DHAM_KLEOK
ID DHAM_KLEOK Reviewed; 472 AA.
AC A0A0H3H456;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=PEP-dependent dihydroxyacetone kinase, phosphoryl donor subunit DhaM {ECO:0000250|UniProtKB:P37349};
DE EC=2.7.1.121 {ECO:0000250|UniProtKB:P37349};
DE AltName: Full=Dihydroxyacetone kinase subunit M {ECO:0000250|UniProtKB:P37349};
GN Name=dhaM {ECO:0000250|UniProtKB:P37349};
GN OrderedLocusNames=KOX_03180 {ECO:0000312|EMBL:AEX02377.1};
OS Klebsiella oxytoca (strain ATCC 8724 / DSM 4798 / JCM 20051 / NBRC 3318 /
OS NRRL B-199 / KCTC 1686 / BUCSAV 143 / CCM 1901).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=1006551;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8724 / DSM 4798 / JCM 20051 / NBRC 3318 / NRRL B-199 / KCTC
RC 1686 / BUCSAV 143 / CCM 1901;
RX PubMed=22493189; DOI=10.1128/jb.00026-12;
RA Shin S.H., Kim S., Kim J.Y., Lee S., Um Y., Oh M.K., Kim Y.R., Lee J.,
RA Yang K.S.;
RT "Complete genome sequence of Klebsiella oxytoca KCTC 1686, used in
RT production of 2,3-butanediol.";
RL J. Bacteriol. 194:2371-2372(2012).
RN [2]
RP PROTEIN-LYSINE DEACETYLASE ACTIVITY, AND CAUTION.
RC STRAIN=ATCC 8724 / DSM 4798 / JCM 20051 / NBRC 3318 / NRRL B-199 / KCTC
RC 1686 / BUCSAV 143 / CCM 1901;
RX PubMed=26716769; DOI=10.7554/elife.05322;
RA Tu S., Guo S.J., Chen C.S., Liu C.X., Jiang H.W., Ge F., Deng J.Y.,
RA Zhou Y.M., Czajkowsky D.M., Li Y., Qi B.R., Ahn Y.H., Cole P.A., Zhu H.,
RA Tao S.C.;
RT "YcgC represents a new protein deacetylase family in prokaryotes.";
RL Elife 4:E05322-E05322(2015).
RN [3]
RP NO PROTEIN-LYSINE DEACETYLASE ACTIVITY IN E.COLI ORTHOLOG, AND CAUTION.
RX PubMed=29939131; DOI=10.7554/elife.37798;
RA Kremer M., Kuhlmann N., Lechner M., Baldus L., Lammers M.;
RT "Comment on 'YcgC represents a new protein deacetylase family in
RT prokaryotes'.";
RL Elife 7:E37798-E37798(2018).
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:0000250|UniProtKB:P37349}.
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:P37349};
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:P37349}.
CC -!- DOMAIN: Consists of three domains. The N-terminal dimerization domain
CC has the same fold as the IIA domain of the mannose transporter of the
CC bacterial phosphoenolpyruvate:sugar phosphotransferase system (PTS).
CC The middle domain is similar to HPr and the C-terminus is similar to
CC the N-terminal domain of enzyme I (EI) of the PTS. The IIA domain of
CC DhaM (via phospho-His-9), instead of ATP, is the phosphoryl donor to
CC dihydroxyacetone (Dha). The phosphoryl flow likely involves HPr ('His-
CC 15') -> DhaM (His-432 -> His-170 -> His-9) -> DhaL-ADP -> Dha. The HPr-
CC like domain of DhaM cannot efficiently substitute for the general
CC carrier protein HPr. {ECO:0000250|UniProtKB:P37349}.
CC -!- MISCELLANEOUS: Unlike the carbohydrate-specific transporters of the
CC PTS, the complex DhaKLM has no transport activity.
CC {ECO:0000250|UniProtKB:P37349}.
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family. {ECO:0000305}.
CC -!- CAUTION: Was reported to be a protein deacetylase that removes acetyl
CC groups on specific lysine residues in target proteins
CC (PubMed:26716769). However, later experiments demonstrate that the
CC protein ortholog in E.coli does not have any protein deacetylase
CC activity; the discrepancy observed seems to be due to contaminants
CC having proteolytic activity (PubMed:29939131).
CC {ECO:0000269|PubMed:26716769, ECO:0000269|PubMed:29939131}.
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DR EMBL; CP003218; AEX02377.1; -; Genomic_DNA.
DR RefSeq; WP_014226903.1; NC_016612.1.
DR AlphaFoldDB; A0A0H3H456; -.
DR SMR; A0A0H3H456; -.
DR EnsemblBacteria; AEX02377; AEX02377; KOX_03180.
DR KEGG; kox:KOX_03180; -.
DR PATRIC; fig|1006551.4.peg.636; -.
DR HOGENOM; CLU_045361_0_0_6; -.
DR OMA; TDHVLVM; -.
DR Proteomes; UP000007843; Chromosome.
DR GO; GO:0016021; C:integral component of 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; 1.10.274.10; -; 1.
DR Gene3D; 3.30.1340.10; -; 1.
DR Gene3D; 3.40.50.510; -; 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 PANTHER; PTHR38594; PTHR38594; 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; SSF47831; 1.
DR SUPFAM; SSF52009; SSF52009; 1.
DR SUPFAM; SSF53062; SSF53062; 1.
DR SUPFAM; SSF55594; SSF55594; 1.
DR TIGRFAMs; TIGR02364; dha_pts; 1.
DR TIGRFAMs; TIGR01003; PTS_HPr_family; 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.
FT CHAIN 1..472
FT /note="PEP-dependent dihydroxyacetone kinase, phosphoryl
FT donor subunit DhaM"
FT /id="PRO_0000435889"
FT DOMAIN 1..135
FT /note="PTS EIIA type-4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00419"
FT DOMAIN 156..243
FT /note="HPr"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00681"
FT REGION 266..472
FT /note="PTS EI-like, N-terminal part"
FT /evidence="ECO:0000250|UniProtKB:P37349"
FT ACT_SITE 9
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00419"
FT ACT_SITE 170
FT /note="Pros-phosphohistidine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00681"
FT ACT_SITE 432
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P37349"
SQ SEQUENCE 472 AA; 50197 MW; E67D4B95245DE206 CRC64;
MVNLVIVSHS ARLGEGVGEL ARQMLMNDGC KLAIAAGIDD PASPIGTDPI KVMEAIESVA
DADHILVMMD IGSALLSAET ALDLLDPAIA AKVRLCAAPL VEGTLAATVS AAAGAGIDKV
IEDAMNALEA KRVQLGLPSQ PQHASLTAAP VDDRDARSVS VVIQNHNGLH VRPASKLVAA
LAGFNADLVL EKGGKCVTPD SLNQIALLQV RRNDTLRLLA RGPDADAALA AFQALAAENF
GEPTEAAPAR RPASADRVEG KVVLYPQPQD RISRETSAAI GQQQLRLKRA IDRTLEDLSA
LTTLAEATFS ADIAAIFSGH HTLLDDPDLY AAACDIIRDE QCSAAWAWQQ VLSDLSQQYR
HLDDAYLQAR YIDIEDILHR TLRHLNERNE ALPQFSAPSI LVADDIFPST VLQLNAEQVK
GICLQAGSEL SHGAIIARQA GIAMLCQQSD ALTLQDGENV ILDIPGKRVI RG
