PPSE_MYCTO
ID PPSE_MYCTO Reviewed; 1488 AA.
AC P9WQE0; L0TDU0; P96204; Q7D6E9;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Phenolphthiocerol/phthiocerol polyketide synthase subunit E {ECO:0000305};
DE EC=2.3.1.292 {ECO:0000250|UniProtKB:P9WQE1};
DE AltName: Full=(Phenol)carboxyphthiodiolenone synthase subunit E;
DE AltName: Full=Beta-ketoacyl-acyl-carrier-protein synthase I;
DE AltName: Full=Phthiocerol synthesis polyketide synthase type I PpsE;
GN Name=ppsE; OrderedLocusNames=MT3005;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- FUNCTION: Part of the PpsABCDE complex involved in the biosynthesis of
CC the lipid core common to phthiocerols and phenolphthiocerols by
CC successive additions of malonyl-CoA or methylmalonyl-CoA extender
CC units. PpsA can accept as substrate the activated forms of either
CC icosanoyl (C20), docosanoyl (C22) or lignoceroyl (C24) groups from
CC FadD26, or a (4-hydroxyphenyl)-C17 or (4-hydroxyphenyl)-C19 fatty acyl
CC from FadD29. PpsA initiates the biosynthesis and extends its substrate
CC using a malonyl-CoA extender unit. The PpsB and PpsC proteins add the
CC second and third malonyl-CoA extender units. PpsD adds an (R)-
CC methylmalonyl unit and PpsE adds a second (R)-methylmalonyl unit. The
CC incorporation of the methylmalonyl units results in formation of two
CC branched methyl groups in the elongated product.
CC {ECO:0000250|UniProtKB:P9WQE1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 (S)-methylmalonyl-CoA + 10 H(+) + icosanoyl-
CC [(phenol)carboxyphthiodiolenone synthase] + 3 malonyl-CoA + 5 NADPH =
CC C32-carboxyphthiodiolenone-[(phenol)carboxyphthiodiolenone synthase]
CC + 5 CO2 + 5 CoA + 2 H2O + 5 NADP(+); Xref=Rhea:RHEA:57748, Rhea:RHEA-
CC COMP:14985, Rhea:RHEA-COMP:14986, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57327, ChEBI:CHEBI:57384, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:87848, ChEBI:CHEBI:142236;
CC EC=2.3.1.292; Evidence={ECO:0000250|UniProtKB:P9WQE1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 (S)-methylmalonyl-CoA + docosanoyl-
CC [(phenol)carboxyphthiodiolenone synthase] + 10 H(+) + 3 malonyl-CoA +
CC 5 NADPH = C34-carboxyphthiodiolenone-[(phenol)carboxyphthiodiolenone
CC synthase] + 5 CO2 + 5 CoA + 2 H2O + 5 NADP(+); Xref=Rhea:RHEA:57752,
CC Rhea:RHEA-COMP:14987, Rhea:RHEA-COMP:14988, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57327, ChEBI:CHEBI:57384, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:142237, ChEBI:CHEBI:142238;
CC EC=2.3.1.292; Evidence={ECO:0000250|UniProtKB:P9WQE1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 (S)-methylmalonyl-CoA + 17-(4-hydroxyphenyl)heptadecanoyl-
CC [(phenol)carboxyphthiodiolenone synthase] + 10 H(+) + 3 malonyl-CoA +
CC 5 NADPH = C35-(phenol)carboxyphthiodiolenone-
CC [(phenol)carboxyphthiodiolenone synthase] + 5 CO2 + 5 CoA + 2 H2O + 5
CC NADP(+); Xref=Rhea:RHEA:57756, Rhea:RHEA-COMP:14272, Rhea:RHEA-
CC COMP:14989, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57327, ChEBI:CHEBI:57384,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133300,
CC ChEBI:CHEBI:142259; EC=2.3.1.292;
CC Evidence={ECO:0000250|UniProtKB:P9WQE1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 (S)-methylmalonyl-CoA + 19-(4-hydroxyphenyl)nonadecanoyl-
CC [(phenol)carboxyphthiodiolenone synthase] + 10 H(+) + 3 malonyl-CoA +
CC 5 NADPH = C37-(phenol)carboxyphthiodiolenone-
CC [(phenol)carboxyphthiodiolenone synthase] + 5 CO2 + 5 CoA + 2 H2O + 5
CC NADP(+); Xref=Rhea:RHEA:57760, Rhea:RHEA-COMP:14273, Rhea:RHEA-
CC COMP:14990, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57327, ChEBI:CHEBI:57384,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133301,
CC ChEBI:CHEBI:142260; EC=2.3.1.292;
CC Evidence={ECO:0000250|UniProtKB:P9WQE1};
CC -!- COFACTOR:
CC Name=NADP(+); Xref=ChEBI:CHEBI:58349;
CC Evidence={ECO:0000250|UniProtKB:P9WQE1};
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000250};
CC Note=Binds 1 phosphopantetheine covalently. {ECO:0000250};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000250|UniProtKB:P9WQE1}.
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DR EMBL; AE000516; AAK47332.1; -; Genomic_DNA.
DR PIR; C70984; C70984.
DR RefSeq; WP_003900602.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WQE0; -.
DR SMR; P9WQE0; -.
DR EnsemblBacteria; AAK47332; AAK47332; MT3005.
DR KEGG; mtc:MT3005; -.
DR PATRIC; fig|83331.31.peg.3245; -.
DR HOGENOM; CLU_000022_16_14_11; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.30.559.10; -; 1.
DR Gene3D; 3.40.366.10; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00668; Condensation; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 3: Inferred from homology;
KW Fatty acid metabolism; Lipid metabolism; Multifunctional enzyme; NADP;
KW Oxidoreductase; Phosphopantetheine; Phosphoprotein; Transferase.
FT CHAIN 1..1488
FT /note="Phenolphthiocerol/phthiocerol polyketide synthase
FT subunit E"
FT /id="PRO_0000426792"
FT DOMAIN 930..1004
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 6..389
FT /note="Beta-ketoacyl synthase"
FT /evidence="ECO:0000250"
FT REGION 551..868
FT /note="Acyltransferase"
FT /evidence="ECO:0000250"
FT ACT_SITE 184
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 641
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT BINDING 1286..1331
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT MOD_RES 965
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 1488 AA; 158745 MW; C6418D88A27BB701 CRC64;
MSIPENAIAV VGMAGRFPGA KDVSAFWSNL RRGKESIVTL SEQELRDAGV SDKTLADPAY
VRRAPLLDGI DEFDAGFFGF PPLAAQVLDP QHRLFLQCAW HALEDAGADP ARFDGSIGVY
GTSSPSGYLL HNLLSHRDPN AVLAEGLNFD QFSLFLQNDK DFLATRISHA FNLRGPSIAV
QTACSSSLVA VHLACLSLLS GECDMALAGG SSLCIPHRVG YFTSPGSMVS AVGHCRPFDV
RADGTVFGSG VGLVVLKPLA AAIDAGDRIH AVIRGSAINN DGSAKMGYAA PNPAAQADVI
AEAHAVSGID SSTVSYVECH GTGTPLGDPI EIQGLRAAFE VSQTSRSAPC VLGSVKSNIG
HLEVAAGIAG LIKTILCLKN KALPATLHYT SPNPELRLDQ SPFVVQSKYG PWECDGVRRA
GVSSFGVGGT NAHVVLEEAP AEASEVSAHA EPAGPQVILL SAQTAAALGE SRTALAAALE
TQDGPRLSDV AYTLARRRKH NVTMAAVVHD REHAATVLRA AEHDNVFVGE AAHDGEHGDR
ADAAPTSDRV VFLFPGQGAQ HVGMAKGLYD TEPVFAQHFD TCAAGFRDET GIDLHAEVFD
GTATDLERID RSQPALFTVE YALAKLVDTF GVRAGAYIGY STGEYIAATL AGVFDLQTAI
KTVSLRARLM HESPPGAMVA VALGPDDVTQ YLPPEVELSA VNDPGNCVVA GPKDQIRALR
QRLTEAGIPV RRVRATHAFH TSAMDPMLGQ FQEFLSRQQL RPPRTPLLSN LTGSWMSDQQ
VVDPASWTRQ ISSPIRFADE LDVVLAAPSR ILVEVGPGGS LTGSAMRHPK WSTTHRTVRL
MRHPLQDVDD RDTFLRALGE LWSAGVEVDW TPRRPAVPHL VSLPGYPFAR QRHWVEPNHT
VWAQAPGANN GSPAGTADGS TAATVDAARN GESQTEVTLQ RIWSQCLGVS SVDRNANFFD
LGGDSLMAIS IAMAAANEGL TITPQDLYEY PTLASLTAAV DASFASSGLA KPPEAQANPA
VPPNVTYFLD RGLRDTGRCR VPLILRLDPK IGLPDIRAVL TAVVNHHDAL RLHLVGNDGI
WEQHIAAPAE FTGLSNRSVP NGVAAGSPEE RAAVLGILAE LLEDQTDPNA PLAAVHIAAA
HGGPHYLCLA IHAMVTDDSS RQILATDIVT AFGQRLAGEE ITLEPVSTGW REWSLRCAAL
ATHPAALDTR SYWIENSTKA TLWLADALPN AHTAHPPRAD ELTKLSSTLS VEQTSELDDG
RRRFRRSIQT ILLAALGRTI AQTVGEGVVA VELEGEGRSV LRPDVDLRRT VGWFTTYYPV
PLACATGLGA LAQLDAVHNT LKSVPHYGIG YGLLRYVYAP TGRVLGAQRT PDIHFRYAGV
IPELPSGDAP VQFDSDMTLP VREPIPGMGH AIELRVYRFG GSLHLDWWYD TRRIPAATAE
ALERTFPLAL SALIQEAIAA EHTEHDDSEI VGEPEAGALV DLSSMDAG
