Reviewed, UniProtKB/Swiss-Prot P32718 (ALSK_ECOLI)

Names and origin

Protein names

Recommended name:
    D-allose kinase
      Short name=Allokinase
    EC=2.7.1.55

Gene names

Name:	alsK
Synonyms:	yjcT
Ordered Locus Names:	b4084, JW5724

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	309 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the phosphorylation of D-allose to D-allose 6-P. Has also low level glucokinase activity in vitro. Ref.4 Ref.5
Catalytic activity	ATP + D-allose = ADP + D-allose 6-phosphate.
Pathway	Carbohydrate degradation; D-allose degradation.
Sequence similarities	Belongs to the ROK (nagC/xylR) family.
biophysicochemical properties	Kinetic parameters: Catalytic efficiency with D-allose as substrate is 735-fold higher than that with D-glucose. KM=0.19 mM for D-allose (at 25 degrees Celsius and pH 7.6) Ref.5 KM=0.27 mM for ATP (at 25 degrees Celsius and pH 7.6) KM=29 mM for D-glucose (at 25 degrees Celsius and pH 7.6) KM=210 mM for D-altrose (at 25 degrees Celsius and pH 7.6) KM=380 mM for 2'-deoxy-D-glucose (at 25 degrees Celsius and pH 7.6) KM=390 mM for D-mannose (at 25 degrees Celsius and pH 7.6)

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW allose kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 309	309	D-allose kinase		PRO_0000095688
Regions
	Nucleotide binding	10 – 17	8	ATP Potential
	Nucleotide binding	142 – 149	8	ATP Potential
Experimental info
	Mutagenesis	73	1	A → G: 60-fold increase in catalytic efficiency for glucose phosphorylation. 45-fold increase in D-glucose affinity. No change in catalytic efficiency for D-allose phosphorylation. Ref.5
	Mutagenesis	145	1	F → L: 10-fold increase in catalytic efficiency for glucose phosphorylation. Slight increase in catalytic efficiency for D-allose phosphorylation. Ref.5
	Sequence conflict	308 – 309	2	AP → EGANKRGNSSRLTQSFHFFM FEPIFSPVNALNQPI in BAE78087. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P32718-1 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: 7C655FD2E5A8BF2E	FASTA	309	33,821
	10 20 30 40 50 60 MQKQHNVVAG VDMGATHIRF CLRTAEGETL HCEKKRTAEV IAPGLVSGIG EMIDEQLRRF 70 80 90 100 110 120 NARCHGLVMG FPALVSKDKR TIISTPNLPL TAADLYDLAD KLENTLNCPV EFSRDVNLQL 130 140 150 160 170 180 SWDVVENRLT QQLVLAAYLG TGMGFAVWMN GAPWTGAHGV AGELGHIPLG DMTQHCACGN 190 200 210 220 230 240 PGCLETNCSG MALRRWYEQQ PRNYPLRDLF VHAENAPFVQ SLLENAARAI ATSINLFDPD 250 260 270 280 290 300 AVILGGGVMD MPAFPRETLV AMTQKYLRRP LPHQVVRFIA ASSSDFNGAQ GAAILAHQRF LPQFCAKAP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes." Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L. Nucleic Acids Res. 21:5408-5417(1993) [PubMed: 8265357] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[2]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"The D-allose operon of Escherichia coli K-12." Kim C., Song S., Park C. J. Bacteriol. 179:7631-7637(1997) [PubMed: 9401019] [Abstract] Cited for: FUNCTION. Strain: K12.
[5]	"Divergent evolution of function in the ROK sugar kinase superfamily: role of enzyme loops in substrate specificity." Larion M., Moore L.B., Thompson S.M., Miller B.G. Biochemistry 46:13564-13572(2007) [PubMed: 17979299] [Abstract] Cited for: FUNCTION, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS, MUTAGENESIS OF ALA-73 AND PHE-145.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U00006 Genomic DNA. Translation: AAC43178.1. U00096 Genomic DNA. Translation: AAC77045.1. AP009048 Genomic DNA. Translation: BAE78087.1.
PIR	C65217.
RefSeq	AP_004586.1. NP_418508.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:9097N.
Genome annotation databases
GeneID	948596.
GenomeReviews	Gene locus JW5724 in contig AP009048_GR. Gene locus b4084 in contig U00096_GR.
KEGG	ecj:JW5724. eco:b4084.
Organism-specific databases
EchoBASE	EB1899.
EcoGene	EG11956. alsK.
CMR	Search...
Phylogenomic databases
HOGENOM	P32718.
OMA	P32718. QSCAKAP.
Enzyme and pathway databases
BioCyc	EcoCyc:EG11956-MON. MetaCyc:EG11956-MON.
Family and domain databases
InterPro	IPR000600. ROK. [Graphical view]
Pfam	PF00480. ROK. 1 hit. [Graphical view]
PROSITE	PS01125. ROK. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ALSK_ECOLI

Accession

Primary (citable) accession number: P32718
Secondary accession number(s): Q2M6L9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	June 16, 2009
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)