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
ec00030  Pentose phosphate pathway
ec00680  Methane metabolism
ec01100  Metabolic pathways
ec01120  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: ECUMN_2963
STM: STM2755
SEO: STM14_3320
SEV: STMMW_27231
SEY: SL1344_2739(hxlA)
SEM: STMDT12_C28070
SEJ: STMUK_2743
SEB: STM474_2890
SEF: UMN798_2989(hxlA)
SETU: STU288_13940
SENI: CY43_14395
SEH: SeHA_C2929(hxlA)
SHB: SU5_03243
ECLZ: LI64_16165
KPN: KPN_02957
SOD: Sant_0061
MAH: MEALZ_1912(hpsi2) MEALZ_3953(hps1)
MEJ: Q7A_2498(hxlA) Q7A_2501(hxlA)
MEP: MPQ_0281(sgbH) MPQ_1561
MBAC: BN1209_0202(rmpA) BN1209_0771(rmpA)
MBAT: BN1208_0845(hps)
BSU: BSU03460(hxlA)
BSR: I33_0397(hxlA)
BSL: A7A1_1851
BSH: BSU6051_03460(hxlA)
BSUT: BSUB_00396(hxlA)
BSUL: BSUA_00396(hxlA)
BSUS: Q433_02070
BSS: BSUW23_01790(hxlA)
BST: GYO_0559(hxlA)
BSO: BSNT_06681(hxlA)
BSQ: B657_03460(hxlA)
BSX: C663_0338(hxlA)
BLI: BL02045(hxlA)
BLD: BLi02805(hxlA)
BLH: BaLi_c29000(hxlA)
BAY: RBAM_003630(hxlA)
BAQ: BACAU_0303(hxlA)
BYA: BANAU_0305(hxlA)
BAMP: B938_01575
BAML: BAM5036_0322(hxlA)
BAMA: RBAU_0337(hxlA)
BAMN: BASU_0321(hxlA)
BAMB: BAPNAU_0307(hxlA)
BAMT: AJ82_01980
BAMY: V529_03250(hxlA)
BMP: NG74_00345(hxlA)
BAO: BAMF_0310(hxlA)
BAZ: BAMTA208_01555(hxlA)
BQL: LL3_00318(hxlA)
BXH: BAXH7_00321(hxlA)
BQY: MUS_0325(hxlA)
BAMI: KSO_017855
BAMC: U471_03230
BAMF: U722_01860
BATR: TD68_19410
BCL: ABC3351(hxlA)
BPU: BPUM_2333
BPUM: BW16_12650
BPUS: UP12_11780
BMQ: BMQ_0891(hxlA) BMQ_1538(hxlA) BMQ_2942(hxlA)
BMD: BMD_0891(hxlA) BMD_1519(hxlA) BMD_2971(hxlA)
BMEG: BG04_3186(hxlA) BG04_3830(hxlA) BG04_4896(hxlA) BG04_5472 BG04_5588(hxlA) BG04_5930(hxlA)
BAG: Bcoa_0968
BJS: MY9_0361
BMET: BMMGA3_06845(hxlA)
BACW: QR42_11740
BACP: SB24_07990
BACB: OY17_04480
BACY: QF06_00690
BACL: BS34A_04030(hxlA)
BALM: BsLM_0362
BGY: BGLY_3090(hxlA)
BKW: BkAM31D_07120(hxlA_1) BkAM31D_16315(hxlA_2)
BBEV: BBEV_0241(hxlA)
BALT: CFN77_12450(hxlA)
OIH: OB2806
GTN: GTNG_1490
GGH: GHH_c21400(hxlA)
GEA: GARCT_00704(hxlA_1) GARCT_02004(hxlA_2)
ANM: GFC28_662
ANL: GFC29_964
SAU: SA0528
SAV: SAV0570
SAW: SAHV_0568
SAM: MW0525
SAS: SAS0528
SAR: SAR0574
SAC: SACOL0617
SAE: NWMN_0533
SAD: SAAV_0533(hxlA)
SUE: SAOV_0605
SUJ: SAA6159_00524(hxlA)
SUK: SAA6008_00578(hxlA)
SUC: ECTR2_524(hxlA)
SUQ: HMPREF0772_12618(hxlA)
SUZ: MS7_0560(hxlA)
SUG: SAPIG0645(hxlA)
SAUA: SAAG_00991
SAUE: RSAU_000524(hps)
SAUS: SA40_0511
SAUU: SA957_0526
SAUG: SA268_0524
SAUF: X998_0612(hxlA)
SAB: SAB0520
SAUB: C248_0645
SAUM: BN843_5640
SAUC: CA347_586(hxlA)
SAUR: SABB_00621
SAUI: AZ30_02885
SAUD: CH52_02905
SAMS: NI36_02840
SEP: SE0341
SER: SERP0216
SEPP: SEB_00262
SEPS: DP17_1647(hxlA)
SHA: SH2420
SHH: ShL2_02215(hxlA)
SDT: SPSE_2213(hxlA)
SPAS: STP1_1658
SHU: SHYC_10795(hxlA)
SSCH: LH95_10395
SSCZ: RN70_11130
SAGQ: EP23_11365
SSIF: AL483_08720(hxlA)
SPET: CEP67_09865(hxlA)
SSCU: CEP64_01020(hxlA)
SKL: C7J89_12605(hxlA)
MCL: MCCL_0037
MCAK: MCCS_00640
ESI: Exig_2372
EAN: Eab7_2216
PPY: PPE_04673
PPM: PPSC2_24305(hxlA)
PPO: PPM_4826(hxlA)
PPOL: X809_40845
PPQ: PPSQR21_049250(sgbH)
PPOY: RE92_12975
PMS: KNP414_07885(hxlA)
PMW: B2K_37330
PRI: PRIO_3567 PRIO_6499(hxlA)
PSWU: SY83_08105
PDH: B9T62_30300(hxlA)
PLX: CW734_09535(hxlA) CW734_13380(hxlA)
LBR: LVIS_0442
LPAP: LBPC_0348
LBN: LBUCD034_0077(hxlA)
LSN: LSA_03490
PCE: PECL_1750
OOE: OEOE_0131
LMM: MI1_09731
AUR: HMPREF9243_0240(hxlA)
CAC: CA_C0396
CAE: SMB_G0404(sgbH)
CAY: CEA_G0406
CBE: Cbei_4647
CBZ: Cbs_4647
CBEI: LF65_06885
ROB: CK5_18950
PFT: JBW_00828
EUC: EC1_08720
CDX: CDES_00570(rmpA)
CMI: CMM_1123(sgaH)
CMS: CMS1443(hps)
CMC: CMN_01092(sgaH)
ART: Arth_3708
ARR: ARUE_c04640(rmpA)
ARN: CGK93_01940(hxlA)
ARX: ARZXY2_3983(hxlA)
AAU: AAur_0494(hps)
AAI: AARI_06580(rmpA)
AMQ: AMETH_4519(hps) AMETH_4538(hps)
BDE: BDP_0013
BDN: BBDE_0013
BANG: BBAG_0932
TTR: Tter_2273
RBA: RB5319
PIR: VN12_13465(hxlA)
ABAC: LuPra_03104(hxlA)
CPI: Cpin_5671
FLN: FLA_3348
ZPR: ZPR_1061
MARM: YQ22_17840
CBAL: M667_16185
CBAT: M666_16170
ZGA: ZOBELLIA_3942(hxlA)
AALG: AREALGSMS7_04556(hxlA)
MMP: MMP1270
MMD: GYY_07185
MBU: Mbur_1994(fae-hps)
MEMA: MMAB1_1386(fae-hps) MMAB1_1456(hpsA)
MPD: MCP_0861 MCP_2904(fae_hps)
MEZ: Mtc_0381(fae) Mtc_1411
RCI: RCIX1492 RCIX775(fae-hps)
MMG: MTBMA_c00570(fae_hps) MTBMA_c12830
MWO: MWSIV6_0011(fae-hps) MWSIV6_1262(hpsA)
METE: tca_00853(proA) tca_01421(fae)
METH: MBMB1_0009(fae-hps) MBMB1_0388
MFI: DSM1535_0057 DSM1535_1378(fae-hps)
MCUB: MCBB_0021(fae-hps_1) MCBB_0344(hpsA)
MKA: MK0153(sgbH) MK1449(menG)
MEAR: Mpt1_c14440(faeB)
MARC: AR505_0014
PHO: PH1938(PH1938)
PAB: PAB1222
PFU: PF0220
PFI: PFC_00160
PYN: PNA2_0868
PYS: Py04_0376
TKO: TK0475
TON: TON_0336
TGA: TGAM_1891(hps)
TSI: TSIB_0428
THE: GQS_03555
THA: TAM4_82
THM: CL1_0365
TLT: OCC_09933
THS: TES1_0756
TNU: BD01_0222
TEU: TEU_06790
PPAC: PAP_05755
ABI: Aboo_0457
APE: APE_0952.1(hxlA)
ACJ: ACAM_0624(hxlA)
SMR: Smar_0492
IHO: Igni_0269
IIS: EYM_01130
DKA: DKAM_1456
TAG: Tagg_1068
IAG: Igag_1921
HBU: Hbut_0129
SSO: SSO0202(hpS-2)
SOL: Ssol_1184
SSOA: SULA_1220
SSOL: SULB_1221
SSOF: SULC_1219
STO: STK_02380(hxlA)
SAI: Saci_0802
SID: M164_1939
SII: LD85_2191
SIH: SiH_1876
SIR: SiRe_1804
SIC: SiL_1785
MSE: Msed_0227
MCN: Mcup_1845
AHO: Ahos_0599
PAI: PAE1679
PIS: Pisl_1686
PCL: Pcal_0568
PAS: Pars_1830
PYR: P186_0040
POG: Pogu_0300
TNE: Tneu_0708
CMA: Cmaq_1871
TUZ: TUZN_2015
TTN: TTX_1521(hps)
VDI: Vdis_1817
VMO: VMUT_0258
TPE: Tpen_0372
ASC: ASAC_0959
NCV: NCAV_0256
KCR: Kcr_1307
BARC: AOA65_1083(faeB-hpsB)
 » 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 144:477-86 (1974)
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 523:236-44 (1978)
DOI:10.1016/0005-2744(78)90026-8
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 135:201-5 (1996)
  Sequence
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 5:367-75 (2005)
DOI:10.1002/tcr.20056
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 70:10-21 (2006)
DOI:10.1271/bbb.70.10
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 187:3636-42 (2005)
DOI:10.1128/JB.187.11.3636-3642.2005
  Sequence
[pho:PH1938]
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 52:2659-2661 (1988)
Other DBs
ExplorEnz - The Enzyme Database: 4.1.2.43
IUBMB Enzyme Nomenclature: 4.1.2.43
ExPASy - ENZYME nomenclature database: 4.1.2.43
BRENDA, the Enzyme Database: 4.1.2.43

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