DHAK_LACLA
ID DHAK_LACLA Reviewed; 332 AA.
AC Q9CIV8;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=PTS-dependent dihydroxyacetone kinase, dihydroxyacetone-binding subunit DhaK {ECO:0000303|PubMed:18957416};
DE EC=2.7.1.121 {ECO:0000250|UniProtKB:Q92EU2};
GN Name=dhaK {ECO:0000303|PubMed:18957416}; OrderedLocusNames=LL0248;
GN ORFNames=L45677;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH DIHYDROXYACETONE,
RP FUNCTION, SUBUNIT, ACTIVE SITE, AND INDUCTION.
RX PubMed=18957416; DOI=10.1074/jbc.m804893200;
RA Zurbriggen A., Jeckelmann J.M., Christen S., Bieniossek C., Baumann U.,
RA Erni B.;
RT "X-ray structures of the three Lactococcus lactis dihydroxyacetone kinase
RT subunits and of a transient intersubunit complex.";
RL J. Biol. Chem. 283:35789-35796(2008).
CC -!- FUNCTION: Dihydroxyacetone binding subunit of the dihydroxyacetone
CC kinase, which is responsible the phosphoenolpyruvate (PEP)-dependent
CC phosphorylation of dihydroxyacetone via a phosphoryl group transfer
CC from DhaL-ATP. {ECO:0000269|PubMed:18957416}.
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:0000250|UniProtKB:Q92EU2};
CC -!- PATHWAY: Polyol metabolism; glycerol degradation. {ECO:0000305}.
CC -!- SUBUNIT: Homodimer. The dihydroxyacetone kinase complex is composed of
CC a homodimer of DhaM, a homodimer of DhaK and the subunit DhaL.
CC {ECO:0000269|PubMed:18957416}.
CC -!- INDUCTION: Induced by dihydroxyacetone via the DhaQ-DhaS complex.
CC {ECO:0000305|PubMed:18957416}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK04346.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE005176; AAK04346.1; ALT_INIT; Genomic_DNA.
DR PIR; H86655; H86655.
DR RefSeq; NP_266404.2; NC_002662.1.
DR RefSeq; WP_010905235.1; NC_002662.1.
DR PDB; 3CT4; X-ray; 2.50 A; A/B/C=1-332.
DR PDBsum; 3CT4; -.
DR AlphaFoldDB; Q9CIV8; -.
DR SMR; Q9CIV8; -.
DR STRING; 272623.L45677; -.
DR PaxDb; Q9CIV8; -.
DR EnsemblBacteria; AAK04346; AAK04346; L45677.
DR KEGG; lla:L45677; -.
DR PATRIC; fig|272623.7.peg.273; -.
DR eggNOG; COG2376; Bacteria.
DR HOGENOM; CLU_017054_0_0_9; -.
DR OMA; MLSAACP; -.
DR UniPathway; UPA00616; -.
DR EvolutionaryTrace; Q9CIV8; -.
DR Proteomes; UP000002196; Chromosome.
DR GO; GO:0004371; F:glycerone kinase activity; IEA:InterPro.
DR GO; GO:0047324; F:phosphoenolpyruvate-glycerone phosphotransferase activity; ISS:UniProtKB.
DR GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR InterPro; IPR012736; DhaK_1.
DR InterPro; IPR004006; DhaK_dom.
DR Pfam; PF02733; Dak1; 1.
DR TIGRFAMs; TIGR02363; dhaK1; 1.
DR PROSITE; PS51481; DHAK; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycerol metabolism; Kinase; Reference proteome; Transferase.
FT CHAIN 1..332
FT /note="PTS-dependent dihydroxyacetone kinase,
FT dihydroxyacetone-binding subunit DhaK"
FT /id="PRO_0000270534"
FT DOMAIN 9..331
FT /note="DhaK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00814"
FT ACT_SITE 58
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P76015"
FT ACT_SITE 220
FT /note="Tele-hemiaminal-histidine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00814,
FT ECO:0000269|PubMed:18957416, ECO:0007744|PDB:3CT4"
FT BINDING 55..58
FT /ligand="dihydroxyacetone"
FT /ligand_id="ChEBI:CHEBI:16016"
FT /evidence="ECO:0000269|PubMed:18957416,
FT ECO:0007744|PDB:3CT4"
FT BINDING 106
FT /ligand="dihydroxyacetone"
FT /ligand_id="ChEBI:CHEBI:16016"
FT /evidence="ECO:0000269|PubMed:18957416,
FT ECO:0007744|PDB:3CT4"
FT BINDING 111
FT /ligand="dihydroxyacetone"
FT /ligand_id="ChEBI:CHEBI:16016"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00814,
FT ECO:0000269|PubMed:18957416, ECO:0007744|PDB:3CT4"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:3CT4"
FT HELIX 13..24
FT /evidence="ECO:0007829|PDB:3CT4"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:3CT4"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:3CT4"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:3CT4"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:3CT4"
FT STRAND 49..58
FT /evidence="ECO:0007829|PDB:3CT4"
FT TURN 59..62
FT /evidence="ECO:0007829|PDB:3CT4"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:3CT4"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:3CT4"
FT STRAND 70..79
FT /evidence="ECO:0007829|PDB:3CT4"
FT HELIX 85..95
FT /evidence="ECO:0007829|PDB:3CT4"
FT STRAND 101..107
FT /evidence="ECO:0007829|PDB:3CT4"
FT HELIX 109..124
FT /evidence="ECO:0007829|PDB:3CT4"
FT STRAND 129..134
FT /evidence="ECO:0007829|PDB:3CT4"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:3CT4"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:3CT4"
FT HELIX 155..167
FT /evidence="ECO:0007829|PDB:3CT4"
FT HELIX 172..183
FT /evidence="ECO:0007829|PDB:3CT4"
FT STRAND 186..194
FT /evidence="ECO:0007829|PDB:3CT4"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:3CT4"
FT STRAND 225..229
FT /evidence="ECO:0007829|PDB:3CT4"
FT HELIX 233..248
FT /evidence="ECO:0007829|PDB:3CT4"
FT STRAND 255..262
FT /evidence="ECO:0007829|PDB:3CT4"
FT STRAND 264..266
FT /evidence="ECO:0007829|PDB:3CT4"
FT HELIX 268..283
FT /evidence="ECO:0007829|PDB:3CT4"
FT STRAND 288..295
FT /evidence="ECO:0007829|PDB:3CT4"
FT STRAND 305..312
FT /evidence="ECO:0007829|PDB:3CT4"
FT HELIX 316..322
FT /evidence="ECO:0007829|PDB:3CT4"
SQ SEQUENCE 332 AA; 36243 MW; FE475501D3D8BE11 CRC64;
MSDEKIINQP QDVVSEMLDG LTYAYGDLIE KVPDFEIIQR KSPKSGKVAL VSGGGSGHKP
AHAGFVGEGM LSAAVCGAIF TSPTPDQIYE AIKSADEGAG VLLIIKNYLG DVMNFEMARE
MAEMEEIKVE QIIVDDDIAV ENSLYTQGRR GVAGTVLVHK ILGAAAHQEA SLDEIKDLAD
KVVKNIKTIG LALSAATVPE VGKPGFVLDD NEIEYGVGIH SEPGYRREKM KTSYELATEL
VGKLKEEFKF EAGQKYGILV NGMGATPLME QFIFMNDVAK LLTEENIEIL FKKVGNYMTS
IDMAGLSLTM IKLEDDQWLK NLNEDVKTIS WG
