DHAK2_LISIN
ID DHAK2_LISIN Reviewed; 331 AA.
AC Q92EU2;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=PTS-dependent dihydroxyacetone kinase 2, dihydroxyacetone-binding subunit DhaK {ECO:0000305|PubMed:22773791};
DE EC=2.7.1.121 {ECO:0000305|PubMed:22773791};
GN Name=dhaK-2 {ECO:0000303|PubMed:22773791};
GN OrderedLocusNames=lin0366 {ECO:0000312|EMBL:CAC95599.1};
OS Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=272626 {ECO:0000312|Proteomes:UP000002513};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-680 / CLIP 11262;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, INDUCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC BAA-680 / CLIP 11262;
RX PubMed=22773791; DOI=10.1128/jb.00801-12;
RA Monniot C., Zebre A.C., Ake F.M., Deutscher J., Milohanic E.;
RT "Novel listerial glycerol dehydrogenase- and phosphoenolpyruvate-dependent
RT dihydroxyacetone kinase system connected to the pentose phosphate
RT pathway.";
RL J. Bacteriol. 194:4972-4982(2012).
CC -!- FUNCTION: Dihydroxyacetone binding subunit of the dihydroxyacetone
CC kinase, which is responsible for the phosphoenolpyruvate (PEP)-
CC dependent phosphorylation of dihydroxyacetone via a phosphoryl group
CC transfer from DhaL-ATP. {ECO:0000305|PubMed:22773791}.
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:0000305|PubMed:22773791};
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:0000250|UniProtKB:Q9CIV8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:22773791}.
CC -!- INDUCTION: Repressed by GolR. {ECO:0000269|PubMed:22773791}.
CC -!- MISCELLANEOUS: Unlike the carbohydrate-specific transporters of the
CC PTS, the complex DhaKML has no transport activity.
CC {ECO:0000305|PubMed:22773791}.
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DR EMBL; AL596164; CAC95599.1; -; Genomic_DNA.
DR PIR; AG1478; AG1478.
DR RefSeq; WP_003770294.1; NC_003212.1.
DR AlphaFoldDB; Q92EU2; -.
DR SMR; Q92EU2; -.
DR STRING; 272626.lin0366; -.
DR EnsemblBacteria; CAC95599; CAC95599; CAC95599.
DR GeneID; 61169373; -.
DR KEGG; lin:lin0366; -.
DR eggNOG; COG2376; Bacteria.
DR HOGENOM; CLU_017054_0_0_9; -.
DR OMA; DLDWVKW; -.
DR OrthoDB; 857242at2; -.
DR UniPathway; UPA00616; -.
DR Proteomes; UP000002513; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004371; F:glycerone kinase activity; IEA:InterPro.
DR GO; GO:0047324; F:phosphoenolpyruvate-glycerone phosphotransferase activity; IDA:UniProtKB.
DR GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR InterPro; IPR004006; DhaK_dom.
DR Pfam; PF02733; Dak1; 1.
DR PROSITE; PS51481; DHAK; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Glycerol metabolism; Kinase; Transferase.
FT CHAIN 1..331
FT /note="PTS-dependent dihydroxyacetone kinase 2,
FT dihydroxyacetone-binding subunit DhaK"
FT /id="PRO_0000439399"
FT DOMAIN 7..328
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 218
FT /note="Tele-hemiaminal-histidine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00814"
FT BINDING 55..58
FT /ligand="dihydroxyacetone"
FT /ligand_id="ChEBI:CHEBI:16016"
FT /evidence="ECO:0000250|UniProtKB:Q9CIV8,
FT ECO:0000255|PROSITE-ProRule:PRU00814"
FT BINDING 111
FT /ligand="dihydroxyacetone"
FT /ligand_id="ChEBI:CHEBI:16016"
FT /evidence="ECO:0000250|UniProtKB:Q9CIV8,
FT ECO:0000255|PROSITE-ProRule:PRU00814"
SQ SEQUENCE 331 AA; 35702 MW; C5A12BCBF15516F1 CRC64;
MRRLVNDGYE AVEEMLAGYV AAQGKYVDFA ENDKRVIVSK QMSEEPRVRI IVGGGSGHEP
LFLGYVGKDF ADAAVVGNIN TSPSPEPCYN AVKAVDSGKG CLYMYGNYAG DVMNFDMGAE
MAADDGIRVE TVLVTDDIYS AENVEDRRGV AGDLIVFKAA ASAAAKGLDL DAVKQAAEKA
NANTFSMGVA LSSSTLPVTG KAIFEMKEGE MEVGMGIHGE PGIKRTSIEP ADKVVDQIMG
YLIEEMKLTA GEEVHVLING LGGLPVMDQY ICYRRVDEIL KEKGVHIHSP LVGNYATSMD
MIGMSITLVR LDDELKDLLD TPCDTPYFKV D
