PPSB_MYCTO
ID PPSB_MYCTO Reviewed; 1538 AA.
AC P9WQE4; L0TB25; O53234; Q10978;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Phenolphthiocerol/phthiocerol polyketide synthase subunit B {ECO:0000305};
DE EC=2.3.1.292 {ECO:0000250|UniProtKB:P9WQE5};
DE AltName: Full=(Phenol)carboxyphthiodiolenone synthase subunit B;
DE AltName: Full=Beta-ketoacyl-acyl-carrier-protein synthase I;
DE AltName: Full=Phthiocerol synthesis polyketide synthase type I PpsB;
GN Name=ppsB; OrderedLocusNames=MT3002;
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:P9WQE5}.
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:P9WQE5};
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:P9WQE5};
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:P9WQE5};
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:P9WQE5};
CC -!- COFACTOR:
CC Name=NADP(+); Xref=ChEBI:CHEBI:58349;
CC Evidence={ECO:0000250|UniProtKB:P9WQE5};
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:P9WQE5}.
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DR EMBL; AE000516; AAK47329.1; -; Genomic_DNA.
DR PIR; E70874; E70874.
DR RefSeq; WP_003899547.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WQE4; -.
DR SMR; P9WQE4; -.
DR EnsemblBacteria; AAK47329; AAK47329; MT3002.
DR KEGG; mtc:MT3002; -.
DR PATRIC; fig|83331.31.peg.3242; -.
DR HOGENOM; CLU_000022_35_0_11; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0034081; C:polyketide synthase complex; ISS:UniProtKB.
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:0071766; P:Actinobacterium-type cell wall biogenesis; ISS:UniProtKB.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0097041; P:phenolic phthiocerol biosynthetic process; ISS:UniProtKB.
DR GO; GO:0097040; P:phthiocerol biosynthetic process; ISS:UniProtKB.
DR Gene3D; 1.10.1200.10; -; 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; 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; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR013968; PKS_KR.
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; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 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; SSF51735; SSF51735; 2.
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..1538
FT /note="Phenolphthiocerol/phthiocerol polyketide synthase
FT subunit B"
FT /id="PRO_0000426790"
FT DOMAIN 1423..1498
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 36..458
FT /note="Beta-ketoacyl synthase"
FT /evidence="ECO:0000250"
FT REGION 553..882
FT /note="Acyltransferase"
FT /evidence="ECO:0000250"
FT REGION 1153..1328
FT /note="Beta-ketoacyl reductase"
FT /evidence="ECO:0000250"
FT ACT_SITE 205
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 649
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT BINDING 1153..1196
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT MOD_RES 1458
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 1538 AA; 162528 MW; B55E2A2042AD00CC CRC64;
MMRTAFSRIS GMTAQQRTSL ADEFDRVSRI AVAEPVAVVG IGCRFPGDVD GPESFWDFLV
AGRNAISTVP ADRWDAEAFY HPDPLTPGRM TTKWGGFVPD VAGFDAEFFG ITPREAAAMD
PQQRMLLEVA WEALEHAGIP PDSLGGTRTA VMMGVYFNEY QSMLAASPQN VDAYSGTGNA
HSITVGRISY LLGLRGPAVA VDTACSSSLV AVHLACQSLR LRETDLALAG GVSITLRPET
QIAISAWGLL SPQGRCAAFD AAADGFVRGE GAGVVVLKRL TDAVRDGDQV LAVVRGSAVN
QDGRSNGVTA PNTAAQCDVI ADALRSGDVA PDSVNYVEAH GTGTVLGDPI EFEALAATYG
HGGDACALGA VKTNIGHLEA AAGIAGFIKA TLAVQRATIP PNLHFSQWNP AIDAASTRFF
VPTQNSPWPT AEGPRRAAVS SFGLGGTNAH VIIEQGSELA PVSEGGEDTG VSTLVVTGKT
AQRMAATAQV LADWMEGPGA EVAVADVAHT VNHHRARQAT FGTVVARDRA QAIAGLRALA
AGQHAPGVVS HQDGSPGPGT VFVYSGRGSQ WAGMGRQLLA DEPAFAAAVA ELEPVFVEQA
GFSLRDVIAT GKELVGIEQI QLGLIGMQLT LTELWRSYGV QPDLVIGHSM GEVAAAVVAG
ALTPAEGLRV TATRARLMAP LSGQGGMALL GLDAAATEAL IADYPQVTVG IYNSPRQTVI
AGPTEQIDEL IARVRAQNRF ASRVNIEVAP HNPAMDALQP AMRSELADLT PRTPTIGIIS
TTYADLHTQP IFDAEHWATN MRNPVRFQQA IASAGSGADG AYHTFIEISA HPLLTQAIAD
TLEDAHRPTK SAAKYLSIGT LQRDADDTVT FRTNLYTADI AHPPHTCHPP EPHPTIPTTP
WQHTHHWIAT THPSTAAPED PGSNKVVVNG QSTSESRALE DWCHQLAWPI RPAVSADPPS
TAAWLVVADN ELCHELARAA DSRVDSLSPP ALAAGSDPAA LLDALRGVDN VLYAPPVPGE
LLDIESAYQV FHATRRLAAA MVASSATAIS PPKLFIMTRN AQPISEGDRA NPGHAVLWGL
GRSLALEHPE IWGGIIDLDD SMPAELAVRH VLTAAHGTDG EDQVVYRSGA RHVPRLQRRT
LPGKPVTLNA DASQLVIGAT GNIGPHLIRQ LARMGAKTIV AMARKPGALD ELTQCLAATG
TDLIAVAADA TDPAAMQTLF DRFGTELPPL EGIYLAAFAG RPALLSEMTD DDVTTMFRPK
LDALALLHRR SLKSPVRHFV LFSSVSGLLG SRWLAHYTAT SAFLDSFAGA RRTMGLPATV
VDWGLWKSLA DVQKDATQIS AESGLQPMAD EVAIGALPLV MNPDAAVATV VVAADWPLLA
AAYRTRGALR IVDDLLPAPE DVGKGESEFR TSLRSCPAEK RRDMLFDHVG ALAATVMGMP
PTEPLDPSAG FFQLGMDSLM SVTLQRALSE SLGEFLPASV VFDYPTVYSL TDYLATVLPE
LLEIGATAVA TQQATDSYHE LTEAELLEQL SERLRGTQ
