KEGG   ENZYME: 4.1.2.43Help
Entry
EC 4.1.2.43                 Enzyme                                 

Name
3-hexulose-6-phosphate synthase;
D-arabino-3-hexulose 6-phosphate formaldehyde-lyase;
3-hexulosephosphate synthase;
3-hexulose phosphate synthase;
HPS
Class
Lyases;
Carbon-carbon lyases;
Aldehyde-lyases
BRITE hierarchy
Sysname
D-arabino-hex-3-ulose-6-phosphate formaldehyde-lyase (D-ribulose-5-phosphate-forming)
Reaction(IUBMB)
D-arabino-hex-3-ulose 6-phosphate = D-ribulose 5-phosphate + formaldehyde [RN:R05338]
Reaction(KEGG)
Substrate
D-arabino-hex-3-ulose 6-phosphate [CPD:C06019]
Product
D-ribulose 5-phosphate [CPD:C00199];
formaldehyde [CPD:C00067]
Comment
Requires Mg2+ or Mn2+ for maximal activity [1]. The enzyme is specific for D-ribulose 5-phosphate as substrate as ribose 5-phosphate, xylulose 5-phosphate, allulose 6-phosphate and fructose 6-phosphate cannot act as substrate. In addition to formaldehyde, the enzyme can also use glycolaldehyde and methylglyoxal [7]. This enzyme, along with EC 5.3.1.27, 6-phospho-3-hexuloisomerase, plays a key role in the ribulose-monophosphate cycle of formaldehyde fixation, which is present in many microorganisms that are capable of utilizing C1-compounds [1]. The hyperthermophilic and anaerobic archaeon Pyrococcus horikoshii OT3 constitutively produces a bifunctional enzyme that sequentially catalyses the reactions of this enzyme and EC 5.3.1.27, 6-phospho-3-hexuloisomerase [6]. This enzyme is a member of the orotidine 5'-monophosphate decarboxylase (OMPDC) suprafamily [5].
History
EC 4.1.2.43 created 2008
Pathway
Pentose phosphate pathway
Methane metabolism
Metabolic pathways
Microbial metabolism in diverse environments
Orthology
K08093  
3-hexulose-6-phosphate synthase
K13812  
bifunctional enzyme Fae/Hps
K13831  
3-hexulose-6-phosphate synthase / 6-phospho-3-hexuloisomerase
Genes
EUM: 
STM: 
SEO: 
SEV: 
SEY: 
SEM: 
SEJ: 
SEB: 
SEF: 
SETU: 
SETC: 
SENR: 
SEND: 
SEH: 
SHB: 
SENH: 
SEEH: 
SOD: 
KPN: 
PGE: 
MCA: 
MMT: 
MAH: 
MEALZ_1912(hpsi2) MEALZ_3953(hps1)
MEJ: 
MEC: 
MFA: 
MMB: 
MEH: 
MEI: 
MEP: 
NSA: 
DAO: 
BSU: 
BSU03460(hxlA)
BSR: 
I33_0397(hxlA)
BSL: 
BSH: 
BSY: 
BSS: 
BST: 
GYO_0559(hxlA)
BSO: 
BSN: 
BSQ: 
BSUB: 
BSX: 
C663_0338(hxlA)
BSP: 
BLI: 
BL02045(hxlA)
BLD: 
BLi02805(hxlA)
BLH: 
BAO: 
BAMF_0310(hxlA)
BAY: 
BAQ: 
BYA: 
BAMP: 
BAML: 
BAMA: 
RBAU_0337(hxlA)
BAMN: 
BASU_0321(hxlA)
BAMB: 
BAMT: 
BAZ: 
BQL: 
LL3_00318(hxlA)
BXH: 
BQY: 
MUS_0325(hxlA)
BAMI: 
BAMC: 
BAMF: 
BAE: 
BCL: 
ABC3351(hxlA)
BPU: 
BPUM_2333(hxlA)
BPUM: 
BMQ: 
BMQ_0891(hxlA) BMQ_1538(hxlA) BMQ_2942(hxlA)
BMD: 
BMD_0891(hxlA) BMD_1519(hxlA) BMD_2971(hxlA)
BMH: 
BAG: 
BJS: 
BIF: 
BMET: 
OIH: 
GTN: 
GTH: 
GMC: 
GGH: 
GJF: 
GST: 
SAU: 
SAV: 
SAW: 
SAH: 
SAJ: 
SAM: 
SAS: 
SAR: 
SAC: 
SAX: 
SAA: 
SAO: 
SAE: 
SAD: 
SAAV_0533(hxlA)
SUU: 
SUV: 
SUH: 
SUE: 
SUJ: 
SUK: 
SUC: 
ECTR2_524(hxlA)
SUT: 
SUQ: 
SUZ: 
MS7_0560(hxlA)
SUD: 
SUX: 
SUW: 
SUG: 
SAPIG0645(hxlA)
SUF: 
SAUA: 
SAUE: 
SAUN: 
SAUS: 
SAUU: 
SAUZ: 
SAB: 
SUY: 
SAUB: 
SAUM: 
SAUC: 
CA347_586(hxlA)
SAUR: 
SAUI: 
SAUT: 
SAUJ: 
SAUK: 
SAUQ: 
SAUV: 
SAUW: 
SAUX: 
SAUY: 
SEP: 
SER: 
SEPP: 
SHA: 
SSP: 
SCA: 
SLG: 
SLN: 
SSD: 
SDT: 
SPSE_2213(hxlA)
SWA: 
SPAS: 
SXY: 
SXL: 
MCL: 
ESI: 
EAN: 
EXM: 
PJD: 
GYM: 
PPY: 
PPM: 
PPO: 
PPM_4826(hxlA)
PPOL: 
PPQ: 
PMS: 
PMQ: 
PMW: 
PTA: 
PSAB: 
PDU: 
LBR: 
LBK: 
LCB: 
LCZ: 
LCS: 
LCE: 
LCW: 
LCL: 
LBN: 
LSN: 
LPI: 
LPQ: 
PCE: 
OOE: 
LMM: 
AUR: 
CAC: 
CAE: 
SMB_G0404(sgbH)
CAY: 
CBE: 
CSR: 
ROB: 
EUC: 
RHA: 
ROA: 
CMI: 
CMM_1123(sgaH)
CMS: 
CMC: 
CMN_01092(sgaH)
ART: 
AAU: 
AAI: 
APN: 
ARR: 
AMQ: 
BDE: 
TRS: 
STR: 
CPI: 
CMR: 
EVI: 
ZPR: 
CAO: 
ZGA: 
MPG: 
MJA: 
MFE: 
MVU: 
MFS: 
MIF: 
MJH: 
MIG: 
MMP: 
MMQ: 
MMX: 
MMZ: 
MMD: 
MAE: 
MVN: 
MOK: 
MAC: 
MBA: 
MMA: 
MMAZ: 
MBU: 
MMH: 
MEV: 
MZH: 
MPY: 
MHZ: 
MTP: 
MCJ: 
MHI: 
MHU: 
MLA: 
MEM: 
MBG: 
MPI: 
MBN: 
MFO: 
MPL: 
MPD: 
MEZ: 
RCI: 
RCIX1492 RCIX775(fae-hps)
MER: 
MTH: 
MMG: 
MST: 
MSI: 
MRU: 
MEB: 
MEL: 
MEW: 
METH: 
MFV: 
MKA: 
MK0153(SgbH) MK1449(MenG)
MAX: 
AFU: 
AF0861(hps-1) AF1305(hps-2)
AFG: 
APO: 
AVE: 
AST: 
FPL: 
TAR: 
PHO: 
PAB: 
PAB1222(hps)
PFU: 
PFI: 
PYN: 
PYA: 
PYS: 
TKO: 
TON: 
TGA: 
TSI: 
TBA: 
THE: 
THA: 
THM: 
TLT: 
THS: 
TNU: 
PPAC: 
ABI: 
ACF: 
APE: 
ACJ: 
ACAM_0624(hxlA)
SMR: 
SHC: 
IHO: 
DKA: 
DMU: 
DFD: 
TAG: 
IAG: 
THG: 
HBU: 
PFM: 
SSO: 
SSO0202(hpS-2)
SOL: 
STO: 
SAI: 
SACN: 
SACR: 
SACS: 
SIS: 
SIA: 
SIM: 
SID: 
SIY: 
SIN: 
SII: 
SIH: 
SIR: 
SIC: 
MSE: 
MCN: 
AHO: 
PAI: 
PIS: 
PCL: 
PAS: 
PYR: 
POG: 
TNE: 
CMA: 
TUZ: 
TTN: 
VDI: 
VMO: 
TPE: 
THB: 
ASC: 
CLG: 
FFO: 
KCR: 
 » show all
Taxonomy
Reference
1  [PMID:4219834]
  Authors
Ferenci T, Strom T, Quayle JR
  Title
Purification and properties of 3-hexulose phosphate synthase and phospho-3-hexuloisomerase from Methylococcus capsulatus.
  Journal
Biochem. J. 144 (1974) 477-86.
Reference
2  [PMID:564713]
  Authors
Kato N, Ohashi H, Tani Y, Ogata K
  Title
3-Hexulosephosphate synthase from Methylomonas aminofaciens 77a. Purification, properties and kinetics.
  Journal
Biochim. Biophys. Acta. 523 (1978) 236-44.
Reference
3  [PMID:8595859]
  Authors
Yanase H, Ikeyama K, Mitsui R, Ra S, Kita K, Sakai Y, Kato N
  Title
Cloning and sequence analysis of the gene encoding 3-hexulose-6-phosphate synthase from the methylotrophic bacterium, Methylomonas aminofaciens 77a, and its expression in Escherichia coli.
  Journal
FEMS. Microbiol. Lett. 135 (1996) 201-5.
  Sequence
[up:Q48907]
Reference
4  [PMID:16278835]
  Authors
Yurimoto H, Kato N, Sakai Y
  Title
Assimilation, dissimilation, and detoxification of formaldehyde, a central metabolic intermediate of methylotrophic metabolism.
  Journal
Chem. Rec. 5 (2005) 367-75.
Reference
5  [PMID:16428816]
  Authors
Kato N, Yurimoto H, Thauer RK
  Title
The physiological role of the ribulose monophosphate pathway in bacteria and archaea.
  Journal
Biosci. Biotechnol. Biochem. 70 (2006) 10-21.
Reference
6  [PMID:15901685]
  Authors
Orita I, Yurimoto H, Hirai R, Kawarabayasi Y, Sakai Y, Kato N
  Title
The archaeon Pyrococcus horikoshii possesses a bifunctional enzyme for formaldehyde fixation via the ribulose monophosphate pathway.
  Journal
J. Bacteriol. 187 (2005) 3636-42.
Reference
7
  Authors
Kato, N., Miyamoto, N., Shimao, M. and Sakazawa, C.
  Title
3-Hexulose phosphate pynthase from a new facultative methylotroph, Mycobacterium gastri MB19.
  Journal
Agric. Biol. Chem. 52 (1988) 2659-2661.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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