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) [RN:R12575];
(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] [RN:R12577]
Reaction(KEGG)
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
GKDK6Q96_02925
MAQMaqu_3524
MHCMARHY3424
MARJMARI_31200(menE_2)
MALLPBN92_17845
MSHEMAALD49_35060
AMACMASE_09720
AMGAMEC673_09965
ASPAOR13_248
ASQAVL57_17230
AAWAVL56_16115
ALEAV939_16170
ALZAV940_15925
CATEC2869_06590
HMIsoil367_15780
CATTOLW01_08295
CELLCBR65_18740
GILNHM04_07030
MKEOOT55_16125
STAWNCG89_14200
MIIBTJ40_19050
OAIOLEAN_C24210
BACZKFF03_16070
OMEOLMES_0537
OCEGU3_03570
AAKAA2016_0178
AMIHCO731_00651(fadD_1)
AMISAmn_05660
ANJAMD1_0673(fadD)
SFHSFHH103_01318
EADOV14_a1319
EAHFA04_19980
ECAAJ3R84_21200
ENPJVX98_04515
AVQHRR99_17400
RPATX73_012335
RPBRPB_4394
RPTRpal_2630
RPXRpdx1_3183
NWINwi_2300
CMETK6K41_17350
AUAM673_21065
PGAPGA1_78p00430
PGLPGA2_95p520
PGDGal_04240
LMDMETH_16725
ALIAZOLI_p20606
AZMDM194_19470
SKTIGS68_11030
SMUCJL100_015625
SROEJL101_010045
BANBA_1983(asbC)
BARGBAA_1983(asbC)
BATBAS1840
BAHBAMEG_2607 BAMEG_2608(asbC)
BAIBAA_2051(asbC)
BAXH9401_1880
BANTA16_20200
BANRA16R_20440
BANSBAPAT_1896
BANHHYU01_09935
BANVDJ46_788
BCEBC1980
BCZBCE33L1797
BCBBCB4264_A1985(asbC)
BCUBCAH820_2018(asbC)
BCGBCG9842_B3344(asbC)
BCXBCA_2045(asbC)
BALBACI_c19570
BCFbcf_09760
BTKBT9727_1814
BTLBALH_1755
BTBBMB171_C1767(asbC)
BTTHD73_2149
BTHRYBT1520_10720
BTHIBTK_10860
BTCCT43_CH1936(asbC)
BTMMC28_1186
BTGBTB_c20500(asbC)
BTIBTG_10045
BTNBTF1_07290
BTHTH175_ch1962
BTHUYBT1518_11030
BTWBF38_3197
BTHYAQ980_20255
BWEBcerKBAB4_1846
BWWbwei_3033(asbC)
BMYOBG05_4003
BTYBtoyo_4554
BBYCY96_08995
BWDCT694_10810
BTROFJR70_09680(asbC)
BMOBMLA2C4_10085
BNTGSN03_09685(asbC)
BALUQRY64_12030(asbC)
BWHA9C19_17990
BARDQRY57_11170
BHKB4U37_11085
BCLABC1949
BLEBleG1_1612
SHUAPQ477_16910
BPFBpOF4_08935(asbC)
BONA361_02375
CFIRNAF01_02370
CPSSM5V91_19810
LSPBsph_2961
LFUHR49_11805
LLBR6U77_05295
MLITKDJ21_008470
MENLMVE64_10285
MEBZLPC09_22170
ECTOMUG87_15620
ALKLMM271_23435
EXMU719_06045
EXUESP131_08440
EACEKKI46_06235
BBEBBR47_20470
BLRBRLA_c008690
BFMBP422_05350
BRWGOP56_20345
PMSKNP414_07054
PMQPM3016_6643
PMWB2K_33565
PTRIKDC22_17570
PALRHGI30_15375 HGI30_17890
CCHLFPL14_04890 FPL14_24320
SOBCSE16_06620
 » 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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