KEGG   ORTHOLOGY: K19969Help
Entry
K19969                      KO                                     

Name
acbC, salQ, valA, cetA
Definition
2-epi-5-epi-valiolone synthase [EC:4.2.3.152]
Pathway
ko00525  Acarbose and validamycin biosynthesis
ko01100  Metabolic pathways
ko01130  Biosynthesis of antibiotics
Module
M00814  Acarbose biosynthesis, sedoheptulopyranose-7P => acarbose
M00815  Validamycin A biosynthesis, sedoheptulopyranose-7P => validamycin A
Brite
KEGG Orthology (KO) [BR:ko00001]
 09100 Metabolism
  09110 Biosynthesis of other secondary metabolites
   00525 Acarbose and validamycin biosynthesis
    K19969  acbC, salQ, valA, cetA; 2-epi-5-epi-valiolone synthase
Enzymes [BR:ko01000]
 4. Lyases
  4.2  Carbon-oxygen lyases
   4.2.3  Acting on phosphates
    4.2.3.152  2-epi-5-epi-valiolone synthase
     K19969  acbC, salQ, valA, cetA; 2-epi-5-epi-valiolone synthase
BRITE hierarchy
Other DBs
RN: R10937
Genes
SERA: Ser39006_003950
SERQ: CWC46_03950
RHD: R2APBS1_3641
PFC: PflA506_4591
CJA: CJA_3250
GPB: HDN1F_13870(acbC)
CVC: BKX93_19945
BTZ: BTL_4163
BOK: DM82_5622
COF: FOZ74_00740
SUR: STAUR_1386(gacC)
CBB: CLD_3207
MMI: MMAR_0578(aroB_1)
MMAE: MMARE11_05350(aroB_1)
MHAD: B586_06435
RER: RER_54360
REY: O5Y_25890
RHB: NY08_95
RHS: A3Q41_04747(aroB_3)
SHY: SHJG_0276
SALS: SLNWT_0595
SGU: SGLAU_01035(gacC)
STRM: M444_32560
SRW: TUE45_05037(aroB_3)
SLE: sle_45870(sle_45870)
SFK: KY5_0702
FAL: FRAAL4639
AOI: AORI_5447(aroB)
SESP: BN6_52640
ACTI: UA75_21530
ACAD: UA74_21050
ASE: ACPL_3680(acbC) ACPL_6250
AG: ABL74381(cetA)
 » show all
TaxonomyKoalaUniProt
Reference
  Authors
Stratmann A, Mahmud T, Lee S, Distler J, Floss HG, Piepersberg W
  Title
The AcbC protein from Actinoplanes species is a C7-cyclitol synthase related to 3-dehydroquinate synthases and is involved in the biosynthesis of the alpha-glucosidase inhibitor acarbose.
  Journal
J Biol Chem 274:10889-96 (1999)
DOI:10.1074/jbc.274.16.10889
  Sequence
[ase:ACPL_3680]
Reference
  Authors
Choi WS, Wu X, Choeng YH, Mahmud T, Jeong BC, Lee SH, Chang YK, Kim CJ, Hong SK
  Title
Genetic organization of the putative salbostatin biosynthetic gene cluster including the 2-epi-5-epi-valiolone synthase gene in Streptomyces albus ATCC 21838.
  Journal
Appl Microbiol Biotechnol 80:637-45 (2008)
DOI:10.1007/s00253-008-1591-2
  Sequence
[sals:SLNWT_0595]
Reference
  Authors
Kean KM, Codding SJ, Asamizu S, Mahmud T, Karplus PA
  Title
Structure of a sedoheptulose 7-phosphate cyclase: ValA from Streptomyces hygroscopicus.
  Journal
Biochemistry 53:4250-60 (2014)
DOI:10.1021/bi5003508
  Sequence
[shy:SHJG_0276]
Reference
  Authors
Wu X, Flatt PM, Xu H, Mahmud T
  Title
Biosynthetic gene cluster of cetoniacytone A, an unusual aminocyclitol from the endosymbiotic Bacterium Actinomyces sp. Lu 9419.
  Journal
Chembiochem 10:304-14 (2009)
DOI:10.1002/cbic.200800527
  Sequence

KEGG   ENZYME: 4.2.3.152Help
Entry
EC 4.2.3.152                Enzyme                                 

Name
2-epi-5-epi-valiolone synthase;
AcbC;
ValA;
CetA;
SalQ;
C7-cyclitol synthase
Class
Lyases;
Carbon-oxygen lyases;
Acting on phosphates
BRITE hierarchy
Sysname
alpha-D-sedoheptulopyranose-7-phosphate phosphate-lyase (cyclizing; 2-epi-5-epi-valiolone-forming)
Reaction(IUBMB)
alpha-D-sedoheptulopyranose 7-phosphate = 2-epi-5-epi-valiolone + phosphate [RN:R10937]
Reaction(KEGG)
Substrate
alpha-D-sedoheptulopyranose 7-phosphate [CPD:C20956]
Product
2-epi-5-epi-valiolone [CPD:C17691];
phosphate [CPD:C00009]
Comment
The enzyme is highly specific for alpha-D-sedoheptulopyranose 7-phosphate. It requires a divalent metal ion (Zn2+ or Co2+) and an NAD+ cofactor, which is transiently reduced during the reaction. The enzyme is involved in the biosynthesis of C7N-aminocyclitol natural products, such as the valienamine moiety of the antidiabetic drug acarbose and the crop protectant validamycin A. cf. EC 4.2.3.155, 2-epi-valiolone synthase and EC 4.2.3.154, demethyl-4-deoxygadusol synthase.
History
EC 4.2.3.152 created 2015, modified 2016
Pathway
ec00525  Acarbose and validamycin biosynthesis
ec01100  Metabolic pathways
ec01130  Biosynthesis of antibiotics
Orthology
K19969  2-epi-5-epi-valiolone synthase
Genes
SERA: Ser39006_003950
SERQ: CWC46_03950
RHD: R2APBS1_3641
PFC: PflA506_4591
CJA: CJA_3250
GPB: HDN1F_13870(acbC)
CVC: BKX93_19945
BTZ: BTL_4163
BOK: DM82_5622
COF: FOZ74_00740
SUR: STAUR_1386(gacC)
CBB: CLD_3207
MMI: MMAR_0578(aroB_1)
MMAE: MMARE11_05350(aroB_1)
MHAD: B586_06435
RER: RER_54360
REY: O5Y_25890
RHB: NY08_95
RHS: A3Q41_04747(aroB_3)
SHY: SHJG_0276
SALS: SLNWT_0595
SGU: SGLAU_01035(gacC)
STRM: M444_32560
SRW: TUE45_05037(aroB_3)
SLE: sle_45870(sle_45870)
SFK: KY5_0702
FAL: FRAAL4639
AOI: AORI_5447(aroB)
SESP: BN6_52640
ACTI: UA75_21530
ACAD: UA74_21050
ASE: ACPL_3680(acbC) ACPL_6250
 » show all
Taxonomy
Reference
1  [PMID:10196166]
  Authors
Stratmann A, Mahmud T, Lee S, Distler J, Floss HG, Piepersberg W
  Title
The AcbC protein from Actinoplanes species is a C7-cyclitol synthase related to 3-dehydroquinate synthases and is involved in the biosynthesis of the alpha-glucosidase inhibitor acarbose.
  Journal
J Biol Chem 274:10889-96 (1999)
DOI:10.1074/jbc.274.16.10889
  Sequence
[ase:ACPL_3680]
Reference
2  [PMID:16151088]
  Authors
Yu Y, Bai L, Minagawa K, Jian X, Li L, Li J, Chen S, Cao E, Mahmud T, Floss HG, Zhou X, Deng Z
  Title
Gene cluster responsible for validamycin biosynthesis in Streptomyces hygroscopicus subsp. jinggangensis 5008.
  Journal
Appl Environ Microbiol 71:5066-76 (2005)
DOI:10.1128/AEM.71.9.5066-5076.2005
  Sequence
[shy:SHJG_0276]
Reference
3  [PMID:17195255]
  Authors
Wu X, Flatt PM, Schlorke O, Zeeck A, Dairi T, Mahmud T
  Title
A comparative analysis of the sugar phosphate cyclase superfamily involved in primary and secondary metabolism.
  Journal
Chembiochem 8:239-48 (2007)
DOI:10.1002/cbic.200600446
  Sequence
Reference
4  [PMID:18648803]
  Authors
Choi WS, Wu X, Choeng YH, Mahmud T, Jeong BC, Lee SH, Chang YK, Kim CJ, Hong SK
  Title
Genetic organization of the putative salbostatin biosynthetic gene cluster including the 2-epi-5-epi-valiolone synthase gene in Streptomyces albus ATCC 21838.
  Journal
Appl Microbiol Biotechnol 80:637-45 (2008)
DOI:10.1007/s00253-008-1591-2
  Sequence
[sals:SLNWT_0595]
Reference
5  [PMID:24832673]
  Authors
Kean KM, Codding SJ, Asamizu S, Mahmud T, Karplus PA
  Title
Structure of a sedoheptulose 7-phosphate cyclase: ValA from Streptomyces hygroscopicus.
  Journal
Biochemistry 53:4250-60 (2014)
DOI:10.1021/bi5003508
  Sequence
[shy:SHJG_0276]
Other DBs
ExplorEnz - The Enzyme Database: 4.2.3.152
IUBMB Enzyme Nomenclature: 4.2.3.152
ExPASy - ENZYME nomenclature database: 4.2.3.152
BRENDA, the Enzyme Database: 4.2.3.152

KEGG   REACTION: R10937Help
Entry
R10937                      Reaction                               

Name
alpha-D-sedoheptulopyranose-7-phosphate phosphate-lyase (cyclizing, 2-epi-5-epi-valiolone-forming)
Definition
alpha-D-Sedoheptulopyranose 7-phosphate <=> 2-epi-5-epi-Valiolone + Orthophosphate
Equation
Reaction class
RC03308  C17691_C20956
Enzyme
Pathway
rn00525  Acarbose and validamycin biosynthesis
rn01100  Metabolic pathways
rn01130  Biosynthesis of antibiotics
Module
M00814  Acarbose biosynthesis, sedoheptulopyranose-7P => acarbose
M00815  Validamycin A biosynthesis, sedoheptulopyranose-7P => validamycin A
Orthology
K19969  2-epi-5-epi-valiolone synthase [EC:4.2.3.152]
Other DBs
RHEA: 44187

DBGET integrated database retrieval system