ID   PPSB_MYCBO              Reviewed;        1538 AA.
AC   Q7TXL9; A0A1R3Y310; X2BM25;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 123.
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=BQ2027_MB2957;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
RN   [3]
RP   FUNCTION IN THE PHTHIOCEROL AND PHENOLPHTHIOCEROL BIOSYNTHESIS, PATHWAY,
RP   AND DISRUPTION PHENOTYPE.
RC   STRAIN=BCG;
RX   PubMed=9201977; DOI=10.1074/jbc.272.27.16741;
RA   Azad A.K., Sirakova T.D., Fernandes N.D., Kolattukudy P.E.;
RT   "Gene knockout reveals a novel gene cluster for the synthesis of a class of
RT   cell wall lipids unique to pathogenic mycobacteria.";
RL   J. Biol. Chem. 272:16741-16745(1997).
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 units
CC       (PubMed:9201977). PpsA can accept as substrate the activated forms of
CC       either icosanoyl (C20), docosanoyl (C22) or lignoceroyl (C24) groups
CC       from FadD26, or a (4-hydroxyphenyl)-C17 or (4-hydroxyphenyl)-C19 fatty
CC       acyl from FadD29 (By similarity). PpsA initiates the biosynthesis and
CC       extends its substrate using a malonyl-CoA extender unit. The PpsB and
CC       PpsC proteins add the second and third malonyl-CoA extender units. PpsD
CC       adds an (R)-methylmalonyl unit and PpsE adds a second (R)-methylmalonyl
CC       unit. The incorporation of the methylmalonyl units results in formation
CC       of two branched methyl groups in the elongated product (By similarity).
CC       {ECO:0000250|UniProtKB:P9WQE5, ECO:0000269|PubMed:9201977}.
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:0000269|PubMed:9201977}.
CC   -!- DISRUPTION PHENOTYPE: Disruption of the pps gene cluster abolishes the
CC       production of both phthiocerol and phenolphthiocerol derivatives.
CC       {ECO:0000269|PubMed:9201977}.
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DR   EMBL; LT708304; SIU01578.1; -; Genomic_DNA.
DR   RefSeq; NP_856602.1; NC_002945.3.
DR   RefSeq; WP_003414835.1; NC_002945.4.
DR   AlphaFoldDB; Q7TXL9; -.
DR   SMR; Q7TXL9; -.
DR   PATRIC; fig|233413.5.peg.3245; -.
DR   BioCyc; MetaCyc:MONOMER-19627; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000001419; Chromosome.
DR   GO; GO:0034081; C:polyketide synthase complex; IMP: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; IMP:UniProtKB.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0097041; P:phenolic phthiocerol biosynthetic process; IMP:UniProtKB.
DR   GO; GO:0097040; P:phthiocerol biosynthetic process; IMP:UniProtKB.
DR   CDD; cd05274; KR_FAS_SDR_x; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.30.70.250; Malonyl-CoA ACP transacylase, ACP-binding; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
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; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SMART; SM01294; PKS_PP_betabranch; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
PE   1: Evidence at protein level;
KW   Fatty acid metabolism; Lipid metabolism; Multifunctional enzyme; NADP;
KW   Oxidoreductase; Phosphopantetheine; Phosphoprotein; Reference proteome;
KW   Repeat; Transferase.
FT   CHAIN           1..1538
FT                   /note="Phenolphthiocerol/phthiocerol polyketide synthase
FT                   subunit B"
FT                   /id="PRO_0000406946"
FT   DOMAIN          33..455
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT   DOMAIN          1423..1498
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
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:PRU01348"
FT   ACT_SITE        340
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT   ACT_SITE        377
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
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;  162485 MW;  BD08742044AAFECC 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
     LDALALLHRL 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
//