Thermoresistant gluconokinase - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P46859 (GNTK_ECOLI)

Last modified June 16, 2009. Version 71. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Thermoresistant gluconokinase
    EC=2.7.1.12
Alternative name(s):
    Gluconate kinase 2

Gene names

Name:	gntK
Ordered Locus Names:	b3437, JW3400

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	175 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Catalytic activity	ATP + D-gluconate = ADP + 6-phospho-D-gluconate.
Pathway	Carbohydrate acid metabolism; D-gluconic acid degradation.
Sequence similarities	Belongs to the gluconokinase gntK/gntV family.

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Ontologies

Keywords
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW gluconokinase activity Inferred from electronic annotation. Source: EC shikimate kinase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.4

Chain

2 – 175

174

Thermoresistant gluconokinase

PRO_0000087537

Regions

Nucleotide binding

15 – 22

ATP Potential

Secondary structure

175

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P46859-1 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 5859A38413E8A586
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FASTA

175

19,543

        10         20         30         40         50         60 
MSTTNHDHHI YVLMGVSGSG KSAVASEVAH QLHAAFLDGD FLHPRRNIEK MASGEPLNDD 

        70         80         90        100        110        120 
DRKPWLQALN DAAFAMQRTN KVSLIVCSAL KKHYRDLLRE GNPNLSFIYL KGDFDVIESR 

       130        140        150        160        170 
LKARKGHFFK TQMLVTQFET LQEPGADETD VLVVDIDQPL EGVVASTIEV IKKGK

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Gene organization and transcriptional regulation of the gntRKU operon involved in gluconate uptake and catabolism of Escherichia coli." Izu H., Adachi O., Yamada M. J. Mol. Biol. 267:778-793(1997) [PubMed: 9135111] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[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]	"Cloning and molecular genetic characterization of the Escherichia coli gntR, gntK, and gntU genes of GntI, the main system for gluconate metabolism." Tong S., Porco A., Isturiz T., Conway T. J. Bacteriol. 178:3260-3269(1996) [PubMed: 8655507] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-20, CHARACTERIZATION.
[5]	"Crystallization and preliminary X-ray crystallographic studies of recombinant thermoresistant gluconate kinase GntK from Escherichia coli." Kraft L., Sprenger G.A., Lindqvist Y. Acta Crystallogr. D 57:1159-1161(2001) [PubMed: 11468405] [Abstract] Cited for: CRYSTALLIZATION.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

D84362 Genomic DNA. Translation: BAA12325.1.
U18997 Genomic DNA. Translation: AAA58235.1. Frameshift.
U00096 Genomic DNA. Translation: AAC76462.1. Different initiation.
AP009048 Genomic DNA. Translation: BAE77856.1.

RefSeq

AP_004355.1.
NP_417894.2.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KNQ	X-ray	2.00	A/B	1-175	[»]
1KO1	X-ray	2.09	A/B	1-175	[»]
1KO4	X-ray	2.50	A/B	1-175	[»]
1KO5	X-ray	2.28	A/B	1-175	[»]
1KO8	X-ray	2.40	A/B	1-175	[»]
1KOF	X-ray	2.80	A/B	1-175	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:9820N.

Genome annotation databases

GeneID

947937.

GenomeReviews

Gene locus JW3400 in contig AP009048_GR.
Gene locus b3437 in contig U00096_GR.

KEGG

ecj:JW3400.
eco:b3437.

Organism-specific databases

EchoBASE

EB2513.

EcoGene

EG12629. gntK.

CMR

Search...

Phylogenomic databases

HOGENOM

P46859.

OMA

P46859. GLRSAHR.

Enzyme and pathway databases

BioCyc

EcoCyc:GLUCONOKINII-MON.
MetaCyc:GLUCONOKINII-MON.

Family and domain databases

InterPro

IPR000623. Shik_kinase.
IPR006001. Therm_gnt_kin.
[Graphical view]

Pfam

PF01202. SKI. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01313. therm_gnt_kin. 1 hit.

ProtoNet

Search...

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Entry information

Entry name

GNTK_ECOLI

Accession

Primary (citable) accession number: P46859
Secondary accession number(s): P78116, Q2M7A0, Q59404

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 71 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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

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