KEGG   ENZYME: 6.2.1.62
Entry
EC 6.2.1.62                 Enzyme                                 

Name
3,4-dihydroxybenzoate---[aryl-carrier protein] ligase;
asbC (gene name)
Class
Ligases;
Forming carbon-sulfur bonds;
Acid-thiol ligases
Sysname
3,4-dihydroxybenzoate:[aryl-carrier protein] ligase (AMP-forming)
Reaction(IUBMB)
ATP + 3,4-dihydroxybenzoate + holo-[aryl-carrier protein] = AMP + diphosphate + 3,4-dihydroxybenzoyl-[aryl-carrier protein] (overall reaction);
(1a) ATP + 3,4-dihydroxybenzoate = diphosphate + (3,4-dihydroxybenzoyl)adenylate [RN:R12576];
(1b) (3,4-dihydroxybenzoyl)adenylate + holo-[aryl-carrier protein] = AMP + 3,4-dihydroxybenzoyl-[aryl-carrier protein]
Reaction(KEGG)
R12576;
(other) R12575 R12577
Substrate
ATP [CPD:C00002];
3,4-dihydroxybenzoate [CPD:C00230];
holo-[aryl-carrier protein] [CPD:C20665];
(3,4-dihydroxybenzoyl)adenylate [CPD:C20884]
Product
AMP [CPD:C00020];
diphosphate [CPD:C00013];
3,4-dihydroxybenzoyl-[aryl-carrier protein] [CPD:C20883];
(3,4-dihydroxybenzoyl)adenylate [CPD:C20884]
Comment
The adenylation domain of the enzyme catalyses the activation of 3,4-dihydroxybenzoate to (3,4-dihydroxybenzoyl)adenylate, followed by the transfer of the activated compound to the free thiol of a phosphopantetheine arm of an aryl-carrier protein domain. The aryl-carrier protein domain may be part of the same protein, or of a different protein. This activity is often found as part of a larger non-ribosomal peptide synthase.
History
EC 6.2.1.62 created 2020
Pathway
ec01053  Biosynthesis of siderophore group nonribosomal peptides
Orthology
K24110  3,4-dihydroxybenzoate---[aryl-carrier protein] ligase
Genes
MAQ: Maqu_3524
MHC: MARHY3424
MARJ: MARI_31200(menE_2)
AMAC: MASE_09720
AMG: AMEC673_09965
ASP: AOR13_248
ASQ: AVL57_17230
AAW: AVL56_16115
ALE: AV939_16170
ALZ: AV940_15925
AMIH: CO731_00651(fadD_1)
RPA: RPA2388
RPB: RPB_4394
RPT: Rpal_2630
NWI: Nwi_2300
PGD: Gal_04240
BAN: BA_1983(asbC)
BAR: GBAA_1983(asbC)
BAT: BAS1840
BAI: BAA_2051(asbC)
BANT: A16_20200
BANR: A16R_20440
BANS: BAPAT_1896
BANV: DJ46_788
BCE: BC1980
BCB: BCB4264_A1985(asbC)
BCU: BCAH820_2018(asbC)
BCG: BCG9842_B3344(asbC)
BCX: BCA_2045(asbC)
BCF: bcf_09760
BTL: BALH_1755
BTB: BMB171_C1767(asbC)
BTT: HD73_2149
BTHI: BTK_10860
BTC: CT43_CH1936(asbC)
BTM: MC28_1186
BTG: BTB_c20500(asbC)
BTI: BTG_10045
BTW: BF38_3197
BWW: bwei_3033(asbC)
BMYO: BG05_4003
BTRO: FJR70_09680(asbC)
BCL: ABC1949
BPF: BpOF4_08935(asbC)
LSP: Bsph_2961
PMW: B2K_33565
 » show all
Reference
1  [PMID:17346033]
  Authors
Pfleger BF, Lee JY, Somu RV, Aldrich CC, Hanna PC, Sherman DH
  Title
Characterization and analysis of early enzymes for petrobactin biosynthesis in Bacillus anthracis.
  Journal
Biochemistry 46:4147-57 (2007)
DOI:10.1021/bi6023995
  Sequence
[ban:BA_1983]
Other DBs
ExplorEnz - The Enzyme Database: 6.2.1.62
IUBMB Enzyme Nomenclature: 6.2.1.62
ExPASy - ENZYME nomenclature database: 6.2.1.62
BRENDA, the Enzyme Database: 6.2.1.62

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