KEGG   ENZYME: 3.3.2.15
Entry
EC 3.3.2.15                 Enzyme                                 
Name
trans-2,3-dihydro-3-hydroxyanthranilic acid synthase;
isochorismatase (ambiguous);
phzD (gene name)
Class
Hydrolases;
Acting on ether bonds;
Ether hydrolases
Sysname
(2S)-2-amino-4-deoxychorismate pyruvate-hydrolase
Reaction(IUBMB)
(2S)-2-amino-4-deoxychorismate + H2O = (5S,6S)-6-amino-5-hydroxycyclohexa-1,3-diene-1-carboxylate + pyruvate [RN:R11463]
Reaction(KEGG)
R11463
Substrate
(2S)-2-amino-4-deoxychorismate [CPD:C18054];
H2O [CPD:C00001]
Product
(5S,6S)-6-amino-5-hydroxycyclohexa-1,3-diene-1-carboxylate [CPD:C19830];
pyruvate [CPD:C00022]
Comment
Isolated from the bacterium Pseudomonas aeruginosa. Involved in phenazine biosynthesis.
History
EC 3.3.2.15 created 2016
Pathway
ec00405  Phenazine biosynthesis
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
Orthology
K20261  trans-2,3-dihydro-3-hydroxyanthranilic acid synthase
Genes
KGRJJJ10_13560
SFWWN53_03390
PATREV46_13200
PATOGZ59_18580(ehpB)
PPAVLOZ86_13700
LABLA76x_3334(phzD1)
LAQGLA29479_2367(phzD1)
PAEPA1902(phzD2) PA4213(phzD1)
PAEVN297_1962 N297_4345
PAEIN296_1962 N296_4345
PAUPA14_09450(phzD1) PA14_39925(phzD2)
PAPPSPA7_0886 PSPA7_3382
PAGPLES_07141(phzD1) PLES_34221(phzD2)
PAFPAM18_0724(phzD1) PAM18_3140(phzD2)
PAEBNCGM1900_4587
PDKPADK2_03605 PADK2_16140
PSGG655_03640 G655_15605
PRPM062_22195
PAEPPA1S_03755 PA1S_16430
PAERPA1R_gp2104 PA1R_gp5531
PAEMU769_03785 U769_16145
PAELT223_03690 T223_17490
PAESSCV20265_0748 SCV20265_3493
PAEUBN889_06463(phzD1_1) BN889_06777(phzD1_3) BN889_07359(phzD1_6)
PAEGAI22_00155 AI22_17560
PAECM802_1960 M802_4343
PAEOM801_1961 M801_4211
PFBVO64_0337
POIBOP93_12305
PCHEY04_26285
PCPJM49_05460
PSETTHL1_3621
PYMAK972_2556
PSEPC4K39_3098
BUUWS70_27180
BURBcep18194_B1569
BGLbglu_2g09250
BGUKS03_4992
BVRBVIR_2863
SECHB18_04210 B18_21400
MABMAB_0297
MMVMYCMA_0159
MABBMASS_0298
MABLMMASJCM_0294
MCHEBB28_01465
MIZBAB75_02015
MSAOMYCSP_01295
MSALDSM43276_00252(phzD_1)
CMVCMUST_14535
NBRO3I_033280
NAHF5544_33425
NHUH0264_16225
RFAA3L23_00644(phzD)
RHSA3Q41_02711(phzD)
TPRTpau_0113
SALBXNR_0597
SCBSCAB_12041
SSXSACTE_1752
SALSSLNWT_4919
SFISFUL_3324 SFUL_5262
SGUSGLAU_17220(phzA)
STRMM444_18420
STRCAA958_30770
SCZABE83_19210 ABE83_26415
SRNA4G23_05417(phzD)
STRTA8713_24035
SGMGCM10017557_24350(phzD1)
SCADDN051_13635 DN051_37360
SLSSLINC_5468
SPLULK06_026280
STRDNI25_24440
SNWBBN63_05570
SALJSMD11_1729 SMD11_3253
SQZFQU76_00255 FQU76_33485
SASTCD934_07145
SGZC0216_00425
SVNCP980_14880
SRKFGW37_24780
SVRCP971_17430
SPADDVK44_32315
SCAVCVT27_15340
SSEOD0Z67_01715
SCINCP977_15855
SFUGCNQ36_29865
SSPBCP982_28280
SHUNDWB77_04281(phzD)
SLIAHA039_29910
SFBCP974_28840
SROIIAG44_13945 IAG44_38380
STRYEQG64_08385 EQG64_16160
SMAOCAG99_00490 CAG99_15050
KSKKSE_58300 KSE_59070
KAUB6264_12425
KITCFP65_3611
STRIC7M71_014740
FRPAX769_15030
RTERIDM49_10735
RAMAIDM48_01840
CEZCBP52_12015
KQIF1D05_31625
THAONI17_009045
NDANdas_5030
STRREKD16_18440(phzD)
ACTWF7P10_05705
NOABKM31_19750
NGNLCN96_24510
FREFranean1_3619
SACGFDZ84_16255
AMYCCU254_36750
PHHAFB00_28930
APRECNX65_15955
SSYIEKG83_21240
KPHYAOZ06_22495 AOZ06_25085
ALOCRK58740
MICBMicB006_2898
MICHFJK98_01250
MSAGGCM10017556_11840
PFLAPflav_059760
PSUUPsuf_020500 Psuf_091090
PRYPrubr_64680(phzD1)
GLYK3N28_00720
ACTCCHIBA101_0087
AEYCDG81_16850
 » show all
Reference
1  [PMID:11591691]
  Authors
Mavrodi DV, Bonsall RF, Delaney SM, Soule MJ, Phillips G, Thomashow LS
  Title
Functional analysis of genes for biosynthesis of pyocyanin and phenazine-1-carboxamide from Pseudomonas aeruginosa PAO1.
  Journal
J Bacteriol 183:6454-65 (2001)
DOI:10.1128/JB.183.21.6454-6465.2001
  Sequence
Reference
2  [PMID:12741825]
  Authors
Parsons JF, Calabrese K, Eisenstein E, Ladner JE
  Title
Structure and mechanism of Pseudomonas aeruginosa PhzD, an isochorismatase from the phenazine biosynthetic pathway.
  Journal
Biochemistry 42:5684-93 (2003)
DOI:10.1021/bi027385d
  Sequence
[pae:PA1902]
Other DBs
ExplorEnz - The Enzyme Database: 3.3.2.15
IUBMB Enzyme Nomenclature: 3.3.2.15
ExPASy - ENZYME nomenclature database: 3.3.2.15
BRENDA, the Enzyme Database: 3.3.2.15

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