LERK_MYCS2
ID LERK_MYCS2 Reviewed; 571 AA.
AC A0R758;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=L-erythrulose 1-kinase {ECO:0000305|PubMed:26978037};
DE EC=2.7.1.209 {ECO:0000269|PubMed:26560079, ECO:0000305|PubMed:26978037};
GN Name=lerK {ECO:0000303|PubMed:26560079};
GN OrderedLocusNames=MSMEG_6788 {ECO:0000312|EMBL:ABK72124.1},
GN MSMEI_6605 {ECO:0000312|EMBL:AFP43031.1};
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, INDUCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=26560079; DOI=10.1021/jacs.5b08968;
RA Huang H., Carter M.S., Vetting M.W., Al-Obaidi N., Patskovsky Y.,
RA Almo S.C., Gerlt J.A.;
RT "A general strategy for the discovery of metabolic pathways: D-threitol, L-
RT threitol, and erythritol utilization in Mycobacterium smegmatis.";
RL J. Am. Chem. Soc. 137:14570-14573(2015).
RN [5]
RP ERRATUM OF PUBMED:26560079, AND CORRECTION TO PRODUCT IDENTIFICATION.
RX PubMed=26978037; DOI=10.1021/jacs.6b01906;
RA Huang H., Carter M.S., Vetting M.W., Al-Obaidi N., Patskovsky Y.,
RA Almo S.C., Gerlt J.A.;
RT "Correction to 'A general strategy for the discovery of metabolic pathways:
RT D-threitol, L-threitol, and erythritol utilization in Mycobacterium
RT smegmatis'.";
RL J. Am. Chem. Soc. 138:4267-4267(2016).
CC -!- FUNCTION: Kinase that has a preference for L-erythrulose, producing L-
CC erythrulose-1P. Involved in the degradation pathway of L-threitol, that
CC allows M.smegmatis to grow on this compound as the sole carbon source.
CC Is also able to phosphorylate D-erythrulose and dihydroxyacetone in
CC vitro. {ECO:0000269|PubMed:26560079, ECO:0000269|PubMed:26978037}.
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:26560079,
CC ECO:0000305|PubMed:26978037};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.0 uM for L-erythrulose {ECO:0000269|PubMed:26560079};
CC KM=10.6 uM for D-erythrulose {ECO:0000269|PubMed:26560079};
CC KM=37.8 uM for dihydroxyacetone {ECO:0000269|PubMed:26560079};
CC Note=kcat is 1.79 sec(-1) with L-erythrulose as substrate. kcat is
CC 1.60 sec(-1) with D-erythrulose as substrate. kcat is 2.12 sec(-1)
CC with dihydroxyacetone as substrate. {ECO:0000269|PubMed:26560079};
CC -!- PATHWAY: Carbohydrate metabolism; L-threitol degradation.
CC {ECO:0000269|PubMed:26560079}.
CC -!- INDUCTION: Slightly up-regulated during growth on L-threitol relative
CC to growth on glycerol. {ECO:0000269|PubMed:26560079}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are totally unable to
CC grow on L-threitol. {ECO:0000269|PubMed:26560079}.
CC -!- CAUTION: The product of the reaction was originally identified as L-
CC erythrulose 4-phosphate (PubMed:26560079). It was then corrected to L-
CC erythrulose 1-phosphate by the same group (PubMed:26978037).
CC {ECO:0000269|PubMed:26560079, ECO:0000269|PubMed:26978037}.
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DR EMBL; CP000480; ABK72124.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP43031.1; -; Genomic_DNA.
DR RefSeq; WP_003898168.1; NZ_SIJM01000001.1.
DR RefSeq; YP_890996.1; NC_008596.1.
DR AlphaFoldDB; A0R758; -.
DR SMR; A0R758; -.
DR STRING; 246196.MSMEI_6605; -.
DR EnsemblBacteria; ABK72124; ABK72124; MSMEG_6788.
DR EnsemblBacteria; AFP43031; AFP43031; MSMEI_6605.
DR GeneID; 66738045; -.
DR KEGG; msg:MSMEI_6605; -.
DR KEGG; msm:MSMEG_6788; -.
DR PATRIC; fig|246196.19.peg.6608; -.
DR eggNOG; COG2376; Bacteria.
DR OMA; CRTIICG; -.
DR OrthoDB; 857242at2; -.
DR BioCyc; MetaCyc:MON-19893; -.
DR BRENDA; 2.7.1.209; 3512.
DR UniPathway; UPA01067; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IDA:UniProtKB.
DR GO; GO:0019200; F:carbohydrate kinase activity; IDA:UniProtKB.
DR GO; GO:0004371; F:glycerone kinase activity; IEA:InterPro.
DR GO; GO:0016052; P:carbohydrate catabolic process; IMP:UniProtKB.
DR GO; GO:0009758; P:carbohydrate utilization; IMP:UniProtKB.
DR GO; GO:0071322; P:cellular response to carbohydrate stimulus; IDA:UniProtKB.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:InterPro.
DR Gene3D; 1.25.40.340; -; 1.
DR InterPro; IPR004006; DhaK_dom.
DR InterPro; IPR004007; DhaL_dom.
DR InterPro; IPR036117; DhaL_dom_sf.
DR Pfam; PF02733; Dak1; 1.
DR Pfam; PF02734; Dak2; 1.
DR SMART; SM01120; Dak2; 1.
DR SUPFAM; SSF101473; SSF101473; 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..571
FT /note="L-erythrulose 1-kinase"
FT /id="PRO_0000435516"
FT DOMAIN 7..331
FT /note="DhaK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00814"
FT DOMAIN 367..567
FT /note="DhaL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00813"
FT ACT_SITE 217
FT /note="Tele-hemiaminal-histidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P76015"
FT BINDING 396..402
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P76014"
FT BINDING 442..443
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P76014"
FT BINDING 484
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P76014"
FT BINDING 539
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P76014"
FT BINDING 552..554
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P76014"
SQ SEQUENCE 571 AA; 59357 MW; C5E6A4FA68085E9C CRC64;
MTYLLNSPDD FADEAVRGLV AANPDLLTEV PGGVVRSTET PKGQPALVIG GGSGHYPAFA
GWVGPGMGHG APCGNIFSSP SASEVYSVVR NAENGGGVIL GFGNYAGDVL HFGLAAEKLR
HEGIDVRIVT VSDDIASNSP ENHRDRRGVA GDLPVFKIAG AAIEAGADLD EAERVAWKAN
DATRSFGLAF EGCTLPGATE PLFHVEKGWM GVGLGIHGEP GVRDNRLGTA AEVADMLFDE
VTAEEPPRGE NGYDGRVAVI LNGLGTVKYE ELFVVYGRIA ERLAQQGFTV VRPEVGEFVT
SLDMAGVSLT MVFLDDELER LWTAPVETPA YRRGAMPAVD RTPRTTTWDA AETTIPEASE
GSRECARNIV AVLETFQQVC ADNEAELGRI DAVAGDGDHG QGMSFGSRGA AQAARDAVDR
NAGARTTLLL AGQAWADAAG GTSGALWGAA LTSAGGVFSD TDGADEQAAV DAICAGIDAI
LRLGGAQPGD KTMVDAAVPF RDALVKAFDT QAGPAITSAA RVAREAAEKT ADITARRGRA
RVLGEKSVGT PDPGALSFAM LMKALGEHLT R
