KEGG   ENZYME: 6.2.1.49
Entry
EC 6.2.1.49                 Enzyme                                 

Name
long-chain fatty acid adenylyltransferase FadD28;
fadD28 (gene name)
Class
Ligases;
Forming carbon-sulfur bonds;
Acid-thiol ligases
Sysname
long-chain fatty acid:holo-[mycocerosate synthase] ligase (AMP-forming)
Reaction(IUBMB)
ATP + a long-chain fatty acid + holo-[mycocerosate synthase] = AMP + diphosphate + a long-chain acyl-[mycocerosate synthase] (overall reaction);
(1a) ATP + a long-chain fatty acid = diphosphate + a long-chain acyl-adenylate ester;
(1b) a long-chain acyl-adenylate ester + holo-[mycocerosate synthase] = AMP + a long-chain acyl-[mycocerosate synthase]
Substrate
ATP [CPD:C00002];
long-chain fatty acid [CPD:C00638];
holo-[mycocerosate synthase];
long-chain acyl-adenylate ester
Product
AMP [CPD:C00020];
diphosphate [CPD:C00013];
long-chain acyl-[mycocerosate synthase];
long-chain acyl-adenylate ester
Comment
The enzyme, found in certain mycobacteria, activates long-chain fatty acids by adenylation and transfers them to EC 2.3.1.111, mycocerosate synthase. The enzyme participates in the biosynthesis of the virulent lipids dimycocerosates (DIM) and dimycocerosyl triglycosyl phenolphthiocerol (PGL).
History
EC 6.2.1.49 created 2016 as EC 2.7.7.95, transferred 2017 to EC 6.2.1.49
Orthology
K12427  long-chain fatty acid adenylyltransferase FadD28
Genes
MTU: Rv2941(fadD28)
MTV: RVBD_1521 RVBD_1529 RVBD_2941
MTC: MT3011
MRA: MRA_1533(fadD25) MRA_1541(fadD24) MRA_2967(fadD28)
MTF: TBFG_11554 TBFG_11562 TBFG_12955
MTB: TBMG_01031 TBMG_02448 TBMG_02456
MTK: TBSG_01039 TBSG_02460 TBSG_02468
MTZ: TBXG_001019 TBXG_002429 TBXG_002437
MTG: MRGA327_09540 MRGA327_09595 MRGA327_18075
MTI: MRGA423_09540 MRGA423_09585
MTUR: CFBS_1622(fadD25) CFBS_1630(fadD24) CFBS_3099(fadD28)
MTO: MTCTRI2_1564(fadD25) MTCTRI2_1572(fadD24) MTCTRI2_2998(fadD28)
MTD: UDA_1521(fadD25) UDA_1529(fadD24) UDA_2941(fadD28)
MTN: ERDMAN_1696(fadD25) ERDMAN_1705(fadD24) ERDMAN_3223(fadD28)
MTUT: HKBT1_1622(fadD25) HKBT1_1630(fadD24) HKBT1_3087(fadD28)
MTUU: HKBT2_1629(fadD25) HKBT2_1637(fadD24) HKBT2_3092(fadD28)
MTQ: HKBS1_1626(fadD25) HKBS1_1634(fadD24) HKBS1_3094(fadD28)
MBO: BQ2027_MB1548(fadD25) BQ2027_MB1556(fadD24) BQ2027_MB2966(fadD28)
MBB: BCG_2963(fadD28)
MBT: JTY_1548(fadD25) JTY_1556(fadD24) JTY_2958(fadD28)
MBM: BCGMEX_1545(fadD25) BCGMEX_1553(fadD24) BCGMEX_2958(fadD28)
MAF: MAF_15480(fadD25) MAF_15560(fadD24) MAF_29460(fadD28)
MCE: MCAN_15421(fadD25) MCAN_15521(fadD24) MCAN_29631(fadD28)
MCQ: BN44_20085(fadD) BN44_20093(fadD) BN44_60418(fadD)
MCV: BN43_30642(fadD) BN43_30655(fadD) BN43_40650(fadD)
MCX: BN42_21451(fadD) BN42_21460(fadD) BN42_40940(fadD)
MCZ: BN45_30628(fadD) BN45_40004(fadD) BN45_51353(fadD)
MLE: ML0138(fadD28)
MLB: MLBr00138(fadD28)
MPA: MAP_3752(fadD28)
MAO: MAP4_0017
MAVI: RC58_00085
MAVU: RE97_00085
MIT: OCO_23760
MIA: OCU_23640
MID: MIP_03280
MYO: OEM_22180
MIR: OCQ_22290
MMAN: MMAN_15980(fadD28)
MUL: MUL_1432(fadD28_1) MUL_2008(fadD28)
MMI: MMAR_1765(fadD28) MMAR_2341(fadD25)
MMAE: MMARE11_16840(fadD28) MMARE11_22630(fadD25)
MMM: W7S_11460
MLI: MULP_01920(fadD28)
MSHG: MSG_02209(fadD28)
MSAK: MSAS_03050 MSAS_29300(fadD28)
MXE: MYXE_02300(fadD28)
MNV: MNVI_16080(fadD28)
MCOO: MCOO_24850(fadD28)
MPSE: MPSD_13330 MPSD_40710(fadD28)
MSHO: MSHO_54770(fadD28)
MGAU: MGALJ_24050 MGALJ_58710(fadD28)
MLJ: MLAC_13800(fadD25) MLAC_14030(fadD24) MLAC_28790(fadD28)
MBRD: MBRA_32650(fadD28)
MSHJ: MSHI_07260(fadD28) MSHI_16700(fadD24)
MHAS: MHAS_03481
MCHT: MCHIJ_19900(fadD24)
MAUU: NCTC10437_02878(fadD28)
MMAG: MMAD_24270(fadD28)
MAIC: MAIC_39590(fadD28)
MALV: MALV_42820(fadD28)
MTY: MTOK_49720(fadD28)
MGAD: MGAD_24310(fadD28)
MHEV: MHEL_06730(fadD28)
MSAR: MSAR_29630(fadD28)
MANY: MANY_23040(fadD28)
MBOK: MBOE_03930(fadD28_1)
 » show all
Reference
1  [PMID:9098059]
  Authors
Fitzmaurice AM, Kolattukudy PE
  Title
Open reading frame 3, which is adjacent to the mycocerosic acid synthase gene, is expressed as an acyl coenzyme A synthase in Mycobacterium bovis BCG.
  Journal
J Bacteriol 179:2608-15 (1997)
DOI:10.1128/JB.179.8.2608-2615.1997
  Sequence
Reference
2  [PMID:16582482]
  Authors
Goyal A, Yousuf M, Rajakumara E, Arora P, Gokhale RS, Sankaranarayanan R
  Title
Crystallization and preliminary X-ray crystallographic studies of the N-terminal  domain of FadD28, a fatty-acyl AMP ligase from Mycobacterium tuberculosis.
  Journal
Acta Crystallogr Sect F Struct Biol Cryst Commun 62:350-2 (2006)
DOI:10.1107/S1744309106005938
  Sequence
[mtu:Rv2941]
Reference
3  [PMID:19182784]
  Authors
Arora P, Goyal A, Natarajan VT, Rajakumara E, Verma P, Gupta R, Yousuf M, Trivedi OA, Mohanty D, Tyagi A, Sankaranarayanan R, Gokhale RS
  Title
Mechanistic and functional insights into fatty acid activation in Mycobacterium tuberculosis.
  Journal
Nat Chem Biol 5:166-73 (2009)
DOI:10.1038/nchembio.143
  Sequence
[mtu:Rv2941]
Reference
4  [PMID:24831705]
  Authors
Menendez-Bravo S, Comba S, Sabatini M, Arabolaza A, Gramajo H
  Title
Expanding the chemical diversity of natural esters by engineering a polyketide-derived pathway into Escherichia coli.
  Journal
Metab Eng 24:97-106 (2014)
DOI:10.1016/j.ymben.2014.05.002
  Sequence
[mtu:Rv2941]
Reference
5  [PMID:25561717]
  Authors
Vergnolle O, Chavadi SS, Edupuganti UR, Mohandas P, Chan C, Zeng J, Kopylov M, Angelo NG, Warren JD, Soll CE, Quadri LE
  Title
Biosynthesis of cell envelope-associated phenolic glycolipids in Mycobacterium marinum.
  Journal
J Bacteriol 197:1040-50 (2015)
DOI:10.1128/JB.02546-14
  Sequence
[mmi:MMAR_1765]
Other DBs
ExplorEnz - The Enzyme Database: 6.2.1.49
IUBMB Enzyme Nomenclature: 6.2.1.49
ExPASy - ENZYME nomenclature database: 6.2.1.49
BRENDA, the Enzyme Database: 6.2.1.49

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