P32718 (ALSK_ECOLI) Reviewed, UniProtKB/Swiss-Prot

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)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	309 AA.
Sequence status	Complete.
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	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	D-allose catabolic process Inferred from direct assay. Source: EcoCyc
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW allose kinase activity Inferred from direct assay. Source: EcoCyc glucokinase activity Inferred from direct assay. Source: EcoCyc
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

Secondary structure

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309

Helix Strand Turn

Details...

Beta strand

5 – 8

4

Beta strand

17 – 24

8

Beta strand

29 – 36

8

Helix

37 – 41

5

Helix

52 – 60

9

Beta strand

62 – 64

3

Beta strand

87 – 89

3

Helix

92 – 95

4

Helix

98 – 106

9

Helix

115 – 126

12

Beta strand

134 – 136

3

Beta strand

146 – 148

3

Helix

192 – 197

6

Helix

206 – 208

3

Helix

209 – 213

5

Helix

217 – 237

21

Beta strand

240 – 244

5

Helix

256 – 265

10

Turn

269 – 275

7

Beta strand

277 – 280

4

Helix

293 – 300

8

Sequences

	Sequence		Length	Mass (Da)
	P32718 [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

EMBL
GenBank
DDBJ

U00006 Genomic DNA. Translation: AAC43178.1.
U00096 Genomic DNA. Translation: AAC77045.1.
AP009048 Genomic DNA. Translation: BAE78087.1.

PIR

C65217.

RefSeq

NP_418508.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3HTV	X-ray	1.95	A	1-309	[»]

ProteinModelPortal

P32718.

SMR

P32718. Positions 3-302.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-9097N.

IntAct

P32718. 1 interaction.

Proteomic databases

PRIDE

P32718.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000000103; EBESCP00000000103; EBESCG00000000080.
EBESCT00000017303; EBESCP00000016594; EBESCG00000016360.

GeneID

948596.

GenomeReviews

Gene locus JW5724 in contig AP009048_GR.
Gene locus b4084 in contig U00096_GR.

KEGG

ecj:JW5724.
eco:b4084.

PATRIC

32123723. VBIEscCol129921_4210.

Organism-specific databases

EchoBASE

EB1899.

EcoGene

EG11956. alsK.

Phylogenomic databases

eggNOG

COG1940.

GeneTree

EBGT00050000009665.

HOGENOM

HBG416849.

OMA

CACGNSG.

PhylomeDB

P32718.

ProtClustDB

PRK09698.

Enzyme and pathway databases

BioCyc

EcoCyc:EG11956-MONOMER.
MetaCyc:EG11956-MONOMER.

Gene expression databases

Genevestigator

P32718.

Family and domain databases

InterPro

IPR000600. ROK.
[Graphical view]

KO

K00881.

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:	January 25, 2012
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program