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Entry
EC 2.2.1.10                 Enzyme                                 

Name
2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase;
ADH synthase;
ADHS;
MJ0400 (gene name)
Class
Transferases;
Transferring aldehyde or ketonic groups;
Transketolases and transaldolases
BRITE hierarchy
Sysname
L-aspartate 4-semialdehyde:1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate methylglyoxaltransferase
Reaction(IUBMB)
L-aspartate 4-semialdehyde + 1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate = 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate + 2,3-dioxopropyl phosphate [RN:R08568]
Reaction(KEGG)
Substrate
L-aspartate 4-semialdehyde [CPD:C00441];
1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate [CPD:C16848]
Product
2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate;
2,3-dioxopropyl phosphate [CPD:C16849]
Comment
The enzyme plays a key role in an alternative pathway of the biosynthesis of 3-dehydroquinate (DHQ), which is involved in the canonical pathway for the biosynthesis of aromatic amino acids. The enzyme can also catalyse the reaction of EC 4.1.2.13, fructose-bisphosphate aldolase.
History
EC 2.2.1.10 created 2012
Pathway
Phenylalanine, tyrosine and tryptophan biosynthesis
Biosynthesis of secondary metabolites
Biosynthesis of antibiotics
Orthology
K16306  
fructose-bisphosphate aldolase / 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase
Genes
BMET: 
SRW: 
MJA: 
MFE: 
MVU: 
MFS: 
MIF: 
MJH: 
MIG: 
MMP: 
MMQ: 
MMX: 
MMZ: 
MMD: 
MMAK: 
MMAO: 
MAE: 
MVN: 
MVO: 
MOK: 
MAC: 
MBA: 
MBY: 
MBW: 
MBAR: 
MMA: 
MMAZ: 
MVC: 
MEK: 
MLS: 
METM: 
MEF: 
MEQ: 
MSJ: 
MSZ: 
MSW: 
MTHE: 
MTHR: 
MHOR: 
MBU: 
MMET: 
MMH: 
MEV: 
MZH: 
MPY: 
MHZ: 
MTP: 
MCJ: 
MHI: 
MHU: 
MLA: 
MEM: 
MBG: 
BN140_2035(fbaA1) BN140_2036(fbaA3)
MEMA: 
MPI: 
MBN: 
MFO: 
MPL: 
MPD: 
MEZ: 
RCI: 
RRC153(aroF)
MTH: 
MMG: 
METC: 
MST: 
MSI: 
MRU: 
MEB: 
MMIL: 
MEYE: 
MEL: 
MEW: 
METH: 
MFC: 
MFI: 
MFV: 
MKA: 
MK1409(fbaB)
AFU: 
AFG: 
APO: 
AVE: 
AST: 
FPL: 
GAC: 
GAH: 
HAL: 
HSL: 
OE_1472F(fba2)
HDL: 
HHB: 
HMA: 
rrnAC1881(deoC2)
HHI: 
HAH_2396(fbaB2)
HHN: 
HAB: 
NPH: 
NP_3160A(fba2)
NMO: 
Nmlp_1197(fba2)
HUT: 
HTI: 
HMU: 
HJE: 
HSU: 
HSF: 
HWA: 
HQ_1156A(fba2)
HWC: 
Hqrw_1193(fba2)
HLA: 
HVO: 
HVO_0790(fba2)
HME: 
HFX_0749(fbaB)
HGI: 
HBO: 
HTU: 
NMG: 
HXA: 
NAT: 
NPE: 
NGE: 
HRU: 
NOU: 
SALI: 
HLR: 
TAR: 
MAX: 
MER: 
MEAR: 
Mpt1_c09850(aroA'1) Mpt1_c10430(aroA'2)
MARC: 
THB: 
TCB: 
THF: 
NMR: 
NIR: 
NID: 
NIN: 
NKR: 
CSY: 
NGA: 
Ngar_c16210(aroGFH)
NVN: 
NVIE_005850(aroGFH)
NEV: 
TAA: 
CSU: 
NBV: 
TAH: 
LOKI: 
Lokiarch_06380(aroA'_1) Lokiarch_41970(aroA'_2)
BARB: 
AOA66_0830(aroA')
HAH: 
 » show all
Taxonomy
Reference
1  [PMID:15182204]
  Authors
White RH.
  Title
L-Aspartate semialdehyde and a 6-deoxy-5-ketohexose 1-phosphate are the precursors to the aromatic amino acids in Methanocaldococcus jannaschii.
  Journal
Biochemistry. 43 (2004) 7618-27.
  Sequence
[mja:MJ_0400]
Reference
2  [PMID:18318840]
  Authors
Samland AK, Wang M, Sprenger GA
  Title
MJ0400 from Methanocaldococcus jannaschii exhibits fructose-1,6-bisphosphate aldolase activity.
  Journal
FEMS. Microbiol. Lett. 281 (2008) 36-41.
  Sequence
[mja:MJ_0400]
Reference
3  [PMID:17713928]
  Authors
Morar M, White RH, Ealick SE.
  Title
Structure of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid synthase, a catalyst in the archaeal pathway for the biosynthesis of aromatic amino acids.
  Journal
Biochemistry. 46 (2007) 10562-71.
  Sequence
[mja:MJ_0400]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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