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Information on EC 2.7.1.214 - C7-cyclitol 7-kinase
for references in articles please use BRENDA:EC2.7.1.214
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EC Tree 2 Transferases
2.7 Transferring phosphorus-containing groups
2.7.1 Phosphotransferases with an alcohol group as acceptor
2.7.1.214 C7-cyclitol 7-kinase
IUBMB Comments
The enzyme, characterized from the bacterium Streptomyces hygroscopicus var. jinggangensis, is involved in the biosynthesis of the antifungal agent validamycin A.
The enzyme appears in viruses and cellular organisms
Reaction Schemes
showSynonyms
1-epi-valienol-7-phosphate 1-kinase, AcbU, valC, vldC, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
valC
vldC
valC
-
-
-
-
vldC
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + validone = ADP + validone 7-phosphate
(2)
-
-
-
ATP + valienone = ADP + valienone 7-phosphate
(1)
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
validamycin biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
ATP:C7-cyclitol 7-phosphotransferase
The enzyme, characterized from the bacterium Streptomyces hygroscopicus var. jinggangensis, is involved in the biosynthesis of the antifungal agent validamycin A.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 1-epi-valienol
ADP + 1-epi-valienol 7-phosphate
Substrates: -
Products: -
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?
ATP + valienol
ADP + valienol 7-phosphate
Substrates: -
Products: -
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?
ATP + validone
ADP + validone 7-phosphate
Substrates: -
Products: -
Products: -
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ATP + validone
ADP + validone 7-phosphate
Substrates: -
Products: -
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ATP + valienone
ADP + valienone 7-phosphate
Substrates: -
Products: -
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ATP + valienone
ADP + valienone 7-phosphate
Substrates: -
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additional information
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Substrates: no substrates: 1-epi-2-epi-5-epi-valiolol, 2-epi-5-epi-valiolol, 2-epi-5-epi-valiolone, 5-epi-valiolol, 1-epi-2-epi-5-epi-valiolol
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additional information
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Substrates: ValC is a C7-cyclitol kinase, which phosphorylates valienone and validone, but not 2-epi-5-epi-valiolone, 5-epi-valiolone, and D-glucose, D-fructose, D-mannose, and D-mannitose, to their 7-phosphate derivatives
Products: -
Products: -
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additional information
?
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Substrates: ValC is a C7-cyclitol kinase, which phosphorylates valienone and validone, but not 2-epi-5-epi-valiolone, 5-epi-valiolone, and D-glucose, D-fructose, D-mannose, and D-mannitose, to their 7-phosphate derivatives
Products: -
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additional information
?
-
Substrates: enzyme shows glucokinase activity
Products: -
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additional information
?
-
Substrates: enzyme shows glucokinase activity
Products: -
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 1-epi-valienol
ADP + 1-epi-valienol 7-phosphate
Substrates: -
Products: -
Products: -
?
ATP + valienol
ADP + valienol 7-phosphate
Substrates: -
Products: -
Products: -
?
ATP + validone
ADP + validone 7-phosphate
Substrates: -
Products: -
Products: -
?
ATP + validone
ADP + validone 7-phosphate
Substrates: -
Products: -
Products: -
?
ATP + valienone
ADP + valienone 7-phosphate
Substrates: -
Products: -
Products: -
?
ATP + valienone
ADP + valienone 7-phosphate
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: ValC is a C7-cyclitol kinase, which phosphorylates valienone and validone, but not 2-epi-5-epi-valiolone, 5-epi-valiolone, and D-glucose, D-fructose, D-mannose, and D-mannitose, to their 7-phosphate derivatives
Products: -
Products: -
?
additional information
?
-
Substrates: ValC is a C7-cyclitol kinase, which phosphorylates valienone and validone, but not 2-epi-5-epi-valiolone, 5-epi-valiolone, and D-glucose, D-fructose, D-mannose, and D-mannitose, to their 7-phosphate derivatives
Products: -
Products: -
?
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
inactivation of valC results in mutants that lack the ability to produce validamycin A
physiological function
the ValABC gene cluster is responsible for validamycin biosynthesis in Streptomyces hygroscopicus subsp. jinggangensis
physiological function
within the validamycin biosynthetic gene cluster, VldBC forms an operon of VldABC with VldA, the gene encoding 2-epi-5-epi-valiolone synthase
physiological function
-
within the validamycin biosynthetic gene cluster, VldBC forms an operon of VldABC with VldA, the gene encoding 2-epi-5-epi-valiolone synthase
-
physiological function
-
the ValABC gene cluster is responsible for validamycin biosynthesis in Streptomyces hygroscopicus subsp. jinggangensis
-
physiological function
-
inactivation of valC results in mutants that lack the ability to produce validamycin A
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). VALC_STRHJ
Streptomyces hygroscopicus subsp. jinggangensis (strain 5008)
351
0
35966
Swiss-Prot
-
VLDC_STRHL
351
0
35935
Swiss-Prot
-
Q27GS3_ACTS5
Actinoplanes sp. (strain ATCC 31044 / CBS 674.73 / SE50/110)
492
0
54195
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 40000, SDS-PAGE of recombinant His-tagged protein, x * 36750, calculated
?
-
x * 40000, SDS-PAGE of recombinant His-tagged protein, x * 36750, calculated
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Seo, M.; Im, E.; Singh, D.; Rajkarnikar, A.; Kwon, H.; Hyun, C.; Suh, J.; Pyun, Y.; Kim, S.
Characterization of D-glucose alpha -1-phosphate uridylyltransferase (VldB) and glucokinase (VldC) involved in validamycin biosynthesis of Streptomyces hygroscopicus var. limoneus KCCM 11405
J. Microbiol. Biotechnol.
16
1311-1315
2006
Streptomyces hygroscopicus subsp. limoneus (Q15JG5), Streptomyces hygroscopicus subsp. limoneus KCCM 11405 (Q15JG5)
-
brenda
Yu, Y.; Bai, L.; Minagawa, K.; Jian, X.; Li, L.; Li, J.; Chen, S.; Cao, E.; Mahmud, T.; Floss, H.G.; Zhou, X.; Deng, Z.
Gene cluster responsible for validamycin biosynthesis in Streptomyces hygroscopicus subsp. jinggangensis 5008
Appl. Environ. Microbiol.
71
5066-5076
2005
Streptomyces hygroscopicus subsp. jinggangensis (Q3T6E2), Streptomyces hygroscopicus subsp. jinggangensis 5008 (Q3T6E2)
brenda
Minagawa, K.; Zhang, Y.; Ito, T.; Bai, L.; Deng, Z.; Mahmud, T.
ValC, a new type of C7-Cyclitol kinase involved in the biosynthesis of the antifungal agent validamycin A
ChemBioChem
8
632-641
2007
Streptomyces hygroscopicus subsp. jinggangensis (Q3T6E2), Streptomyces hygroscopicus subsp. jinggangensis 5008 (Q3T6E2)
brenda
Zhang, C.S.; Podeschwa, M.; Block, O.; Altenbach, H.J.; Piepersberg, W.; Wehmeier, U.F.
Identification of a 1-epi-valienol 7-kinase activity in the producer of acarbose, Actinoplanes sp. SE50/110
FEBS Lett.
540
53-57
2003
Actinoplanes sp. SE50/110 (Q27GS3)
brenda
EXTERNAL LINKS (specific for EC-Number 2.7.1.214)
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Release 2023.1 (January 2023)
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