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Information on EC 2.7.2.7 - butyrate kinase and Organism(s) Thermotoga maritima and UniProt Accession Q9X278

for references in articles please use BRENDA:EC2.7.2.7
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EC Tree
IUBMB Comments
The enzyme from Clostridium sp. also acts, more slowly, on pentanoate and propanoate, and on some branched-chain fatty acids (cf. EC 2.7.1.14 sedoheptulokinase).
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This record set is specific for:
Thermotoga maritima
UNIPROT: Q9X278
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Word Map
The taxonomic range for the selected organisms is: Thermotoga maritima
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
butyrate kinase, butyrate kinase 2, butyrate kinase i, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
butyrate kinase 2
-
BK
-
-
-
-
Buk
-
-
-
-
butyrokinase
-
-
-
-
kinase (phosphorylating), butyrate
-
-
-
-
kinase, butyrate (phosphorylating)
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
ATP:butanoate 1-phosphotransferase
The enzyme from Clostridium sp. also acts, more slowly, on pentanoate and propanoate, and on some branched-chain fatty acids (cf. EC 2.7.1.14 sedoheptulokinase).
CAS REGISTRY NUMBER
COMMENTARY hide
37278-14-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + butanoate
ADP + butanoyl phosphate
show the reaction diagram
ATP + isobutanoate
ADP + isobutanoyl phosphate
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + butanoate
ADP + butanoyl phosphate
show the reaction diagram
ATP + isobutanoate
ADP + isobutanoyl phosphate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
octamer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Buk2 complexed with (beta,gamma-methylene) adenosine 5'-triphosphate, sitting drop vapor diffusion method, using 1.7-3.0 M sodium formate, 1 M acetic acid (pH 4.5)
sitting drop vapor diffusion method, using 77 mM phosphate-citrate and 55% (w/v) PEG 200
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitiation, heparin column chromatography, and Sephadex G25 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli B834 cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Diao, J.; Hasson, M.S.
Crystal structure of butyrate kinase 2 from Thermotoga maritima, a member of the ASKHA superfamily of phosphotransferases
J. Bacteriol.
191
2521-2529
2009
Thermotoga maritima (Q9X278), Thermotoga maritima
Manually annotated by BRENDA team
Diao, J.; Ma, Y.D.; Hasson, M.S.
Open and closed conformations reveal induced fit movements in butyrate kinase 2 activation
Proteins
80
1712
2009
Thermotoga maritima (Q9X278), Thermotoga maritima
Manually annotated by BRENDA team