KEGG   ENZYME: 2.6.1.86Help
Entry
EC 2.6.1.86                 Enzyme                                 

Name
2-amino-4-deoxychorismate synthase;
ADIC synthase;
2-amino-2-deoxyisochorismate synthase;
SgcD
Class
Transferases;
Transferring nitrogenous groups;
Transaminases
BRITE hierarchy
Sysname
(2S)-2-amino-4-deoxychorismate:2-oxoglutarate aminotransferase
Reaction(IUBMB)
(2S)-2-amino-4-deoxychorismate + L-glutamate = chorismate + L-glutamine [RN:R08956]
Reaction(KEGG)
Substrate
(2S)-2-amino-4-deoxychorismate [CPD:C18054];
L-glutamate [CPD:C00025]
Product
chorismate [CPD:C00251];
L-glutamine [CPD:C00064]
Comment
Requires Mg2+. The reaction occurs in the reverse direction to that shown above. In contrast to most anthranilate-synthase I (ASI) homologues, this enzyme is not inhibited by tryptophan. In Streptomyces globisporus, the sequential action of this enzyme and EC 1.3.99.24, 2-amino-4-deoxychorismate dehydrogenase, leads to the formation of the benzoxazolinate moiety of the enediyne antitumour antibiotic C-1027 [1,2]. In certain Pseudomonads the enzyme participates in the biosynthesis of phenazine, a precursor for several compounds with antibiotic activity [3,4].
History
EC 2.6.1.86 created 2008
Pathway
ec00405  Phenazine biosynthesis
ec01059  Biosynthesis of enediyne antibiotics
ec01130  Biosynthesis of antibiotics
Orthology
K13063  2-amino-4-deoxychorismate synthase
K20159  2-amino-4-deoxychorismate synthase
K21175  2-amino-4-deoxychorismate synthase, glutamine amidotransferase component
Genes
KOC: AB185_20690
SFW: WN53_03385
ECA: ECA2701(ehpC)
PATR: EV46_13195
PATO: GZ59_18590(ehpC)
XDO: XDD1_2436(phzE)
XPO: XPG1_2291(tomD)
XHO: A9255_10780
LAB: LA76x_3333
LAQ: GLA29479_2366(phzE)
PAE: PA1903(phzE2) PA4214(phzE1)
PAU: PA14_09440(phzE1)
PAG: PLES_07131(phzE1) PLES_34211(phzE2)
PAF: PAM18_0723(phzE1) PAM18_3139(phzE2)
PNC: NCGM2_2820(phzE2) NCGM2_5459(phzE2)
PAEB: NCGM1900_0745(phzE2) NCGM1900_4586(phzE2)
PAEL: T223_17485
PAEU: BN889_06971(phzE1_4) BN889_07067(phzE1_7) BN889_07250(phzE1_9)
PFB: VO64_0338
PSET: THL1_3622
BGU: KS03_4991
BVR: BVIR_2862
MAB: MAB_0298
MABB: MASS_0299
MABO: NF82_01500
MCHE: BB28_01470
MSTE: MSTE_00260
SCO: SCO2117(SC6E10.11)
SMA: SAVERM_6084(phzE)
SGR: SGR_5385
SCB: SCAB_67631(trpE)
SCT: SCAT_1246(phzB)
SFA: Sfla_4700
SBH: SBI_07844
SHY: SHJG_3601
SVE: SVEN_1778
SDV: BN159_6319(phzB)
STRP: F750_1981
SALL: SAZ_14330
SLV: SLIV_27120(phzB)
STRE: GZL_06398
SLD: T261_6049
SAMB: SAM23877_2213(phzB)
SPRI: SPRI_5382
SRW: TUE45_02649(trpE_2)
SLE: sle_50210(sle_50210) sle_57420(sle_57420)
SRN: A4G23_01307(trpG) A4G23_05416(trpE_2)
SMAL: SMALA_2052
SLAU: SLA_1712
SALF: SMD44_02324(phzE)
SLX: SLAV_26615(phnA)
SFK: KY5_2100
MTS: MTES_0388
SERJ: SGUI_2558
NCA: Noca_4529
NDK: I601_1070(phnA_1)
PSIM: KR76_01360
NDA: Ndas_5031
FAL: FRAAL3440
KRA: Krad_1199
KAL: KALB_2053
SAQ: Sare_3182
MIL: ML5_4130
ASE: ACPL_1962(phzE)
ACTN: L083_2374 L083_5379(phzE)
AFS: AFR_11460
ACTS: ACWT_1840
CAI: Caci_0239
 » show all
Taxonomy
Reference
1  [PMID:18182490]
  Authors
Van Lanen SG, Lin S, Shen B.
  Title
Biosynthesis of the enediyne antitumor antibiotic C-1027 involves a new branching point in chorismate metabolism.
  Journal
Proc Natl Acad Sci U S A 105:494-9 (2008)
DOI:10.1073/pnas.0708750105
  Sequence
Reference
2
  Authors
Yu, L., Mah, S., Otani, T. and Dedon, P.
  Title
The benzoxazolinate of C-1027 confers intercalative DNA binding.
  Journal
J Am Chem Soc 117:8877-8878 (1995)
Reference
3  [PMID:11562236]
  Authors
McDonald M, Mavrodi DV, Thomashow LS, Floss HG.
  Title
Phenazine biosynthesis in Pseudomonas fluorescens: branchpoint from the primary shikimate biosynthetic pathway and role of phenazine-1,6-dicarboxylic acid.
  Journal
J Am Chem Soc 123:9459-60 (2001)
  Sequence
Reference
4  [PMID:15008629]
  Authors
Laursen JB, Nielsen J.
  Title
Phenazine natural products: biosynthesis, synthetic analogues, and biological activity.
  Journal
Chem Rev 104:1663-86 (2004)
DOI:10.1021/cr020473j
Other DBs
ExplorEnz - The Enzyme Database: 2.6.1.86
IUBMB Enzyme Nomenclature: 2.6.1.86
ExPASy - ENZYME nomenclature database: 2.6.1.86
BRENDA, the Enzyme Database: 2.6.1.86

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