MSL7_MYCBO
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 03-AUG-2022, entry version 128.
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; Actinobacteria; Corynebacteriales; 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 RefSeq; WP_010950804.1; NC_002945.4.
DR AlphaFoldDB; Q7TXK8; -.
DR SMR; Q7TXK8; -.
DR EnsemblBacteria; SIU01593; SIU01593; BQ2027_MB2971C.
DR PATRIC; fig|233413.5.peg.3263; -.
DR OMA; TFRWEED; -.
DR BioCyc; MetaCyc:MON-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 Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.10.129.110; -; 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; IPR013154; ADH_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; IPR020807; PKS_dehydratase.
DR InterPro; IPR042104; PKS_dehydratase_sf.
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 Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08240; ADH_N; 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 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; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF101173; SSF101173; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 3.
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.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Fatty acid metabolism; Lipid metabolism;
KW Multifunctional enzyme; Phosphopantetheine; Phosphoprotein; Transferase.
FT CHAIN 1..2112
FT /note="Phenolphthiocerol synthesis polyketide synthase type
FT I Pks15/1"
FT /id="PRO_0000406362"
FT DOMAIN 2010..2085
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 42..471
FT /note="Beta-ketoacyl synthase"
FT /evidence="ECO:0000250"
FT REGION 579..893
FT /note="Acyltransferase"
FT /evidence="ECO:0000250"
FT REGION 941..1101
FT /note="Dehydratase"
FT /evidence="ECO:0000250"
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:PRU10022"
FT ACT_SITE 670
FT /note="For acyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
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
