ID B7LT27_ESCF3 Unreviewed; 584 AA.
AC B7LT27;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Dihydroxyacetone kinase {ECO:0000313|EMBL:CAQ87990.1};
DE EC=2.7.1.29 {ECO:0000313|EMBL:CAQ87990.1};
GN OrderedLocusNames=EFER_0430 {ECO:0000313|EMBL:CAQ87990.1};
OS Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM
OS 14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585054 {ECO:0000313|EMBL:CAQ87990.1, ECO:0000313|Proteomes:UP000000745};
RN [1] {ECO:0000313|Proteomes:UP000000745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35469 / DSM 13698 / BCRC 15582 / CCUG 18766 / IAM 14443 /
RC JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73
RC {ECO:0000313|Proteomes:UP000000745};
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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DR EMBL; CU928158; CAQ87990.1; -; Genomic_DNA.
DR RefSeq; WP_000220049.1; NC_011740.1.
DR AlphaFoldDB; B7LT27; -.
DR GeneID; 75058497; -.
DR KEGG; efe:EFER_0430; -.
DR HOGENOM; CLU_017054_6_1_6; -.
DR OrthoDB; 9806345at2; -.
DR Proteomes; UP000000745; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004371; F:glycerone kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.340; -; 1.
DR InterPro; IPR004006; DhaK_dom.
DR InterPro; IPR004007; DhaL_dom.
DR InterPro; IPR036117; DhaL_dom_sf.
DR PANTHER; PTHR28629; TRIOKINASE/FMN CYCLASE; 1.
DR PANTHER; PTHR28629:SF4; TRIOKINASE_FMN CYCLASE; 1.
DR Pfam; PF02733; Dak1; 1.
DR Pfam; PF02734; Dak2; 1.
DR SMART; SM01120; Dak2; 1.
DR SUPFAM; SSF82549; DAK1/DegV-like; 1.
DR SUPFAM; SSF101473; DhaL-like; 1.
DR PROSITE; PS51481; DHAK; 1.
DR PROSITE; PS51480; DHAL; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CAQ87990.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CAQ87990.1}.
FT DOMAIN 7..330
FT /note="DhaK"
FT /evidence="ECO:0000259|PROSITE:PS51481"
FT DOMAIN 366..568
FT /note="DhaL"
FT /evidence="ECO:0000259|PROSITE:PS51480"
SQ SEQUENCE 584 AA; 60443 MW; 63683034FA0ACD67 CRC64;
MTWLFNNPSD FAKEMVAGFV SANADIVRQV PGGVIRNTQS QQGTVAIIIG GGSGHYPAFA
GLVGQGLAHG AAMGNLFASP SAQQICSVAK AANNGAGVLL AFGNYAGDVL HFGLARERLI
AEGIPCELIA VTDDITSAGQ HEPEKRRGVA GDLVVFKAAA AAAEQGASLE EVLTVARHAN
DRTRTIGVAF SGCTLPGAEQ PLFTIPQGQM GFGMGIHGEP GIREIAVPGA DELATMLVEH
LLNDVPSGVS IKGARVGAIL NGLGSVKYEE LFVVWHSVQQ RLNEQGIILA DIQVGEFVTS
FDMAGLSLTL IWFSEALEAQ WQAPAYTSAF RRGAVIAAQP RQASSDDECQ QQTVPAASDA
SRSAAVRVVA MVDALAEVVI ANVDELGRID AVAGDGDHGM GMERGVRAAR ESAHQYLALG
AGAGTVLQQA ADAWADNAGG TSGAIWGVIL NTLGTALGNQ QQPQADTVVQ AVSDAAHGVM
HFGKAKPGDK TLVDVLLPFS EALNENVKKG LPLAQAWHAA ASYAQQCAKD TSQLLPKIGR
ARPLAERSLG TPDAGAVSLA MIVTAVGGCF TEAAGREKEG AVWQ
//
