KEGG   ORTHOLOGY: K19546Help
Entry
K19546                      KO                                     

Name
bacA
Definition
prephenate decarboxylase [EC:4.1.1.100]
Pathway
ko00998  Biosynthesis of various secondary metabolites - part 2
ko01100  Metabolic pathways
ko01130  Biosynthesis of antibiotics
Module
M00787  Bacilysin biosynthesis, prephenate => bacilysin
Brite
KEGG Orthology (KO) [BR:ko00001]
 09100 Metabolism
  09110 Biosynthesis of other secondary metabolites
   00998 Biosynthesis of various secondary metabolites - part 2
    K19546  bacA; prephenate decarboxylase
Enzymes [BR:ko01000]
 4. Lyases
  4.1  Carbon-carbon lyases
   4.1.1  Carboxy-lyases
    4.1.1.100  prephenate decarboxylase
     K19546  bacA; prephenate decarboxylase
BRITE hierarchy
Other DBs
RN: R10934
COG: COG0077
Genes
DAQ: DAQ1742_03406(bacA)
DIC: Dpoa569_001039
PGZ: C2E15_12625
PLUM: A4R40_15200
VGA: BSQ33_21065
MYA: MORIYA_1930
LPA: lpa_03409
RAC: RA876_04040
CMED: FE773_03760
MBD: MEBOL_005605
BSU: BSU37740(bacA)
BSR: I33_3922
BSL: A7A1_0193
BSH: BSU6051_37740(bacA)
BSUT: BSUB_04010(bacA)
BSUL: BSUA_04010(bacA)
BSUS: Q433_20785
BSS: BSUW23_18640(bacA)
BST: GYO_4160
BSQ: B657_37740(bacA)
BSX: C663_3679(bacA)
BAQ: BACAU_3522(bacA)
BYA: BANAU_3675(bacA)
BAMP: B938_17925(bacA)
BAML: BAM5036_3423(bacA)
BAMA: RBAU_3631(bacA)
BAMN: BASU_3407(bacA)
BAMB: BAPNAU_3689(bacA)
BAMT: AJ82_19710
BAMY: V529_37650(bacA)
BAO: BAMF_3607(bacA)
BAZ: BAMTA208_19100(bacA)
BQL: LL3_03918(bacA)
BXH: BAXH7_03910(bacA)
BQY: MUS_4152(bacA)
BAMI: KSO_001595
BAMC: U471_36380
BAMF: U722_18660
BPU: BPUM_3420
BPUM: BW16_18160
BPUS: UP12_17605
BJS: MY9_3866
BACW: QR42_17160
BACP: SB24_11230
BACB: OY17_01130
BACY: QF06_17310
BACL: BS34A_40920(bacA)
BALM: BsLM_3804
STRM: M444_35590
SRO: Sros_3665
MAR: MAE_56560
MPK: VL20_295
PAGH: NIES204_06210(aerD)
NSP: BMF81_03788(bacA_2)
 » show all
TaxonomyKoalaUniProt
Reference
  Authors
Mahlstedt SA, Walsh CT
  Title
Investigation of anticapsin biosynthesis reveals a four-enzyme pathway to tetrahydrotyrosine in Bacillus subtilis.
  Journal
Biochemistry 49:912-23 (2010)
DOI:10.1021/bi9021186
  Sequence
[bsu:BSU37740]
Reference
  Authors
Ozcengiz G, Ogulur I
  Title
Biochemistry, genetics and regulation of bacilysin biosynthesis and its significance more than an antibiotic.
  Journal
N Biotechnol 32:612-9 (2015)
DOI:10.1016/j.nbt.2015.01.006

KEGG   ENZYME: 4.1.1.100Help
Entry
EC 4.1.1.100                Enzyme                                 

Name
prephenate decarboxylase;
BacA;
AerD;
SalX;
non-aromatizing prephenate decarboxylase
Class
Lyases;
Carbon-carbon lyases;
Carboxy-lyases
BRITE hierarchy
Sysname
prephenate carboxy-lyase (3-[(4R)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate-forming)
Reaction(IUBMB)
prephenate = 3-[(4R)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate + CO2 [RN:R10934]
Reaction(KEGG)
Substrate
prephenate [CPD:C00254]
Product
3-[(4R)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate [CPD:C20953];
CO2 [CPD:C00011]
Comment
The enzyme, characterized from the bacterium Bacillus subtilis, is involved in the biosynthesis of the nonribosomally synthesized dipeptide antibiotic bacilysin, composed of L-alanine and L-anticapsin. The enzyme isomerizes only the pro-R double bond in prephenate.
History
EC 4.1.1.100 created 2015
Pathway
ec00998  Biosynthesis of various secondary metabolites - part 2
ec01100  Metabolic pathways
ec01130  Biosynthesis of antibiotics
Orthology
K19546  prephenate decarboxylase
Genes
DAQ: DAQ1742_03406(bacA)
DIC: Dpoa569_001039
PGZ: C2E15_12625
PLUM: A4R40_15200
VGA: BSQ33_21065
MYA: MORIYA_1930
LPA: lpa_03409
RAC: RA876_04040
CMED: FE773_03760
MBD: MEBOL_005605
BSU: BSU37740(bacA)
BSR: I33_3922
BSL: A7A1_0193
BSH: BSU6051_37740(bacA)
BSUT: BSUB_04010(bacA)
BSUL: BSUA_04010(bacA)
BSUS: Q433_20785
BSS: BSUW23_18640(bacA)
BST: GYO_4160
BSQ: B657_37740(bacA)
BSX: C663_3679(bacA)
BAQ: BACAU_3522(bacA)
BYA: BANAU_3675(bacA)
BAMP: B938_17925(bacA)
BAML: BAM5036_3423(bacA)
BAMA: RBAU_3631(bacA)
BAMN: BASU_3407(bacA)
BAMB: BAPNAU_3689(bacA)
BAMT: AJ82_19710
BAMY: V529_37650(bacA)
BAO: BAMF_3607(bacA)
BAZ: BAMTA208_19100(bacA)
BQL: LL3_03918(bacA)
BXH: BAXH7_03910(bacA)
BQY: MUS_4152(bacA)
BAMI: KSO_001595
BAMC: U471_36380
BAMF: U722_18660
BPU: BPUM_3420
BPUM: BW16_18160
BPUS: UP12_17605
BJS: MY9_3866
BACW: QR42_17160
BACP: SB24_11230
BACB: OY17_01130
BACY: QF06_17310
BACL: BS34A_40920(bacA)
BALM: BsLM_3804
STRM: M444_35590
SRO: Sros_3665
MAR: MAE_56560
MPK: VL20_295
PAGH: NIES204_06210(aerD)
NSP: BMF81_03788(bacA_2)
 » show all
Taxonomy
Reference
1  [PMID:20052993]
  Authors
Mahlstedt SA, Walsh CT
  Title
Investigation of anticapsin biosynthesis reveals a four-enzyme pathway to tetrahydrotyrosine in Bacillus subtilis.
  Journal
Biochemistry 49:912-23 (2010)
DOI:10.1021/bi9021186
Reference
2  [PMID:20863139]
  Authors
Mahlstedt S, Fielding EN, Moore BS, Walsh CT
  Title
Prephenate decarboxylases: a new prephenate-utilizing enzyme family that performs nonaromatizing decarboxylation en route to diverse secondary metabolites.
  Journal
Biochemistry 49:9021-3 (2010)
DOI:10.1021/bi101457h
Reference
3  [PMID:22483065]
  Authors
Parker JB, Walsh CT
  Title
Olefin isomerization regiochemistries during tandem action of BacA and BacB on prephenate in bacilysin biosynthesis.
  Journal
Biochemistry 51:3241-51 (2012)
DOI:10.1021/bi300254u
Other DBs
ExplorEnz - The Enzyme Database: 4.1.1.100
IUBMB Enzyme Nomenclature: 4.1.1.100
ExPASy - ENZYME nomenclature database: 4.1.1.100
BRENDA, the Enzyme Database: 4.1.1.100

KEGG   REACTION: R10934Help
Entry
R10934                      Reaction                               

Name
prephenate carboxy-lyase (3-[(4R)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate-forming)
Definition
Prephenate <=> 3-[(4R)-4-Hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate + CO2
Equation
Reaction class
RC03316  C00254_C20953
Enzyme
Pathway
rn00998  Biosynthesis of various secondary metabolites - part 2
rn01100  Metabolic pathways
rn01130  Biosynthesis of antibiotics
Module
M00787  Bacilysin biosynthesis, prephenate => bacilysin
Orthology
K19546  prephenate decarboxylase [EC:4.1.1.100]
Other DBs
RHEA: 33502

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