Glycerol kinase - Escherichia coli (strain K12)

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P0A6F3 (GLPK_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 67. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Glycerol kinase
EC=2.7.1.30

Alternative name(s):
ATP:glycerol 3-phosphotransferase
Glycerokinase
Short name=GK

Gene names

Name:	glpK
Ordered Locus Names:	b3926, JW3897

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	502 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Key enzyme in the regulation of glycerol uptake and metabolism. HAMAP MF_00186
Catalytic activity	ATP + glycerol = ADP + sn-glycerol 3-phosphate. HAMAP MF_00186
Cofactor	Binds 1 zinc ion per glycerol kinase EIIA-Glc dimer. The zinc ion is important for dimerization.
Enzyme regulation	Activity of this regulatory enzyme is affected by several metabolites. The inhibition by fructose 1,6-biphosphate causes alterations in the quaternary structure of the enzyme. Phosphotransferase system phosphocarrier protein (IIIGlc or IIAGlc) inhibits activity of wild-type enzyme but activates the mutant enzyme. HAMAP MF_00186
Pathway	Polyol metabolism; glycerol degradation via glycerol kinase pathway; sn-glycerol 3-phosphate from glycerol: step 1/1. HAMAP MF_00186
Subunit structure	Homotetramer and homodimer (in equilibrium). Heterodimer with EIIA-Glc (crr).
Induction	By L-alpha-glycerol 3-phosphate. HAMAP MF_00186
Miscellaneous	This enzyme is inactivated by modification with sulfhydryl reagents or the adenine nucleotide affinity label, 5'-P-(fluorosulfonyl)-benzoyl adenosine. HAMAP MF_00186
Sequence similarities	Belongs to the FGGY kinase family.

Ontologies

Keywords
Biological process	Glycerol metabolism
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Kinase Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	glycerol-3-phosphate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW glycerol kinase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.7

Chain

2 – 502

501

Glycerol kinase HAMAP MF_00186

PRO_0000059451

Regions

Nucleotide binding

412 – 416

ATP HAMAP MF_00186

Sites

Metal binding

479

Zinc; shared with EIIA-Glc

Binding site

Substrate

Binding site

ATP

Binding site

Substrate

Binding site

136

Substrate

Binding site

246

Substrate

Binding site

268

ATP

Binding site

311

ATP; via carbonyl oxygen

Experimental info

Mutagenesis

305

G → S in glpK22; abolishes glucose control of glycerol utilization.

Secondary structure

502

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0A6F3 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 854B61EA4648AB80
Show »

FASTA

502

56,231

        10         20         30         40         50         60 
MTEKKYIVAL DQGTTSSRAV VMDHDANIIS VSQREFEQIY PKPGWVEHDP MEIWATQSST 

        70         80         90        100        110        120 
LVEVLAKADI SSDQIAAIGI TNQRETTIVW EKETGKPIYN AIVWQCRRTA EICEHLKRDG 

       130        140        150        160        170        180 
LEDYIRSNTG LVIDPYFSGT KVKWILDHVE GSRERARRGE LLFGTVDTWL IWKMTQGRVH 

       190        200        210        220        230        240 
VTDYTNASRT MLFNIHTLDW DDKMLEVLDI PREMLPEVRR SSEVYGQTNI GGKGGTRIPI 

       250        260        270        280        290        300 
SGIAGDQQAA LFGQLCVKEG MAKNTYGTGC FMLMNTGEKA VKSENGLLTT IACGPTGEVN 

       310        320        330        340        350        360 
YALEGAVFMA GASIQWLRDE MKLINDAYDS EYFATKVQNT NGVYVVPAFT GLGAPYWDPY 

       370        380        390        400        410        420 
ARGAIFGLTR GVNANHIIRA TLESIAYQTR DVLEAMQADS GIRLHALRVD GGAVANNFLM 

       430        440        450        460        470        480 
QFQSDILGTR VERPEVREVT ALGAAYLAGL AVGFWQNLDE LQEKAVIERE FRPGIETTER 

       490        500 
NYRYAGWKKA VKRAMAWEEH DE

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Escherichia coli glycerol kinase. Cloning and sequencing of the glpK gene and the primary structure of the enzyme." Pettigrew D.W., Ma D.-P., Conrad C.A., Johnson J.R. J. Biol. Chem. 263:135-139(1988) [PubMed: 2826434] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Structure and regulation of the glpFK operon encoding glycerol diffusion facilitator and glycerol kinase of Escherichia coli K-12." Weissenborn D.L., Wittekindt N., Larson T.J. J. Biol. Chem. 267:6122-6131(1992) [PubMed: 1372899] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes." Plunkett G. III, Burland V., Daniels D.L., Blattner F.R. Nucleic Acids Res. 21:3391-3398(1993) [PubMed: 8346018] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"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.
[5]	"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.
[6]	"Nucleotide sequence of the region encompassing the glpKF operon and its upstream region containing a bent DNA sequence of Escherichia coli." Muramatsu S., Mizuno T. Nucleic Acids Res. 17:4378-4378(1989) [PubMed: 2544860] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31.
[7]	"FIS is a regulator of metabolism in Escherichia coli." Gonzalez-Gil G., Bringmann P., Kahmann R. Mol. Microbiol. 22:21-29(1996) [PubMed: 8899705] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-14. Strain: K12.
[8]	"A single amino acid change in Escherichia coli glycerol kinase abolishes glucose control of glycerol utilization in vivo." Pettigrew D.W., Liu W.Z., Holmes C., Meadow N.D., Roseman S. J. Bacteriol. 178:2846-2852(1996) [PubMed: 8631672] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTANT GLPK22.
[9]	"Structure of the regulatory complex of Escherichia coli IIIGlc with glycerol kinase." Hurley J.H., Faber H.R., Worthylake D., Meadow N.D., Roseman S., Pettigrew D.W., Remington S.J. Science 259:673-677(1993) [PubMed: 8430315] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH EIIA-GLC.
[10]	"Cation-promoted association of a regulatory and target protein is controlled by protein phosphorylation." Feese M., Pettigrew D.W., Meadow N.D., Roseman S., Remington S.J. Proc. Natl. Acad. Sci. U.S.A. 91:3544-3548(1994) [PubMed: 8170944] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS).
[11]	"Crystal structure of a complex of Escherichia coli glycerol kinase and an allosteric effector fructose 1,6-bisphosphate." Ormoe M., Bystrom C.E., Remington S.J. Biochemistry 37:16565-16572(1998) [PubMed: 9843423] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
[12]	"Glycerol kinase from Escherichia coli and an Ala65-->Thr mutant: the crystal structures reveal conformational changes with implications for allosteric regulation." Feese M.D., Faber H.R., Bystrom C.E., Pettigrew D.W., Remington S.J. Structure 6:1407-1418(1998) [PubMed: 9817843] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.37 ANGSTROMS).
[13]	"Crystal structures of Escherichia coli glycerol kinase variant S58-->W in complex with nonhydrolyzable ATP analogues reveal a putative active conformation of the enzyme as a result of domain motion." Bystrom C.E., Pettigrew D.W., Branchaud B.P., O'Brien P., Remington S.J. Biochemistry 38:3508-3518(1999) [PubMed: 10090737] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF MUTANT TRP-59.
+	Additional computationally mapped references.

Web resources

Worthington enzyme manual

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M18393 Genomic DNA. Translation: AAA23913.1.
M55990 Genomic DNA. Translation: AAA23887.1.
L19201 Genomic DNA. Translation: AAB03058.1.
U00096 Genomic DNA. Translation: AAC76908.1.
AP009048 Genomic DNA. Translation: BAE77384.1.
X15054 Genomic DNA. Translation: CAA33154.1.
U41468 Genomic DNA. Translation: AAB60196.1.

PIR

KIECGL. A27339.

RefSeq

NP_418361.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BO5	X-ray	3.20	O/Z	2-502	[»]
1BOT	X-ray	3.05	O/Z	2-502	[»]
1BU6	X-ray	2.37	O/X/Y/Z	2-502	[»]
1BWF	X-ray	3.00	O/Y	2-502	[»]
1GLA	X-ray	2.60	G	2-502	[»]
1GLB	X-ray	2.60	G	2-502	[»]
1GLC	X-ray	2.65	G	2-502	[»]
1GLD	X-ray	2.93	G	2-502	[»]
1GLE	X-ray	2.94	G	2-502	[»]
1GLF	X-ray	2.62	O/X/Y/Z	2-502	[»]
1GLJ	X-ray	3.00	O/Y	2-502	[»]
1GLL	X-ray	3.00	O/Y	2-502	[»]
3EZW	X-ray	2.00	A/B/C/D/E/F/G/H	2-501	[»]

ProteinModelPortal

P0A6F3.

SMR

P0A6F3. Positions 3-501.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-36011N.

IntAct

P0A6F3. 17 interactions.

2D gel databases

SWISS-2DPAGE

P0A6F3.

ECO2DBASE

E048.7. 6TH EDITION.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000002503; EBESCP00000002503; EBESCG00000002042.
EBESCT00000016546; EBESCP00000015837; EBESCG00000015606.

GeneID

948423.

GenomeReviews

Gene locus JW3897 in contig AP009048_GR.
Gene locus b3926 in contig U00096_GR.

KEGG

ecj:JW3897.
eco:b3926.

PATRIC

32123365. VBIEscCol129921_4043.

Organism-specific databases

EchoBASE

EB0393.

EcoGene

EG10398. glpK.

Phylogenomic databases

eggNOG

COG0554.

GeneTree

EBGT00050000009228.

HOGENOM

HBG511469.

OMA

ALYGQLC.

PhylomeDB

P0A6F3.

ProtClustDB

PRK00047.

Enzyme and pathway databases

BioCyc

EcoCyc:GLYCEROL-KIN-MONOMER.
MetaCyc:GLYCEROL-KIN-MONOMER.

Gene expression databases

Genevestigator

P0A6F3.

Family and domain databases

HAMAP

MF_00186. Glycerol_kin.
[Tree]

InterPro

IPR000577. Carb_kinase_FGGY.
IPR018485. Carb_kinase_FGGY_C.
IPR018483. Carb_kinase_FGGY_CS.
IPR018484. Carb_kinase_FGGY_N.
IPR005999. Glycerol_kin.
[Graphical view]

K00864.

PANTHER

PTHR10196. FGGY_kin. 1 hit.
PTHR10196:SF9. Glycerol_kin. 1 hit.

Pfam

PF02782. FGGY_C. 1 hit.
PF00370. FGGY_N. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01311. Glycerol_kin. 1 hit.

PROSITE

PS00933. FGGY_KINASES_1. 1 hit.
PS00445. FGGY_KINASES_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

GLPK_ECOLI

Accession

Primary (citable) accession number: P0A6F3
Secondary accession number(s): P08859, Q2M8M2, Q59381

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2005
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 67 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Secondary structure

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents