ID LERK_PECAS Reviewed; 590 AA.
AC Q6D8V6;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=L-erythrulose kinase {ECO:0000303|PubMed:29867142};
DE EC=2.7.1.209 {ECO:0000269|PubMed:29867142};
GN Name=lerK {ECO:0000303|PubMed:29867142};
GN OrderedLocusNames=ECA0866 {ECO:0000312|EMBL:CAG73778.1};
OS Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS carotovora subsp. atroseptica).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=218491;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCRI 1043 / ATCC BAA-672;
RX PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT subsp. atroseptica and characterization of virulence factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RX PubMed=29867142; DOI=10.1038/s41589-018-0067-7;
RA Carter M.S., Zhang X., Huang H., Bouvier J.T., Francisco B.S.,
RA Vetting M.W., Al-Obaidi N., Bonanno J.B., Ghosh A., Zallot R.G.,
RA Andersen H.M., Almo S.C., Gerlt J.A.;
RT "Functional assignment of multiple catabolic pathways for D-apiose.";
RL Nat. Chem. Biol. 14:696-705(2018).
CC -!- FUNCTION: Involved in catabolism of D-apiose. Catalyzes the
CC phosphorylation of L-erythrulose to L-erythrulose 1-phosphate
CC (PubMed:29867142). Can also phosphorylate D-erythrulose and
CC dihydroxyacetone in vitro (PubMed:29867142).
CC {ECO:0000269|PubMed:29867142}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-erythrulose = ADP + H(+) + L-erythrulose 1-phosphate;
CC Xref=Rhea:RHEA:48780, ChEBI:CHEBI:15378, ChEBI:CHEBI:27913,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58002, ChEBI:CHEBI:456216;
CC EC=2.7.1.209; Evidence={ECO:0000269|PubMed:29867142};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.007 mM for L-erythrulose {ECO:0000269|PubMed:29867142};
CC KM=0.005 mM for D-erythrulose {ECO:0000269|PubMed:29867142};
CC KM=0.015 mM for dihydroxyacetone {ECO:0000269|PubMed:29867142};
CC Note=kcat is 2.76 sec(-1) with L-erythrulose as substrate. kcat is
CC 0.72 sec(-1) with D-erythrulose as substrate. kcat is 1.34 sec(-1)
CC with dihydroxyacetone as substrate. {ECO:0000269|PubMed:29867142};
CC -!- PATHWAY: Carbohydrate metabolism. {ECO:0000269|PubMed:29867142}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX950851; CAG73778.1; -; Genomic_DNA.
DR RefSeq; WP_011092469.1; NC_004547.2.
DR AlphaFoldDB; Q6D8V6; -.
DR SMR; Q6D8V6; -.
DR STRING; 218491.ECA0866; -.
DR KEGG; eca:ECA0866; -.
DR PATRIC; fig|218491.5.peg.866; -.
DR eggNOG; COG2376; Bacteria.
DR HOGENOM; CLU_017054_6_1_6; -.
DR OrthoDB; 9806345at2; -.
DR BioCyc; MetaCyc:MONOMER-20962; -.
DR SABIO-RK; Q6D8V6; -.
DR Proteomes; UP000007966; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004371; F:glycerone kinase activity; IEA:InterPro.
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 1: Evidence at protein level;
KW ATP-binding; Carbohydrate metabolism; Kinase; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..590
FT /note="L-erythrulose kinase"
FT /id="PRO_0000446039"
FT DOMAIN 7..331
FT /note="DhaK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00814"
FT DOMAIN 366..568
FT /note="DhaL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00813"
FT ACT_SITE 217
FT /note="Tele-hemiaminal-histidine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00814"
FT BINDING 398..401
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P76014"
FT BINDING 441..442
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P76014"
FT BINDING 483
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P76014"
FT BINDING 540
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P76014"
FT BINDING 553..555
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P76014"
SQ SEQUENCE 590 AA; 61435 MW; 9CA3A43095E84BE4 CRC64;
MTYLFNQPSS FARELTEGFV AAHADKVRQV PGGVVRSTRS REGGVAIVVG GGSGHYPAFA
GLVGQGLAHG AAMGNLFASP SAQQICSVAR AAHNGGGVLL TFGNYAGDVL HFGQAKARLN
AEGIPCELLA VTDDISSAPL NEWQKRRGVA GDLMVFKAVS AAAEAGYDLA AVLEVAERAN
QRTRSLGVAF SGCTLPGAEH PLFTVPEGMM AVGMGIHGEP GIRDVPISTA DELAELLVSS
LLKEVPHGIT TLSGQRISVV LNGLGGVKYE ELFVVYRRVS QLLVEQGLTV VEPEVGELVT
SFNMAGLSLT LFWLDEELER FWRAPADAPA FRKGSMSPGE PLAERTFVAE LEVIPNATAA
SKAAAHCVAA ALNAARDIVL ANVTELGRID AIAGDGDHGI GMERGVIAAA DKATEMLERQ
AGAGTLLQRA ADAWADQAGG TSGAIWGVAL NALGTVLGDE QRPDGRRVAD GVRQAKESVM
HFGKAKPGDK TLVDALIPFS LALTQRVETG MSLPEAWQQA AQCAQQAADD TAQLLPKIGR
ARPLAEKSLG TPDAGAISLA MILDAVSAVL NSDTTSTSSH QTATQAESER
//
