KEGG   ENZYME: 2.3.1.282
Entry
EC 2.3.1.282                Enzyme                                 
Name
phenolphthiocerol/phthiocerol/phthiodiolone dimycocerosyl transferase;
papA5 (gene name)
Class
Transferases;
Acyltransferases;
Transferring groups other than aminoacyl groups
Sysname
mycocerosyl-[mycocerosic acid synthase]:phenolphthiocerol/phthiocerol/phthiodiolone dimycocerosyl transferase
Reaction(IUBMB)
(1) 2 a mycocerosyl-[mycocerosic acid synthase] + a phthiocerol = a dimycocerosyl phthiocerol + 2 holo-[mycocerosic acid synthase];
(2) 2 a mycocerosyl-[mycocerosic acid synthase] + a phthiodiolone = a dimycocerosyl phthiodiolone + 2 holo-[mycocerosic acid synthase];
(3) 2 a mycocerosyl-[mycocerosic acid synthase] + a phenolphthiocerol = a dimycocerosyl phenolphthiocerol + 2 holo-[mycocerosic acid synthase]
Substrate
a mycocerosyl-[mycocerosic acid synthase];
phthiocerol;
phthiodiolone;
phenolphthiocerol
Product
dimycocerosyl phthiocerol;
holo-[mycocerosic acid synthase];
dimycocerosyl phthiodiolone;
dimycocerosyl phenolphthiocerol
Comment
The enzyme, present in certain pathogenic species of mycobacteria, catalyses the transfer of mycocerosic acids to the two hydroxyl groups at the common lipid core of phthiocerol, phthiodiolone, and phenolphthiocerol, forming dimycocerosate esters. The fatty acid precursors of mycocerosic acids are activated by EC 6.2.1.49, long-chain fatty acid adenylyltransferase FadD28, which loads them onto EC 2.3.1.111, mycocerosate synthase. That enzyme extends the precursors to form mycocerosic acids that remain attached until transferred by EC 2.3.1.282.
History
EC 2.3.1.282 created 2019
Orthology
K23414  phenolphthiocerol/phthiocerol/phthiodiolone dimycocerosyl transferase
Genes
PBRULZC95_19305
MTURv2939(papA5)
MTVRVBD_2939
MTCMT3009
MRAMRA_2965(papA5)
MTFTBFG_12953
MTBTBMG_01033
MTKTBSG_01041
MTZTBXG_001021
MTGMRGA327_18065
MTECCDC5079_2699
MTURCFBS_3097(papA5)
MTLCCDC5180_2663
MTOMTCTRI2_2996(papA5)
MTDUDA_2939(papA5)
MTNERDMAN_3221(papA5)
MTJJ112_15730
MTUBMT7199_2973
MTUCJ113_20430
MTUEJ114_15695
MTXM943_15155
MTULTBHG_02869
MTUTHKBT1_3085(papA5)
MTUUHKBT2_3090(papA5)
MTQHKBS1_3092(papA5)
MBOBQ2027_MB2964(papA5)
MBBBCG_2961(papA5)
MBTJTY_2956(papA5)
MBMBCGMEX_2956(papA5)
MBKK60_030440
MBXBCGT_2777
MAFMAF_29440(papA5)
MMICRN08_3238
MCEMCAN_29611(papA5)
MCQBN44_60416(papA)
MCVBN43_40647(papA)
MCXBN42_40937(papA)
MCZBN45_51351(papA)
MORYMO_003071
MLEML2349
MLBMLBr02349
MSAMycsm_05871
MULMUL_2011(papA5)
MMIMMAR_1768(papA5)
MMAEMMARE11_16880(papA5)
MLIMULP_01924(papA5)
MPSEMPSD_40660(papA5)
MSHOMSHO_54720(papA5)
MMCMmcs_2828
MKMMkms_2872
MJLMjls_2857
MKNMKAN_24000
MHADB586_03535
MDXBTO20_18105
MSHGMSG_01623(papA5)
MFJMFLOJ_16830(papA5)
MSTOMSTO_18420(papA5)
MSIMMSIM_07810(papA5)
MLWMJO58_08790
MPAGC0J29_10290
MNMMNVM_38420(papA5)
MCOOMCOO_18260(papA5)
MBAIMB901379_01585(papA5)
MGAUMGALJ_49450(papA5)
MLJMLAC_28750(papA5)
MSHJMSHI_07280(papA5)
MMAMK3U93_07805
MSPGF6B93_07125
MOTLTS72_15970
MLMMLPF_2691
MPAAMKK62_06600
MMEHM5I08_15240 M5I08_15295
MWUPT015_10800
MVAMvan_3119
MGIMflv_3386
MSPMspyr1_27170
MCBMycch_2769
MVQMYVA_2956(papA5)
MDUMDUV_13070(papA5)
MAUUNCTC10437_03014(papA5)
MPSCMPSYJ_36520(papA5)
MPOFMPOR_33480(papA5)
MSEIMSEDJ_33280(papA5)
MMONEWR22_14995
MRFMJO55_13995
MAUSJN090_14880
MYQTUM20985_51720(papA5)
MPATMPNTM1_03831(papA5)
MKRMKOR_16460(papA5)
MPAKMIU77_12280
MMVMYCMA_02745
MABBMASS_4932
MABLMMASJCM_2046 MMASJCM_3096 MMASJCM_4925
MCHEBB28_20865 BB28_24715
MIZBAB75_07595 BAB75_16630 BAB75_27425
MSTEMSTE_04219
MSAOMYCSP_14000 MYCSP_22545
MSALDSM43276_03871(papA5_2) DSM43276_04662(papA5_3)
MJDJDM601_2209(papA5)
MTER4434518_02132(papA5)
MMINMMIN_38070(papA5)
MHIBMHIB_16580(papA5)
MHERK3U94_12435
MVMMJO54_12380
MKKMU0083_002057
NFANFA_14610
NFRERS450000_02658(papA5)
NCYNOCYR_1519 NOCYR_2391
NBRO3I_006920 O3I_008740 O3I_009815 O3I_022155 O3I_033785
NSLBOX37_07180
NSRNS506_02688
NTPCRH09_08050 CRH09_14155 CRH09_20665
NOZDMB37_17945 DMB37_27790 DMB37_30560
NAHF5544_08085 F5544_21435 F5544_30935 F5544_30945 F5544_31775 F5544_41640 F5544_44790
NADNCTC11293_02450(papA5_2)
NIEKV110_07475 KV110_10345
NHUH0264_22540
NGPLTT66_03835
NSPUIFM12276_47310(papA5)
NVUV7968_17565
RFAA3L23_04949(papA5)
GOILK459_21355
TPRTpau_1036 Tpau_1039 Tpau_1040 Tpau_1646
TSMASU32_17865 ASU32_17880
TPULTPB0596_38030(papA5_2)
SRTSrot_1147 Srot_1825 Srot_2445 Srot_2530 Srot_2532 Srot_2533 Srot_2688
SALBXNR_5892
SCXAS200_43245
SRWTUE45_pSRc_0201(papA5)
SKYD0C37_31720
SPLULK06_031380
SALJSMD11_0468
SGDELQ87_00185
SASTCD934_28920
SGFHEP81_00439
SSPBCP982_05710 CP982_35270
SRUGF0345_01210
SVIOHWN34_29800
SCYSCATT_p16520
FSYFsymDg_2299
AOIAORI_5400
AORISD37_10955
KALKALB_5458
 » show all
Reference
1  [PMID:15070765]
  Authors
Onwueme KC, Ferreras JA, Buglino J, Lima CD, Quadri LE
  Title
Mycobacterial polyketide-associated proteins are acyltransferases: proof of principle with Mycobacterium tuberculosis PapA5.
  Journal
Proc Natl Acad Sci U S A 101:4608-13 (2004)
DOI:10.1073/pnas.0306928101
  Sequence
[mtu:Rv2939]
Reference
2  [PMID:15123643]
  Authors
Buglino J, Onwueme KC, Ferreras JA, Quadri LE, Lima CD
  Title
Crystal structure of PapA5, a phthiocerol dimycocerosyl transferase from Mycobacterium tuberculosis.
  Journal
J Biol Chem 279:30634-42 (2004)
DOI:10.1074/jbc.M404011200
  Sequence
[mtu:Rv2939]
Reference
3  [PMID:22361940]
  Authors
Chavadi SS, Onwueme KC, Edupuganti UR, Jerome J, Chatterjee D, Soll CE, Quadri LE
  Title
The mycobacterial acyltransferase PapA5 is required for biosynthesis of cell wall-associated phenolic glycolipids.
  Journal
Microbiology 158:1379-87 (2012)
DOI:10.1099/mic.0.057869-0
Reference
4  [PMID:26271001]
  Authors
Touchette MH, Bommineni GR, Delle Bovi RJ, Gadbery JE, Nicora CD, Shukla AK, Kyle JE, Metz TO, Martin DW, Sampson NS, Miller WT, Tonge PJ, Seeliger JC
  Title
Diacyltransferase Activity and Chain Length Specificity of Mycobacterium tuberculosis PapA5 in the Synthesis of Alkyl beta-Diol Lipids.
  Journal
Biochemistry 54:5457-68 (2015)
DOI:10.1021/acs.biochem.5b00455
  Sequence
[mtu:Rv2939]
Other DBs
ExplorEnz - The Enzyme Database: 2.3.1.282
IUBMB Enzyme Nomenclature: 2.3.1.282
ExPASy - ENZYME nomenclature database: 2.3.1.282
BRENDA, the Enzyme Database: 2.3.1.282

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