KEGG   ORTHOLOGY: K22345
Entry
K22345                      KO                                     
Symbol
E4.3.1.9
Name
glucosaminate ammonia-lyase [EC:4.3.1.9]
Pathway
map00030  Pentose phosphate pathway
map01100  Metabolic pathways
Brite
KEGG Orthology (KO) [BR:ko00001]
 09100 Metabolism
  09101 Carbohydrate metabolism
   00030 Pentose phosphate pathway
    K22345  E4.3.1.9; glucosaminate ammonia-lyase
Enzymes [BR:ko01000]
 4. Lyases
  4.3  Carbon-nitrogen lyases
   4.3.1  Ammonia-lyases
    4.3.1.9  glucosaminate ammonia-lyase
     K22345  E4.3.1.9; glucosaminate ammonia-lyase
Other DBs
RN: R01544
COG: COG0492
GO: 0047930
Genes
PAE: PA0849(trxB2)
PAEV: N297_876(trxB)
PAEI: N296_876(trxB)
PAU: PA14_53290(trxB2)
PAP: PSPA7_4671(trxB1)
PAG: PLES_44691(trxB2)
PAF: PAM18_4191(trxB2)
PNC: NCGM2_1623(trxB2)
PAEB: NCGM1900_1877(trxB2)
PDK: PADK2_21460
PAEP: PA1S_22200
PAEM: U769_21570
PAEL: T223_22835
PAEU: BN889_00876(trxB2)
PAEG: AI22_11740
PAEC: M802_872(trxB)
PAEO: M801_876(trxB)
PMY: Pmen_0978
PMK: MDS_1066
PRE: PCA10_47670(trxB)
PPSE: BN5_3403
PMUI: G4G71_08585(trxB)
PPU: PP_0786(trxB)
PPF: Pput_0809
PPT: PPS_0839
PPB: PPUBIRD1_0830(trxB)
PPI: YSA_06637
PPX: T1E_2100(trxB)
PPUH: B479_04405
PPUT: L483_03945
PPUN: PP4_44970(trxB)
PPUD: DW66_0801
PMON: X969_02440
PMOT: X970_02420
PMOL: CLJ08_17245(trxB)
PST: PSPTO_1178(trxB)
PSB: Psyr_1016
PSYR: N018_20605
PSP: PSPPH_1067(trxB)
PAMG: BKM19_007795(trxB)
PAVL: BKM03_06735(trxB)
PCAB: JGS08_05510(trxB)
PFL: PFL_0945(trxB_1)
PPRC: PFLCHA0_c09600(trxB1)
PPRO: PPC_0979
PFE: PSF113_2176(trxB1) PSF113_4883(trxB2)
PFS: PFLU_5162
PFC: PflA506_4454(trxB)
PFB: VO64_2002
PMAN: OU5_2518(trxB)
PRX: HRH33_22510(trxB)
PFW: PF1751_v1c46110(trxB)
PEN: PSEEN0924(trxB)
PLUL: FOB45_09070(trxB)
PPUU: PputUW4_00805(trxB1)
PKC: PKB_4627(trxb3)
PSES: PSCI_0771
PSEM: TO66_04840
PSOS: POS17_0950
PANR: A7J50_4906
PSET: THL1_4770
PSIL: PMA3_24915
PKE: DLD99_04830(trxB)
PALL: UYA_04805
PUM: HGP31_04615(trxB)
POJ: PtoMrB4_46880(trxB2)
PPSH: G5J76_22520(trxB)
PGY: AWU82_19430(trxB)
PLAL: FXN65_22930(trxB)
PSEJ: HNQ25_19360(trxB)
PVK: EPZ47_04655(trxB)
PEZ: HWQ56_04785(trxB)
PBZ: GN234_23410(trxB)
PKH: JLK41_05140(trxB)
PTY: JWV26_15885(trxB)
PMAO: PMYSY11_0858(trxB)
PATA: JWU58_23070(trxB)
PDW: BV82_0171(trxB)
PZE: HU754_005895(trxB)
PMOE: HV782_005500(trxB)
PCAM: HNE05_11920(trxB)
PSEP: C4K39_0964
PVW: HU752_027775(trxB)
PTRT: HU722_0024570(trxB)
PXA: KSS93_25260(trxB)
PSAM: HU731_010990(trxB)
PTZ: HU718_005555(trxB)
PQI: KH389_04205(trxB)
PSHH: HU773_005415(trxB)
PXN: HU772_020750(trxB)
PHV: HU739_013055(trxB)
PPRG: HU725_019070(trxB)
PNN: KEM63_02915(trxB)
PANH: HU763_004140(trxB)
PASG: KSS96_23885(trxB)
PFAK: KSS94_22760(trxB)
PMUY: KSS95_23555(trxB)
PMAM: KSS90_21625(trxB)
PAZE: KSS91_04870(trxB)
PALV: KSS97_05625(trxB)
PORY: EJA05_23790(trxB)
PWZ: J7655_04615(trxB)
PTK: EXN22_05660(trxB)
PTW: TUM18999_50800(trxB2)
PZA: HU749_024815(trxB)
PIE: HU724_005340(trxB)
PWY: HU734_021970(trxB)
PTAE: NCTC10697_03611(trxB)
HPEG: EAO82_18575(trxB)
HAES: LO767_02085(trxB)
HAM: HALO0949
HHH: CLM76_03120(trxB)
HALK: CUU95_09030(trxB)
HVN: EI420_17130(trxB)
HOL: HORIV_57640(trxB2)
HSR: HSBAA_55260(trxB2)
HMD: CTT34_15625(trxB)
HTT: HZS52_09595(trxB)
HPIZ: GYM47_14845(trxB)
DNO: DNO_1099(trxB)
CHJ: NCTC10426_00934(trxB)
NWE: SAMEA3174300_0977(trxB)
NSI: A6J88_08345(trxB)
NMJ: NM96_03025(trxB)
NEI: BG910_11830(trxB)
NSF: FAH66_02675(trxB)
NZL: D0T92_06925(trxB)
KKI: KKKWG1_1505(trxB)
PLG: NCTC10937_04342(trxB)
AXY: AXYL_00105(trxB1)
SUTT: SUTMEG_20070(trxB)
SUTK: FG381_06245(trxB)
SWS: I6J16_12290(trxB)
GLO: Glov_3350
SECH: B18_15890
PARH: I5S86_24710(trxB)
HSU: HLASF_1657(trxB2)
HSF: HLASA_1644(trxB2)
HHI: HAH_1736(trxB2)
HWA: HQ_1652A(trxB2)
HWC: Hqrw_1767(trxB2)
HME: HFX_1131(trxB)
 » show all
Reference
  Authors
Iwamoto R, Amano C, Ikehara K, Ushida N
  Title
The D-glucosaminate dehydratase alpha-subunit from Pseudomonas fluorescens exhibits thioredoxin reductase activity.
  Journal
Biochim Biophys Acta 1647:310-4 (2003)
DOI:10.1016/S1570-9639(03)00079-7
  Sequence
LinkDB

KEGG   ENZYME: 4.3.1.9
Entry
EC 4.3.1.9                  Enzyme                                 
Name
glucosaminate ammonia-lyase;
glucosaminic dehydrase;
D-glucosaminate dehydratase;
D-glucosaminic acid dehydrase;
aminodeoxygluconate dehydratase;
2-amino-2-deoxy-D-gluconate hydro-lyase (deaminating);
aminodeoxygluconate ammonia-lyase;
2-amino-2-deoxy-D-gluconate ammonia-lyase;
D-glucosaminate ammonia-lyase;
D-glucosaminate ammonia-lyase (isomerizing;
2-dehydro-3-deoxy-D-gluconate-forming)
Class
Lyases;
Carbon-nitrogen lyases;
Ammonia-lyases
Sysname
2-amino-2-deoxy-D-gluconate ammonia-lyase (isomerizing; 2-dehydro-3-deoxy-D-gluconate-forming)
Reaction(IUBMB)
2-amino-2-deoxy-D-gluconate = 2-dehydro-3-deoxy-D-gluconate + NH3 (overall reaction) [RN:R01544];
(1a) 2-amino-2-deoxy-D-gluconate = (2Z,4S,5R)-2-amino-4,5,6-trihydroxyhex-2-enoate + H2O [RN:R10773];
(1b) (2Z,4S,5R)-2-amino-4,5,6-trihydroxyhex-2-enoate = (4S,5R)-4,5,6-trihydroxy-2-iminohexanoate (spontaneous) [RN:R10774];
(1c) (4S,5R)-4,5,6-trihydroxy-2-iminohexanoate + H2O = 2-dehydro-3-deoxy-D-gluconate + NH3 (spontaneous) [RN:R10775]
Reaction(KEGG)
R01544 R10773 R10774 R10775;
(other) R06132
Substrate
2-amino-2-deoxy-D-gluconate [CPD:C03752];
(2Z,4S,5R)-2-amino-4,5,6-trihydroxyhex-2-enoate [CPD:C20844];
(4S,5R)-4,5,6-trihydroxy-2-iminohexanoate [CPD:C20845];
H2O [CPD:C00001]
Product
2-dehydro-3-deoxy-D-gluconate [CPD:C00204];
NH3 [CPD:C00014];
(2Z,4S,5R)-2-amino-4,5,6-trihydroxyhex-2-enoate [CPD:C20844];
H2O [CPD:C00001];
(4S,5R)-4,5,6-trihydroxy-2-iminohexanoate [CPD:C20845]
Comment
Contains pyridoxal phosphate. The enzyme releases an unstable enamine product that tautomerizes to an imine form, which undergoes spontaneous hydrolytic deamination to form the final product.
History
EC 4.3.1.9 created 1972, (EC 4.3.1.21 created 1965 as EC 4.2.1.26, transferred 2002 to EC 4.3.1.21, incorporated 2004) modified 2004
Pathway
ec00030  Pentose phosphate pathway
ec01100  Metabolic pathways
Orthology
K22345  glucosaminate ammonia-lyase
Genes
PAEPA0849(trxB2)
PAEVN297_876(trxB)
PAEIN296_876(trxB)
PAUPA14_53290(trxB2)
PAPPSPA7_4671(trxB1)
PAGPLES_44691(trxB2)
PAFPAM18_4191(trxB2)
PNCNCGM2_1623(trxB2)
PAEBNCGM1900_1877(trxB2)
PDKPADK2_21460
PSGG655_21110
PRPM062_04130
PAEPPA1S_22200
PAERPA1R_gp4371
PAEMU769_21570
PAELT223_22835
PAESSCV20265_4679
PAEUBN889_00876(trxB2)
PAEGAI22_11740
PAECM802_872(trxB)
PAEOM801_876(trxB)
PMYPmen_0978
PMKMDS_1066
PREPCA10_47670(trxB)
PPSEBN5_3403
PFUWKF707C_47340
PALCA0T30_07600
PCQPcP3B5_51170
PMUIG4G71_08585(trxB)
PPUPP_0786(trxB)
PPFPput_0809
PPGPputGB1_0820
PPWPputW619_4408
PPTPPS_0839
PPBPPUBIRD1_0830(trxB)
PPIYSA_06637
PPXT1E_2100(trxB)
PPUHB479_04405
PPUTL483_03945
PPUNPP4_44970(trxB)
PPUDDW66_0801
PFVPsefu_3370
PMONX969_02440
PMOTX970_02420
PMOSO165_028095
PPJRK21_04166
PORAPT59_03560
PMOLCLJ08_17245(trxB)
PSTPSPTO_1178(trxB)
PSBPsyr_1016
PSYRN018_20605
PSPPSPPH_1067(trxB)
PSAVPSA3335_08840
PAMGBKM19_007795(trxB)
PCIPCH70_09420
PAVLBKM03_06735(trxB)
PVDCFBP1590__4340
PCABJGS08_05510(trxB)
PFLPFL_0945(trxB_1)
PPRCPFLCHA0_c09600(trxB1)
PPROPPC_0979
PFEPSF113_2176(trxB1) PSF113_4883(trxB2)
PFNHZ99_22980
PFOPfl01_0887
PFSPFLU_5162
PFCPflA506_4454(trxB)
PPZH045_16490
PFBVO64_2002
PMANOU5_2518(trxB)
PTVAA957_19195
PCGAXG94_05355 AXG94_19945
PVRPverR02_26300
PAZOAYR47_01680
POIBOP93_21720
PRXHRH33_22510(trxB)
PFWPF1751_v1c46110(trxB)
PFFPFLUOLIPICF712960
PFXA7318_21530
PENPSEEN0924(trxB)
PLULFOB45_09070(trxB)
PBAPSEBR_a3564 PSEBR_a4717
PBCCD58_04760
PPUUPputUW4_00805(trxB1)
PDRH681_19980
PSVPVLB_21190
PSKU771_26675
PKCPKB_4627(trxb3)
PCHEY04_04125
PCZPCL1606_51480
PCPJM49_25560
PFZAV641_18765
PLQAA042_14850
PALKPSAKL28_45190
PRHLT40_20370
PSWLK03_09545
PPVNJ69_00675
PSESPSCI_0771
PSEMTO66_04840
PSECCCOS191_4496
PPSYAOC04_15985
PSOSPOS17_0950
PKRAYO71_07225
PFKPFAS1_06720
PANRA7J50_4906
PPSLBJP27_17955
PSETTHL1_4770
PSILPMA3_24915
PYMAK972_4997
PADEC3B55_00980
PKEDLD99_04830(trxB)
PALLUYA_04805
PUMHGP31_04615(trxB)
POJPtoMrB4_46880(trxB2)
PGGFX982_00732
PPSHG5J76_22520(trxB)
PGYAWU82_19430(trxB)
PLALFXN65_22930(trxB)
PSEJHNQ25_19360(trxB)
PVKEPZ47_04655(trxB)
PEZHWQ56_04785(trxB)
PBZGN234_23410(trxB)
PKHJLK41_05140(trxB)
PTYJWV26_15885(trxB)
PMAOPMYSY11_0858(trxB)
PATAJWU58_23070(trxB)
PDWBV82_0171(trxB)
PZEHU754_005895(trxB)
PMOEHV782_005500(trxB)
PCAMHNE05_11920(trxB)
PSEPC4K39_0964
PVWHU752_027775(trxB)
PTRTHU722_0024570(trxB)
PXAKSS93_25260(trxB)
PSAMHU731_010990(trxB)
PTZHU718_005555(trxB)
PQIKH389_04205(trxB)
PSHHHU773_005415(trxB)
PXNHU772_020750(trxB)
PHVHU739_013055(trxB)
PPRGHU725_019070(trxB)
PNNKEM63_02915(trxB)
PANHHU763_004140(trxB)
PASGKSS96_23885(trxB)
PFAKKSS94_22760(trxB)
PMUYKSS95_23555(trxB)
PMAMKSS90_21625(trxB)
PAZEKSS91_04870(trxB)
PALVKSS97_05625(trxB)
PPHABVH74_07995
PORYEJA05_23790(trxB)
PWZJ7655_04615(trxB)
PTKEXN22_05660(trxB)
PTWTUM18999_50800(trxB2)
PZAHU749_024815(trxB)
PIEHU724_005340(trxB)
PWYHU734_021970(trxB)
PTAENCTC10697_03611(trxB)
PBBAKN87_04860
HPEGEAO82_18575(trxB)
HAESLO767_02085(trxB)
HCSFF32_03085
HAKKO116_00917
HAMHALO0949
HHHCLM76_03120(trxB)
HAGBB497_02120
HALKCUU95_09030(trxB)
HVNEI420_17130(trxB)
HOLHORIV_57640(trxB2)
HSRHSBAA_55260(trxB2)
HMDCTT34_15625(trxB)
HAXIHAALTHF_17720n
HTTHZS52_09595(trxB)
HPIZGYM47_14845(trxB)
DNODNO_1099(trxB)
CHJNCTC10426_00934(trxB)
NWESAMEA3174300_0977(trxB)
NSIA6J88_08345(trxB)
NMJNM96_03025(trxB)
NEIBG910_11830(trxB)
NSFFAH66_02675(trxB)
NZLD0T92_06925(trxB)
KKIKKKWG1_1505(trxB)
SMURBWP33_08650
PLGNCTC10937_04342(trxB)
AXYAXYL_00105(trxB1)
SUTTSUTMEG_20070(trxB)
SUTKFG381_06245(trxB)
SWSI6J16_12290(trxB)
GLOGlov_3350
SECHB18_15890
PARHI5S86_24710(trxB)
HJEHacjB3_09255
HSUHLASF_1657(trxB2)
HSFHLASA_1644(trxB2)
HHIHAH_1736(trxB2)
HHNHISP_08860
HABSG26_16590
HTABVU17_08370
HWAHQ_1652A(trxB2)
HWCHqrw_1767(trxB2)
HMEHFX_1131(trxB)
HGIABY42_05470
HALEG3A49_08835
HAERDU502_08980
HRAEI982_04615
HLMDV707_08530
 » show all
Reference
1
  Authors
Imanaga, Y.
  Title
Metabolism of D-glucosamine. III. Enzymic degradation of D-glucosaminic acid.
  Journal
J Biochem (Tokyo) 45:647-650 (1958)
Reference
2
  Authors
Merrick, J.M. and Roseman, S.
  Title
D-Glucosaminic acid dehydrase.
  Journal
Methods Enzymol 9:657-660 (1966)
Reference
3  [PMID:7068563]
  Authors
Iwamoto R, Imanaga Y, Soda K.
  Title
D-glucosaminate dehydratase from Agrobacterium radiobacter. Physicochemical and enzymological properties.
  Journal
J Biochem (Tokyo) 91:283-9 (1982)
DOI:10.1093/oxfordjournals.jbchem.a133686
Reference
4  [PMID:7766176]
  Authors
Iwamoto R, Taniki H, Koishi J, Nakura S.
  Title
D-glucosaminate aldolase activity of D-glucosaminate dehydratase from Pseudomonas fluorescens and its requirement for Mn2+ ion.
  Journal
Biosci Biotechnol Biochem 59:408-11 (1995)
DOI:10.1271/bbb.59.408
Other DBs
ExplorEnz - The Enzyme Database: 4.3.1.9
IUBMB Enzyme Nomenclature: 4.3.1.9
ExPASy - ENZYME nomenclature database: 4.3.1.9
BRENDA, the Enzyme Database: 4.3.1.9
CAS: 37290-91-8
LinkDB

KEGG   REACTION: R01544
Entry
R01544                      Reaction                               
Name
2-amino-2-deoxy-D-gluconate ammonia-lyase (isomerizing; 2-dehydro-3-deoxy-D-gluconate-forming)
Definition
2-Amino-2-deoxy-D-gluconate <=> 2-Dehydro-3-deoxy-D-gluconate + Ammonia
Equation
Comment
PLP-dependent enzyme (see R10773+R10774+R10775)
Reaction class
RC00544  C00204_C03752
Enzyme
Pathway
rn00030  Pentose phosphate pathway
rn01100  Metabolic pathways
Orthology
K22345  glucosaminate ammonia-lyase [EC:4.3.1.9]
Other DBs
RHEA: 12491
LinkDB

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