ID   MSL7_MYCBO              Reviewed;        2112 AA.
AC   Q7TXK8; A0A1R3Y2P2; X2BMA9;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 135.
DE   RecName: Full=Phenolphthiocerol synthesis polyketide synthase type I Pks15/1;
DE   AltName: Full=Beta-ketoacyl-acyl-carrier-protein synthase I;
DE            EC=2.3.1.41;
GN   Name=pks15/1; Synonyms=msl7, pks1; OrderedLocusNames=BQ2027_MB2971C;
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 PHENOLPHTHIOCEROL BIOSYNTHESIS, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12138124; DOI=10.1074/jbc.m206538200;
RA   Constant P., Perez E., Malaga W., Laneelle M.A., Saurel O., Daffe M.,
RA   Guilhot C.;
RT   "Role of the pks15/1 gene in the biosynthesis of phenolglycolipids in the
RT   Mycobacterium tuberculosis complex. Evidence that all strains synthesize
RT   glycosylated p-hydroxybenzoic methyl esters and that strains devoid of
RT   phenolglycolipids harbor a frameshift mutation in the pks15/1 gene.";
RL   J. Biol. Chem. 277:38148-38158(2002).
CC   -!- FUNCTION: Catalyzes the elongation by iterative transfer of p-
CC       hydroxybenzoyl group from FadD22 (pHBA-S-FAdD22) to form p-
CC       hydroxyphenylalkanoate (pHPA) intermediates during phenolphthiocerol
CC       (PPOL) biosynthesis. PPOL is an important intermediate in the
CC       biosynthesis of phenolic glycolipid (mycosid B).
CC       {ECO:0000269|PubMed:12138124}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP]
CC         + CO2 + holo-[ACP]; Xref=Rhea:RHEA:22836, Rhea:RHEA-COMP:9623,
CC         Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:14125,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78449, ChEBI:CHEBI:78776, ChEBI:CHEBI:138651;
CC         EC=2.3.1.41; Evidence={ECO:0000255|PROSITE-ProRule:PRU10022};
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   -!- DISRUPTION PHENOTYPE: Disruption of pks15/1 abolishes the production of
CC       phenolphthiocerol. {ECO:0000269|PubMed:12138124}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC       synthases family. {ECO:0000305}.
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DR   EMBL; LT708304; SIU01593.1; -; Genomic_DNA.
DR   RefSeq; NP_856616.1; NC_002945.3.
DR   AlphaFoldDB; Q7TXK8; -.
DR   SMR; Q7TXK8; -.
DR   PATRIC; fig|233413.5.peg.3263; -.
DR   BioCyc; MetaCyc:MONOMER-17228; -.
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:UniProtKB-EC.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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:0008610; P:lipid biosynthetic process; IMP:UniProtKB.
DR   CDD; cd05195; enoyl_red; 1.
DR   CDD; cd08956; KR_3_FAS_SDR_x; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 3.40.50.11460; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 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; IPR013154; ADH-like_N.
DR   InterPro; IPR011032; GroES-like_sf.
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; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR020807; PKS_DH.
DR   InterPro; IPR049551; PKS_DH_C.
DR   InterPro; IPR049552; PKS_DH_N.
DR   InterPro; IPR020843; PKS_ER.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR036299; Polyketide_synth_docking_sf.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF51; PHENOLPHTHIOCEROL_PHTHIOCEROL POLYKETIDE SYNTHASE SUBUNIT E; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF13602; ADH_zinc_N_2; 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; PF21089; PKS_DH_N; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   Pfam; PF14765; PS-DH; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00826; PKS_DH; 1.
DR   SMART; SM00829; PKS_ER; 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; SSF101173; Docking domain B of the erythromycin polyketide synthase (DEBS); 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 3.
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.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
DR   PROSITE; PS52019; PKS_MFAS_DH; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Fatty acid metabolism; Lipid metabolism;
KW   Multifunctional enzyme; Phosphopantetheine; Phosphoprotein;
KW   Reference proteome; Transferase.
FT   CHAIN           1..2112
FT                   /note="Phenolphthiocerol synthesis polyketide synthase type
FT                   I Pks15/1"
FT                   /id="PRO_0000406362"
FT   DOMAIN          46..469
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT   DOMAIN          941..1215
FT                   /note="PKS/mFAS DH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT   DOMAIN          2010..2085
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          579..893
FT                   /note="Acyltransferase"
FT                   /evidence="ECO:0000250"
FT   REGION          941..1101
FT                   /note="Dehydratase"
FT                   /evidence="ECO:0000250"
FT   REGION          941..1063
FT                   /note="N-terminal hotdog fold"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT   REGION          1075..1215
FT                   /note="C-terminal hotdog fold"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT   REGION          1406..1711
FT                   /note="Enoylreductase"
FT                   /evidence="ECO:0000250"
FT   REGION          1724..1905
FT                   /note="Beta-ketoacyl reductase"
FT                   /evidence="ECO:0000250"
FT   REGION          2084..2112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2084..2098
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        216
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT   ACT_SITE        351
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT   ACT_SITE        391
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT   ACT_SITE        670
FT                   /note="For acyltransferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   ACT_SITE        973
FT                   /note="Proton acceptor; for dehydratase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT   ACT_SITE        1136
FT                   /note="Proton donor; for dehydratase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT   BINDING         1536..1553
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         1725..1740
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2045
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   2112 AA;  218304 MW;  DCB5FA31A58A2785 CRC64;
     MIEEQRTMSV EGADQQSEKL FHYLKKVAVE LDETRARLRE YEQRATEPVA VVGIGCRFPG
     GVDGPDGLWD VVSAGRDVVS EFPTDRGWDV EGLYDPDPDA EGKTYTRWGA FLDDATGFDA
     GFFGIAPSEV LAMDPQQRLM LEVSWEALEH AGIDPLSLRG SATGVYTGIF AASYGNRDTG
     GLQGYGLTGT SISVASGRVS YVLGLQGPAV SVDTACSSSL VAIHWAMSSL RSGECDLALA
     GGVTVMGLPS IFVGFSRQRG LAADGRCKAF AAAADGTGWG EGAGVVVLER LSDARRLGHS
     VLAVVRGSAV NQDGASNGLT APNGLAQQRV IQAALANAGL SAADVDVVEA HGTATTLGDP
     IEAQALLSTY GQGRPAEQPL WVGSIKSNMG HTQAAAGVAG VIKMVQAMRH GVMPATLHVD
     EPSPRVDWTS GAVSVLTEAR EWSVDGRPRR AAVSSFGISG TNAHLILEEA PVPAPAEAPV
     EASESTGGPR PSMVPWVISA RSAEALTAQA GRLMAHVQAN PGLDPIDVGC SLASRSVFEH
     RAVVVGASRE QLIAGLAGLA AGEPGAGVAV GQPGSVGKTV VVFPGQGAQR IGMGRELYGE
     LPVFAQAFDA VADELDRHLR LPLRDVIWGA DADLLDSTEF AQPALFAVEV ASFAVLRDWG
     VLPDFVMGHS VGELAAAHAA GVLTLADAAM LVVARGRLMQ ALPAGGAMVA VAASEDEVEP
     LLGEGVGIAA INAPESVVIS GAQAAANAIA DRFAAQGRRV HQLAVSHAFH SPLMEPMLEE
     FARVAARVQA REPQLGLVSN VTGELAGPDF GSAQYWVDHV RRPVRFADSA RHLQTLGATH
     FIEAGPGSGL TGSIEQSLAP AEAMVVSMLG KDRPELASAL GAAGQVFTTG VPVQWSAVFA
     GSGGRRVQLP TYAFQRRRFW ETPGADGPAD AAGLGLGATE HALLGAVVER PDSDEVVLTG
     RLSLADQPWL ADHVVNGVVL FPGAGFVELV IRAGDEVGCA LIEELVLAAP LVMHPGVGVQ
     VQVVVGAADE SGHRAVSVYS RGDQSQGWLL NAEGMLGVAA AETPMDLSVW PPEGAESVDI
     SDGYAQLAER GYAYGPAFQG LVAIWRRGSE LFAEVVAPGE AGVAVDRMGM HPAVLDAVLH
     ALGLAVEKTQ ASTETRLPFC WRGVSLHAGG AGRVRARFAS AGADAISVDV CDATGLPVLT
     VRSLVTRPIT AEQLRAAVTA AGGASDQGPL EVVWSPISVV SGGANGSAPP APVSWADFCA
     GSDGDASVVV WELESAGGQA SSVVGSVYAA THTALEVLQS WLGADRAATL VVLTHGGVGL
     AGEDISDLAA AAVWGMARSA QAENPGRIVL IDTDAAVDAS VLAGVGEPQL LVRGGTVHAP
     RLSPAPALLA LPAAESAWRL AAGGGGTLED LVIQPCPEVQ APLQAGQVRV AVAAVGVNFR
     DVVAALGMYP GQAPPLGAEG AGVVLETGPE VTDLAVGDAV MGFLGGAGPL AVVDQQLVTR
     VPQGWSFAQA AAVPVVFLTA WYGLADLAEI KAGESVLIHA GTGGVGMAAV QLARQWGVEV
     FVTASRGKWD TLRAMGFDDD HIGDSRTCEF EEKFLAVTEG RGVDVVLDSL AGEFVDASLR
     LLVRGGRFLE MGKTDIRDAQ EIAANYPGVQ YRAFDLSEAG PARMQEMLAE VRELFDTREL
     HRLPVTTWDV RCAPAAFRFM SQARHIGKVV LTMPSALADR LADGTVVITG ATGAVGGVLA
     RHLVGAYGVR HLVLASRRGD RAEGAAELAA DLTEAGAKGQ VVACDVADRA AVAGLFAQLS
     REYPPVRGVI HAAGVLDDAV ITSLTPDRID TVLRAKVDAA WNLHQATSDL DLSMFVLCSS
     IAATVGSPGQ GNYSAANAFL DGLAAHRQAA GLAGISLAWG LWEQPGGMTA HLSSRDLARM
     SRSGLAPMSP AEAVELFDAA LAIDHPLAVA TLLDRAALDA RAQAGALPAL FSGLARRPRR
     RQIDDTGDAT SSKSALAQRL HGLAADEQLE LLVGLVCLQA AAVLGRPSAE DVDPDTEFGD
     LGFDSLTAVE LRNRLKTATG LTLPPTVIFD HPTPTAVAEY VAQQMSGSRP TESGDPTSQV
     VEPAAAEVSV HA
//