KEGG   ORTHOLOGY: K09483Help
Entry
K09483                      KO                                     

Name
quiC
Definition
3-dehydroshikimate dehydratase [EC:4.2.1.118]
Pathway
ko00400  Phenylalanine, tyrosine and tryptophan biosynthesis
ko01100  Metabolic pathways
ko01110  Biosynthesis of secondary metabolites
ko01130  Biosynthesis of antibiotics
Brite
KEGG Orthology (KO) [BR:ko00001]
 09100 Metabolism
  09105 Amino acid metabolism
   00400 Phenylalanine, tyrosine and tryptophan biosynthesis
    K09483  quiC; 3-dehydroshikimate dehydratase
Enzymes [BR:ko01000]
 4. Lyases
  4.2  Carbon-oxygen lyases
   4.2.1  Hydro-lyases
    4.2.1.118  3-dehydroshikimate dehydratase
     K09483  quiC; 3-dehydroshikimate dehydratase
BRITE hierarchy
Other DBs
RN: R01627
GO: 0046565
Genes
PAO: Pat9b_2424
TCI: A7K98_19065
XSA: SB85_14665
SLM: BIZ42_17435
STEM: CLM74_09120
PPG: PputGB1_4069
PPW: PputW619_3862
PPUT: L483_24900
PPUN: PP4_12570(quiC)
PSV: PVLB_18200
ACB: A1S_1882
ABM: ABSDF2013(quiC)
ABY: ABAYE1683(quiC)
ABN: AB57_2216
ABX: ABK1_2460
ABH: M3Q_2340
ABAD: ABD1_19030(quiC)
ABAZ: P795_7620
ABAU: IX87_20870
ABAA: IX88_11585
ACC: BDGL_001361(quiC)
ACI: ACIAD1714(quiC)
AMIM: MIM_c35790(quiC)
 » show all
TaxonomyKoalaUniProt
Reference
PMID:7592351
  Authors
Elsemore DA, Ornston LN
  Title
Unusual ancestry of dehydratases associated with quinate catabolism in Acinetobacter calcoaceticus.
  Journal
J Bacteriol 177:5971-8 (1995)
DOI:10.1128/JB.177.20.5971-5978.1995
  Sequence
[aci:ACIAD1714]

KEGG   ORTHOLOGY: K15652Help
Entry
K15652                      KO                                     

Name
asbF
Definition
3-dehydroshikimate dehydratase [EC:4.2.1.118]
Pathway
ko00400  Phenylalanine, tyrosine and tryptophan biosynthesis
ko01100  Metabolic pathways
ko01110  Biosynthesis of secondary metabolites
ko01130  Biosynthesis of antibiotics
Brite
KEGG Orthology (KO) [BR:ko00001]
 09100 Metabolism
  09105 Amino acid metabolism
   00400 Phenylalanine, tyrosine and tryptophan biosynthesis
    K15652  asbF; 3-dehydroshikimate dehydratase
Enzymes [BR:ko01000]
 4. Lyases
  4.2  Carbon-oxygen lyases
   4.2.1  Hydro-lyases
    4.2.1.118  3-dehydroshikimate dehydratase
     K15652  asbF; 3-dehydroshikimate dehydratase
BRITE hierarchy
Other DBs
RN: R01627
GO: 0046565
Genes
MAQ: Maqu_3527
MHC: MARHY3427
MARJ: MARI_31170(asbF)
AMAC: MASE_09730
AMG: AMEC673_09975
ASP: AOR13_246
ASQ: AVL57_17240
AAW: AVL56_16125
ALE: AV939_16180
ALZ: AV940_15935
OCE: GU3_03580
AMIH: CO731_00653(asbF)
RPA: RPA2386
RPT: Rpal_2628
NWI: Nwi_2298
MEX: Mext_3763
MDI: METDI4727
MCH: Mchl_4058
MPO: Mpop_4019
META: Y590_18690
PGD: Gal_04238
BYA: BANAU_0281(asbF)
BAMP: B938_01450
BAMA: RBAU_0311
BAMN: BASU_0295
BAMB: BAPNAU_0280(frlC1)
BAMT: AJ82_01860
BAMY: V529_03020
BMP: NG74_00319(asbF)
BAO: BAMF_0287(RBAM_003390)
BQL: LL3_00296(prot)
BQY: MUS_0297
BAMI: KSO_017965
BAMC: U471_02990
BAMF: U722_01745
BAN: BA_1986(asbF)
BAR: GBAA_1986(asbF)
BAT: BAS1843
BAH: BAMEG_2604(asbF)
BAI: BAA_2054(asbF)
BANT: A16_20230
BANR: A16R_20480
BANS: BAPAT_1899
BANV: DJ46_791(asbF)
BCE: BC1983
BCB: BCB4264_A1988(asbF)
BCU: BCAH820_2021(asbF)
BCG: BCG9842_B3341(asbF)
BCX: BCA_2048(asbF)
BCF: bcf_09775
BTL: BALH_1758
BTB: BMB171_C1770(asbF)
BTT: HD73_2152
BTHI: BTK_10875
BTC: CT43_CH1939(asbF)
BTM: MC28_1189(asbF)
BTG: BTB_c20530(asbF)
BTI: BTG_10030
BTW: BF38_3200(asbF)
BWW: bwei_3030(asbF)
BMYO: BG05_4000(asbF)
BCL: ABC1952
BPF: BpOF4_08950(asbF)
BACP: SB24_08110
BACB: OY17_04360
LSP: Bsph_2958
PMS: KNP414_07050(asbF)
PMW: B2K_33545
PSWU: SY83_22190
AAC: Aaci_2516
AAD: TC41_2813
LMOI: VV02_16645
 » show all
TaxonomyKoalaUniProt
Reference
  Authors
Pfleger BF, Kim Y, Nusca TD, Maltseva N, Lee JY, Rath CM, Scaglione JB, Janes BK, Anderson EC, Bergman NH, Hanna PC, Joachimiak A, Sherman DH
  Title
Structural and functional analysis of AsbF: origin of the stealth 3,4-dihydroxybenzoic acid subunit for petrobactin biosynthesis.
  Journal
Proc Natl Acad Sci U S A 105:17133-8 (2008)
DOI:10.1073/pnas.0808118105

KEGG   ENZYME: 4.2.1.118Help
Entry
EC 4.2.1.118                Enzyme                                 

Name
3-dehydroshikimate dehydratase
Class
Lyases;
Carbon-oxygen lyases;
Hydro-lyases
BRITE hierarchy
Sysname
3-dehydroshikimate hydro-lyase
Reaction(IUBMB)
3-dehydro-shikimate = 3,4-dihydroxybenzoate + H2O [RN:R01627]
Reaction(KEGG)
Substrate
3-dehydro-shikimate
Product
3,4-dihydroxybenzoate [CPD:C00230];
H2O [CPD:C00001]
Comment
Catalyses an early step in the biosynthesis of petrobactin, a siderophore produced by many bacteria, including the human pathogen Bacillus anthracis. Requires divalent ions, with a preference for Mn2+.
History
EC 4.2.1.118 created 2009
Pathway
ec00400  Phenylalanine, tyrosine and tryptophan biosynthesis
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
ec01130  Biosynthesis of antibiotics
Orthology
K09483  3-dehydroshikimate dehydratase
K15652  3-dehydroshikimate dehydratase
Genes
PAO: Pat9b_2424
TCI: A7K98_19065
XSA: SB85_14665
SLM: BIZ42_17435
STEM: CLM74_09120
PPG: PputGB1_4069
PPW: PputW619_3862
PPUT: L483_24900
PPUN: PP4_12570(quiC)
PSV: PVLB_18200
ACB: A1S_1882
ABM: ABSDF2013(quiC)
ABY: ABAYE1683(quiC)
ABN: AB57_2216
ABX: ABK1_2460
ABH: M3Q_2340
ABAD: ABD1_19030(quiC)
ABAZ: P795_7620
ABAU: IX87_20870
ABAA: IX88_11585
ACC: BDGL_001361(quiC)
ACI: ACIAD1714(quiC)
MAQ: Maqu_3527
MHC: MARHY3427
MARJ: MARI_31170(asbF)
AMAC: MASE_09730
ASP: AOR13_246
OCE: GU3_03580
AMIM: MIM_c35790(quiC)
AMIH: CO731_00653(asbF)
RPA: RPA2386
RPT: Rpal_2628
NWI: Nwi_2298
MEX: Mext_3763
MDI: METDI4727
MCH: Mchl_4058
MPO: Mpop_4019
META: Y590_18690
PGD: Gal_04238
BYA: BANAU_0281(asbF)
BAMP: B938_01450
BAMA: RBAU_0311
BAMN: BASU_0295
BAMB: BAPNAU_0280(frlC1)
BAMT: AJ82_01860
BAMY: V529_03020
BMP: NG74_00319(asbF)
BAO: BAMF_0287(RBAM_003390)
BQL: LL3_00296(prot)
BQY: MUS_0297
BAMI: KSO_017965
BAMC: U471_02990
BAMF: U722_01745
BAN: BA_1986(asbF)
BAR: GBAA_1986(asbF)
BAT: BAS1843
BAH: BAMEG_2604(asbF)
BAI: BAA_2054(asbF)
BANT: A16_20230
BANR: A16R_20480
BANS: BAPAT_1899
BANV: DJ46_791(asbF)
BCE: BC1983
BCB: BCB4264_A1988(asbF)
BCU: BCAH820_2021(asbF)
BCG: BCG9842_B3341(asbF)
BCX: BCA_2048(asbF)
BCF: bcf_09775
BTL: BALH_1758
BTB: BMB171_C1770(asbF)
BTT: HD73_2152
BTHI: BTK_10875
BTC: CT43_CH1939(asbF)
BTM: MC28_1189(asbF)
BTG: BTB_c20530(asbF)
BTI: BTG_10030
BTW: BF38_3200(asbF)
BWW: bwei_3030(asbF)
BMYO: BG05_4000(asbF)
BCL: ABC1952
BPF: BpOF4_08950(asbF)
BACP: SB24_08110
BACB: OY17_04360
LSP: Bsph_2958
PMS: KNP414_07050(asbF)
PMW: B2K_33545
PSWU: SY83_22190
AAC: Aaci_2516
AAD: TC41_2813
LMOI: VV02_16645
 » show all
Taxonomy
Reference
1  [PMID:18975921]
  Authors
Fox DT, Hotta K, Kim CY, Koppisch AT
  Title
The missing link in petrobactin biosynthesis: asbF encodes a (-)-3-dehydroshikimate dehydratase.
  Journal
Biochemistry 47:12251-3 (2008)
DOI:10.1021/bi801876q
Reference
2  [PMID:18955706]
  Authors
Pfleger BF, Kim Y, Nusca TD, Maltseva N, Lee JY, Rath CM, Scaglione JB, Janes BK, Anderson EC, Bergman NH, Hanna PC, Joachimiak A, Sherman DH
  Title
Structural and functional analysis of AsbF: origin of the stealth 3,4-dihydroxybenzoic acid subunit for petrobactin biosynthesis.
  Journal
Proc Natl Acad Sci U S A 105:17133-8 (2008)
DOI:10.1073/pnas.0808118105
  Sequence
[ban:BA_1986]
Other DBs
ExplorEnz - The Enzyme Database: 4.2.1.118
IUBMB Enzyme Nomenclature: 4.2.1.118
ExPASy - ENZYME nomenclature database: 4.2.1.118
BRENDA, the Enzyme Database: 4.2.1.118

KEGG   REACTION: R01627Help
Entry
R01627                      Reaction                               

Name
3-dehydroshikimate hydro-lyase
Definition
3-Dehydroshikimate <=> 3,4-Dihydroxybenzoate + H2O
Equation
Reaction class
RC00568  C00230_C02637
Enzyme
Pathway
rn00400  Phenylalanine, tyrosine and tryptophan biosynthesis
rn01100  Metabolic pathways
rn01110  Biosynthesis of secondary metabolites
rn01130  Biosynthesis of antibiotics
Orthology
K09483  3-dehydroshikimate dehydratase [EC:4.2.1.118]
K15652  3-dehydroshikimate dehydratase [EC:4.2.1.118]
Other DBs
RHEA: 24851

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