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_2941
MTC: MT3011
MRA: MRA_2967(fadD28)
MTF: TBFG_12955
MTB: TBMG_01031
MTK: TBSG_01039
MTZ: TBXG_001019
MTG: MRGA327_18075
MTE: CCDC5079_2701
MTUR: CFBS_3099(fadD28)
MTL: CCDC5180_2665
MTO: MTCTRI2_2998(fadD28)
MTD: UDA_2941(fadD28)
MTN: ERDMAN_3223(fadD28)
MTJ: J112_15740
MTUB: MT7199_2975
MTUC: J113_20455
MTUE: J114_15705
MTX: M943_15165
MTUH: I917_20620
MTUL: TBHG_02871
MTUT: HKBT1_3087(fadD28)
MTUU: HKBT2_3092(fadD28)
MTQ: HKBS1_3094(fadD28)
MBO: BQ2027_MB2966(fadD28)
MBB: BCG_2963(fadD28)
MBT: JTY_2958(fadD28)
MBM: BCGMEX_2958(fadD28)
MBK: K60_030460
MBX: BCGT_2779
MAF: MAF_29460(fadD28)
MMIC: RN08_3241
MCE: MCAN_29631(fadD28)
MCQ: BN44_60418(fadD)
MCV: BN43_40650(fadD)
MCX: BN42_40940(fadD)
MCZ: BN45_51353(fadD)
MORY: MO_003073(fadD28)
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
MCHI: AN480_11955
MIR: OCQ_22290
MMAL: CKJ54_10740
MMAN: MMAN_15980(fadD28)
MUL: MUL_1432(fadD28_1) MUL_2008(fadD28)
MMI: MMAR_1765(fadD28)
MMAE: MMARE11_16840(fadD28)
MLI: MULP_01920(fadD28)
MPSE: MPSD_13330 MPSD_40710(fadD28)
MSHO: MSHO_54770(fadD28)
MMM: W7S_11460
MKN: MKAN_23975
MYV: G155_04700
MYE: AB431_22340
MHAD: B586_03325
MSHG: MSG_02209(fadD28)
MSAK: MSAS_29300(fadD28)
MXE: MYXE_02300(fadD28)
MNV: MNVI_16080(fadD28)
MPAG: C0J29_10265
MGOR: H0P51_16750
MCOO: MCOO_24850(fadD28)
MBAI: MB901379_01581
MGAU: MGALJ_24050 MGALJ_58710(fadD28)
MLJ: MLAC_28790(fadD28)
MBRD: MBRA_32650(fadD28)
MSHJ: MSHI_07260(fadD28)
MSPG: F6B93_07115
MOT: LTS72_16025(fadD28)
MLM: MLPF_0167(fadD28)
MPAA: MKK62_13605
MMEH: M5I08_12855
MWU: PT015_04235
MFT: XA26_09010
MPHL: MPHLCCUG_00987
MLL: B1R94_07755
MHAS: MHAS_03481
MDU: MDUV_05800
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)
MFG: K6L26_05725
MFLV: NCTC10271_00785 NCTC10271_00787(fadD28)
MCEE: MCEL_41140(fadD28)
MGO: AFA91_26160
MSEN: K3U95_25105
 » 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
[mbo:BQ2027_MB2966]
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

  All links  
Gene (108)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (107)   
Protein sequence (8)   
   UniProt (4)   
   SWISS-PROT (4)   
DNA sequence (2)   
   GenBank (1)   
   EMBL (1)   
Protein domain (5)   
   InterPro (5)   
All databases (123)   

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