 {ECO:0000313|EMBL:ABF03418.1};
OS   Shigella flexneri serotype 5b (strain 8401).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=373384 {ECO:0000313|EMBL:ABF03418.1, ECO:0000313|Proteomes:UP000000659};
RN   [1] {ECO:0000313|EMBL:ABF03418.1, ECO:0000313|Proteomes:UP000000659}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8401 {ECO:0000313|EMBL:ABF03418.1,
RC   ECO:0000313|Proteomes:UP000000659};
RX   PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA   Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA   Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT   "Complete genome sequence of Shigella flexneri 5b and comparison with
RT   Shigella flexneri 2a.";
RL   BMC Genomics 7:173-173(2006).
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}.
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DR   EMBL; CP000266; ABF03418.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0T5J7; -.
DR   KEGG; sfv:SFV_1212; -.
DR   HOGENOM; CLU_045361_0_0_6; -.
DR   OMA; TDHVLVM; -.
DR   Proteomes; UP000000659; 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:InterPro.
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; IPR039643; DhaM.
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; 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; 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   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..112
FT                   /note="PTS EIIA type-4"
FT                   /evidence="ECO:0000259|PROSITE:PS51096"
FT   DOMAIN          132..219
FT                   /note="HPr"
FT                   /evidence="ECO:0000259|PROSITE:PS51350"
SQ   SEQUENCE   449 AA;  48980 MW;  A4364D93654E8BC3 CRC64;
     MLMSDSCKIA IAAGIDDPQN PIGTDAVKVM EAIESVADAD HVLVMMDMGS ALLSAETALE
     LLAPEIAAKV RLCAAPLVEG TLAATVSAAS GADIDKVIFD AMHALEAKRE QLGLPSSDTE
     ISDTCPPYDE EARSLAVVIK NRNGLHVRPA SRLVYTLSTF NADMLLEKNG KCVTPESINQ
     IALLQVRYND TLRLIAKGPE AEEALIAFRH LAEDNFGETE EVAPPTLRPV LPVSGKAFYY
     QPVLCTVQAK STLTAEEEQD RLRQAIDFTL LDLMTLTAKA EASGLDDIAA IFSGHHTLLG
     DPELLAAASE LLQHEHCTAE YAWQQVLKEL SQQYQQLDDE YLQARYIDVD DLLHRTLVHL
     TQTKEELPQF NSPTILLAEN IYPSTVLQLD PAVVKGICLS AGSPVSHSAL IARELGIGWI
     CQQGEKLYAI QPEETLTLDV KTQRFNRQG
//
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