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Information on EC 2.7.1.33 - pantothenate kinase and Organism(s) Pseudomonas aeruginosa and UniProt Accession Q9HWC1

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This record set is specific for:
Pseudomonas aeruginosa
UNIPROT: Q9HWC1 not found.
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The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The enzyme appears in selected viruses and cellular organisms
Synonyms
pank2, pantothenate kinase, pantothenate kinase 2, pank1, pank3, pank4, pank-iii, type ii pantothenate kinase, pfpank1, pantothenate kinase-2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
type III pantothenate kinase
-
D-pantothenate kinase
-
-
-
-
hPanK
-
-
-
-
hPanK1
-
-
-
-
hPANK2
-
-
-
-
hPanK3
-
-
-
-
hPanK4
-
-
-
-
kinase, pantothenate (phosphorylating)
-
-
-
-
mPank
-
-
-
-
mPank1
-
-
-
-
mPanK3
-
-
-
-
PAK
-
-
-
-
pantothenic acid kinase
-
-
-
-
rPanK4
-
-
-
-
Rts protein
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
ATP:(R)-pantothenate 4'-phosphotransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9026-48-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NH4+
induces a 5fold higher activation than either K+ or Rb+
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
x-ray crystallography
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method using 28% (w/v) PEG 2000 mM and 0.1M Bis-Tris (pH 6.5), at 18°C
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D101A
reduced enzymatic activity
D121A
reduced enzymatic activity
H156A
slightly increased enzymatic activity
K13A
reduced enzymatic activity
N9G
strongly reduced enzymatic activity
T157A
reduced enzymatic activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hong, B.S.; Yun, M.K.; Zhang, Y.M.; Chohnan, S.; Rock, C.O.; White, S.W.; Jackowski, S.; Park, H.W.; Leonardi, R.
Prokaryotic type II and type III pantothenate kinases: The same monomer fold creates dimers with distinct catalytic properties
Structure
14
1251-1261
2006
Staphylococcus aureus (Q6G7I0), Pseudomonas aeruginosa (Q9HWC1)
Manually annotated by BRENDA team