DHAM_LACLA
ID DHAM_LACLA Reviewed; 123 AA.
AC Q9CIV6;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=PTS-dependent dihydroxyacetone kinase, phosphotransferase subunit DhaM {ECO:0000303|PubMed:18957416};
DE EC=2.7.1.121 {ECO:0000250|UniProtKB:Q92ET9};
DE AltName: Full=PTS system EIIA component {ECO:0000303|PubMed:18957416};
DE AltName: Full=Phosphotransferase enzyme IIA component {ECO:0000303|PubMed:18957416};
GN Name=dhaM {ECO:0000303|PubMed:18957416}; OrderedLocusNames=LL0250;
GN ORFNames=L47257;
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 (1.10 ANGSTROMS), FUNCTION, ACTIVE SITE, INDUCTION,
RP AND SUBUNIT.
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: 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:0000305|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:Q92ET9};
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 -!- DOMAIN: The EIIA type-4 domain is phosphorylated by phospho-HPr on a
CC histidyl residue. Then, it transfers the phosphoryl group to the EIIB
CC type-4 domain. {ECO:0000255|PROSITE-ProRule:PRU00419}.
CC -!- MISCELLANEOUS: Unlike the carbohydrate-specific transporters of the
CC PTS, the complex DhaKML has no transport activity.
CC {ECO:0000305|PubMed:18957416}.
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DR EMBL; AE005176; AAK04348.1; -; Genomic_DNA.
DR PIR; B86656; B86656.
DR RefSeq; NP_266406.1; NC_002662.1.
DR RefSeq; WP_010905237.1; NC_002662.1.
DR PDB; 3CR3; X-ray; 2.10 A; C/D=3-123.
DR PDB; 3CT6; X-ray; 1.10 A; A/B=1-123.
DR PDBsum; 3CR3; -.
DR PDBsum; 3CT6; -.
DR AlphaFoldDB; Q9CIV6; -.
DR SMR; Q9CIV6; -.
DR STRING; 272623.L47257; -.
DR PaxDb; Q9CIV6; -.
DR EnsemblBacteria; AAK04348; AAK04348; L47257.
DR GeneID; 66441211; -.
DR KEGG; lla:L47257; -.
DR PATRIC; fig|272623.7.peg.275; -.
DR eggNOG; COG3412; Bacteria.
DR HOGENOM; CLU_045361_1_0_9; -.
DR OMA; IQMDEKP; -.
DR UniPathway; UPA00616; -.
DR EvolutionaryTrace; Q9CIV6; -.
DR Proteomes; UP000002196; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.510; -; 1.
DR InterPro; IPR039643; DhaM.
DR InterPro; IPR012844; DhaM_N.
DR InterPro; IPR004701; PTS_EIIA_man-typ.
DR InterPro; IPR036662; PTS_EIIA_man-typ_sf.
DR PANTHER; PTHR38594; PTHR38594; 1.
DR Pfam; PF03610; EIIA-man; 1.
DR SUPFAM; SSF53062; SSF53062; 1.
DR TIGRFAMs; TIGR02364; dha_pts; 1.
DR PROSITE; PS51096; PTS_EIIA_TYPE_4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Glycerol metabolism; Kinase; Nucleotide-binding;
KW Phosphotransferase system; Reference proteome; Transferase.
FT CHAIN 1..123
FT /note="PTS-dependent dihydroxyacetone kinase,
FT phosphotransferase subunit DhaM"
FT /id="PRO_0000270537"
FT DOMAIN 2..123
FT /note="PTS EIIA type-4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00419,
FT ECO:0000305|PubMed:18957416"
FT ACT_SITE 10
FT /note="Tele-phosphohistidine intermediate; for EIIA
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00419"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:3CT6"
FT HELIX 12..23
FT /evidence="ECO:0007829|PDB:3CT6"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:3CT6"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:3CT6"
FT HELIX 46..55
FT /evidence="ECO:0007829|PDB:3CT6"
FT STRAND 59..67
FT /evidence="ECO:0007829|PDB:3CT6"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:3CT6"
FT HELIX 71..79
FT /evidence="ECO:0007829|PDB:3CT6"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:3CT6"
FT HELIX 92..104
FT /evidence="ECO:0007829|PDB:3CT6"
FT HELIX 109..116
FT /evidence="ECO:0007829|PDB:3CT6"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:3CT6"
SQ SEQUENCE 123 AA; 13394 MW; 972B8CBAE069568A CRC64;
MTYGIVIVSH SPEIASGLKK LIREVAKNIS LTAIGGLENG EIGTSFDRVM NAIEENEADN
LLTFFDLGSA RMNLDLVSEM TDKELTIFNV PLIEGAYTAS ALLEAGATFE AIKEQLEKML
IEK
