ID   PPSB_MYCTU              Reviewed;        1538 AA.
AC   P9WQE5; 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 43.
DE   RecName: Full=Phenolphthiocerol/phthiocerol polyketide synthase subunit B {ECO:0000305};
DE            EC=2.3.1.292 {ECO:0000269|PubMed:15749014, ECO:0000305|PubMed:20553505};
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=Rv2932; ORFNames=MTCY338.21, MTV011.01;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND PATHWAY.
RX   PubMed=15749014; DOI=10.1016/j.molcel.2005.02.009;
RA   Trivedi O.A., Arora P., Vats A., Ansari M.Z., Tickoo R., Sridharan V.,
RA   Mohanty D., Gokhale R.S.;
RT   "Dissecting the mechanism and assembly of a complex virulence mycobacterial
RT   lipid.";
RL   Mol. Cell 17:631-643(2005).
RN   [3]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=20553505; DOI=10.1111/j.1742-4658.2010.07688.x;
RA   Simeone R., Leger M., Constant P., Malaga W., Marrakchi H., Daffe M.,
RA   Guilhot C., Chalut C.;
RT   "Delineation of the roles of FadD22, FadD26 and FadD29 in the biosynthesis
RT   of phthiocerol dimycocerosates and related compounds in Mycobacterium
RT   tuberculosis.";
RL   FEBS J. 277:2715-2725(2010).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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:15749014, PubMed:20553505). PpsA can accept as substrate the
CC       activated forms of either icosanoyl (C20), docosanoyl (C22) or
CC       lignoceroyl (C24) groups from FadD26, or a (4-hydroxyphenyl)-C17 or (4-
CC       hydroxyphenyl)-C19 fatty acyl from FadD29 (PubMed:15749014,
CC       PubMed:20553505). PpsA initiates the biosynthesis and extends its
CC       substrate using a malonyl-CoA extender unit. The PpsB and PpsC proteins
CC       add the 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 (PubMed:15749014).
CC       {ECO:0000269|PubMed:15749014, ECO:0000269|PubMed:20553505}.
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:0000269|PubMed:15749014,
CC         ECO:0000305|PubMed:20553505};
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:0000269|PubMed:15749014,
CC         ECO:0000305|PubMed:20553505};
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:0000269|PubMed:15749014, ECO:0000305|PubMed:20553505};
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:0000269|PubMed:15749014, ECO:0000305|PubMed:20553505};
CC   -!- COFACTOR:
CC       Name=NADP(+); Xref=ChEBI:CHEBI:58349;
CC         Evidence={ECO:0000269|PubMed:15749014};
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:15749014}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL123456; CCP45735.1; -; Genomic_DNA.
DR   PIR; E70874; E70874.
DR   RefSeq; NP_217448.1; NC_000962.3.
DR   RefSeq; WP_003899547.1; NZ_NVQJ01000078.1.
DR   AlphaFoldDB; P9WQE5; -.
DR   SMR; P9WQE5; -.
DR   STRING; 83332.Rv2932; -.
DR   PaxDb; P9WQE5; -.
DR   DNASU; 888023; -.
DR   GeneID; 888023; -.
DR   KEGG; mtu:Rv2932; -.
DR   PATRIC; fig|83332.111.peg.3262; -.
DR   TubercuList; Rv2932; -.
DR   eggNOG; COG1020; Bacteria.
DR   eggNOG; COG1028; Bacteria.
DR   eggNOG; COG3321; Bacteria.
DR   OMA; WVANLRN; -.
DR   PhylomeDB; P9WQE5; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0034081; C:polyketide synthase complex; ISS:UniProtKB.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IDA:MTBBASE.
DR   GO; GO:0004312; F:fatty acid synthase activity; IBA:GO_Central.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0071770; P:DIM/DIP cell wall layer assembly; IDA:MTBBASE.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IDA:MTBBASE.
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   1: Evidence at protein level;
KW   Fatty acid metabolism; Lipid metabolism; Multifunctional enzyme; NADP;
KW   Oxidoreductase; Phosphopantetheine; Phosphoprotein; Reference proteome;
KW   Transferase.
FT   CHAIN           1..1538
FT                   /note="Phenolphthiocerol/phthiocerol polyketide synthase
FT                   subunit B"
FT                   /id="PRO_0000180302"
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