ALSK_ECOLI
ID ALSK_ECOLI Reviewed; 309 AA.
AC P32718; Q2M6L9;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=D-allose kinase {ECO:0000255|HAMAP-Rule:MF_00988};
DE Short=Allokinase {ECO:0000255|HAMAP-Rule:MF_00988};
DE EC=2.7.1.55 {ECO:0000255|HAMAP-Rule:MF_00988};
GN Name=alsK {ECO:0000255|HAMAP-Rule:MF_00988}; Synonyms=yjcT;
GN OrderedLocusNames=b4084, JW5724;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION.
RC STRAIN=K12;
RX PubMed=9401019; DOI=10.1128/jb.179.24.7631-7637.1997;
RA Kim C., Song S., Park C.;
RT "The D-allose operon of Escherichia coli K-12.";
RL J. Bacteriol. 179:7631-7637(1997).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS,
RP AND MUTAGENESIS OF ALA-73 AND PHE-145.
RX PubMed=17979299; DOI=10.1021/bi700924d;
RA Larion M., Moore L.B., Thompson S.M., Miller B.G.;
RT "Divergent evolution of function in the ROK sugar kinase superfamily: role
RT of enzyme loops in substrate specificity.";
RL Biochemistry 46:13564-13572(2007).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
RG Joint Center for Structural Genomics (JCSG);
RT "Crystal structure of D-allose kinase (NP_418508.1) from Escherichia coli
RT K12 at 1.95 A resolution.";
RL Submitted (JUN-2009) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the phosphorylation of D-allose to D-allose 6-
CC phosphate. Has also low level glucokinase activity in vitro.
CC {ECO:0000255|HAMAP-Rule:MF_00988, ECO:0000269|PubMed:17979299,
CC ECO:0000269|PubMed:9401019}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-allose = ADP + D-allose 6-phosphate + H(+);
CC Xref=Rhea:RHEA:14805, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:40822, ChEBI:CHEBI:58328, ChEBI:CHEBI:456216;
CC EC=2.7.1.55; Evidence={ECO:0000255|HAMAP-Rule:MF_00988,
CC ECO:0000269|PubMed:17979299};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.19 mM for D-allose (at 25 degrees Celsius and pH 7.6)
CC {ECO:0000269|PubMed:17979299};
CC KM=0.27 mM for ATP (at 25 degrees Celsius and pH 7.6)
CC {ECO:0000269|PubMed:17979299};
CC KM=29 mM for D-glucose (at 25 degrees Celsius and pH 7.6)
CC {ECO:0000269|PubMed:17979299};
CC KM=210 mM for D-altrose (at 25 degrees Celsius and pH 7.6)
CC {ECO:0000269|PubMed:17979299};
CC KM=380 mM for 2'-deoxy-D-glucose (at 25 degrees Celsius and pH 7.6)
CC {ECO:0000269|PubMed:17979299};
CC KM=390 mM for D-mannose (at 25 degrees Celsius and pH 7.6)
CC {ECO:0000269|PubMed:17979299};
CC Note=Catalytic efficiency with D-allose as substrate is 735-fold
CC higher than that with D-glucose.;
CC -!- PATHWAY: Carbohydrate degradation; D-allose degradation.
CC {ECO:0000255|HAMAP-Rule:MF_00988}.
CC -!- SIMILARITY: Belongs to the ROK (NagC/XylR) family. {ECO:0000255|HAMAP-
CC Rule:MF_00988}.
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DR EMBL; U00006; AAC43178.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77045.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78087.1; -; Genomic_DNA.
DR PIR; C65217; C65217.
DR RefSeq; NP_418508.1; NC_000913.3.
DR RefSeq; WP_001171687.1; NZ_SSZK01000016.1.
DR PDB; 3HTV; X-ray; 1.95 A; A=1-309.
DR PDBsum; 3HTV; -.
DR AlphaFoldDB; P32718; -.
DR SMR; P32718; -.
DR BioGRID; 4262956; 15.
DR BioGRID; 852890; 2.
DR DIP; DIP-9097N; -.
DR IntAct; P32718; 4.
DR STRING; 511145.b4084; -.
DR PaxDb; P32718; -.
DR PRIDE; P32718; -.
DR DNASU; 948596; -.
DR EnsemblBacteria; AAC77045; AAC77045; b4084.
DR EnsemblBacteria; BAE78087; BAE78087; BAE78087.
DR GeneID; 948596; -.
DR KEGG; ecj:JW5724; -.
DR KEGG; eco:b4084; -.
DR PATRIC; fig|1411691.4.peg.2616; -.
DR EchoBASE; EB1899; -.
DR eggNOG; COG1940; Bacteria.
DR HOGENOM; CLU_036604_0_1_6; -.
DR InParanoid; P32718; -.
DR OMA; VNHLMLW; -.
DR PhylomeDB; P32718; -.
DR BioCyc; EcoCyc:EG11956-MON; -.
DR BioCyc; MetaCyc:EG11956-MON; -.
DR SABIO-RK; P32718; -.
DR UniPathway; UPA00361; -.
DR EvolutionaryTrace; P32718; -.
DR PRO; PR:P32718; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0008787; F:allose kinase activity; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0004340; F:glucokinase activity; IDA:EcoCyc.
DR GO; GO:0019316; P:D-allose catabolic process; IDA:EcoCyc.
DR GO; GO:0006351; P:transcription, DNA-templated; IBA:GO_Central.
DR HAMAP; MF_00988; Allose_kinase; 1.
DR InterPro; IPR030883; AlsK.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000600; ROK.
DR PANTHER; PTHR18964; PTHR18964; 1.
DR Pfam; PF00480; ROK; 1.
DR SUPFAM; SSF53067; SSF53067; 1.
DR PROSITE; PS01125; ROK; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Carbohydrate metabolism; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..309
FT /note="D-allose kinase"
FT /id="PRO_0000095688"
FT BINDING 10..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00988"
FT BINDING 142..149
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00988"
FT MUTAGEN 73
FT /note="A->G: 60-fold increase in catalytic efficiency for
FT glucose phosphorylation. 45-fold increase in D-glucose
FT affinity. No change in catalytic efficiency for D-allose
FT phosphorylation."
FT /evidence="ECO:0000269|PubMed:17979299"
FT MUTAGEN 145
FT /note="F->L: 10-fold increase in catalytic efficiency for
FT glucose phosphorylation. Slight increase in catalytic
FT efficiency for D-allose phosphorylation."
FT /evidence="ECO:0000269|PubMed:17979299"
FT CONFLICT 308..309
FT /note="AP -> EGANKRGNSSRLTQSFHFFMFEPIFSPVNALNQPI (in Ref.
FT 3; BAE78087)"
FT /evidence="ECO:0000305"
FT STRAND 5..13
FT /evidence="ECO:0007829|PDB:3HTV"
FT STRAND 15..24
FT /evidence="ECO:0007829|PDB:3HTV"
FT STRAND 29..36
FT /evidence="ECO:0007829|PDB:3HTV"
FT HELIX 37..41
FT /evidence="ECO:0007829|PDB:3HTV"
FT HELIX 45..60
FT /evidence="ECO:0007829|PDB:3HTV"
FT STRAND 62..73
FT /evidence="ECO:0007829|PDB:3HTV"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:3HTV"
FT HELIX 92..95
FT /evidence="ECO:0007829|PDB:3HTV"
FT HELIX 98..106
FT /evidence="ECO:0007829|PDB:3HTV"
FT STRAND 110..114
FT /evidence="ECO:0007829|PDB:3HTV"
FT HELIX 115..126
FT /evidence="ECO:0007829|PDB:3HTV"
FT STRAND 134..149
FT /evidence="ECO:0007829|PDB:3HTV"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:3HTV"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:3HTV"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:3HTV"
FT HELIX 190..197
FT /evidence="ECO:0007829|PDB:3HTV"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:3HTV"
FT HELIX 209..213
FT /evidence="ECO:0007829|PDB:3HTV"
FT HELIX 217..237
FT /evidence="ECO:0007829|PDB:3HTV"
FT STRAND 240..245
FT /evidence="ECO:0007829|PDB:3HTV"
FT TURN 247..250
FT /evidence="ECO:0007829|PDB:3HTV"
FT HELIX 256..265
FT /evidence="ECO:0007829|PDB:3HTV"
FT TURN 269..275
FT /evidence="ECO:0007829|PDB:3HTV"
FT STRAND 277..280
FT /evidence="ECO:0007829|PDB:3HTV"
FT HELIX 287..300
FT /evidence="ECO:0007829|PDB:3HTV"
SQ SEQUENCE 309 AA; 33821 MW; 7C655FD2E5A8BF2E CRC64;
MQKQHNVVAG VDMGATHIRF CLRTAEGETL HCEKKRTAEV IAPGLVSGIG EMIDEQLRRF
NARCHGLVMG FPALVSKDKR TIISTPNLPL TAADLYDLAD KLENTLNCPV EFSRDVNLQL
SWDVVENRLT QQLVLAAYLG TGMGFAVWMN GAPWTGAHGV AGELGHIPLG DMTQHCACGN
PGCLETNCSG MALRRWYEQQ PRNYPLRDLF VHAENAPFVQ SLLENAARAI ATSINLFDPD
AVILGGGVMD MPAFPRETLV AMTQKYLRRP LPHQVVRFIA ASSSDFNGAQ GAAILAHQRF
LPQFCAKAP
