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Q7TXK8 (MSL7_MYCBO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phenolphthiocerol synthesis polyketide synthase type I Pks15/1
Alternative name(s):
Beta-ketoacyl-acyl-carrier-protein synthase I
EC=2.3.1.41
Gene names
Name:pks15/1
Synonyms:msl7, pks1
Ordered Locus Names:Mb2971c
OrganismMycobacterium bovis (strain ATCC BAA-935 / AF2122/97) [Complete proteome] [HAMAP]
Taxonomic identifier233413 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length2112 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the elongation by iterative transfer of p-hydroxybenzoyl group from FadD22 (pHBA-S-FAdD22) to form p-hydroxyphenylalkanoate (pHPA) intermediates during phenolphthiocerol (PPOL) biosynthesis. PPOL is an important intermediate in the biosynthesis of phenolic glycolipid (mycosid B). Ref.2

Catalytic activity

Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl- [acyl-carrier-protein] + CO2 + [acyl-carrier-protein].

Cofactor

Binds 1 phosphopantetheine covalently By similarity.

Pathway

Lipid metabolism; fatty acid biosynthesis.

Disruption phenotype

Disruption of pks15/1 abolishes the production of phenolphthiocerol. Ref.2

Sequence similarities

Belongs to the beta-ketoacyl-ACP synthases family.

Contains 1 acyl carrier domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 21122112Phenolphthiocerol synthesis polyketide synthase type I Pks15/1
PRO_0000406362

Regions

Domain2012 – 208271Acyl carrier
Nucleotide binding1536 – 155318NADP By similarity
Nucleotide binding1725 – 174016NADP By similarity
Region42 – 471430Beta-ketoacyl synthase By similarity
Region579 – 893315Acyltransferase By similarity
Region941 – 1101161Dehydratase By similarity
Region1406 – 1711306Enoylreductase By similarity
Region1724 – 1905182Beta-ketoacyl reductase By similarity

Sites

Active site2161For beta-ketoacyl synthase activity By similarity
Active site6701For acyltransferase activity By similarity

Amino acid modifications

Modified residue20451O-(pantetheine 4'-phosphoryl)serine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7TXK8 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: DCB5FA31A58A2785

FASTA2,112218,304
        10         20         30         40         50         60 
MIEEQRTMSV EGADQQSEKL FHYLKKVAVE LDETRARLRE YEQRATEPVA VVGIGCRFPG 

        70         80         90        100        110        120 
GVDGPDGLWD VVSAGRDVVS EFPTDRGWDV EGLYDPDPDA EGKTYTRWGA FLDDATGFDA 

       130        140        150        160        170        180 
GFFGIAPSEV LAMDPQQRLM LEVSWEALEH AGIDPLSLRG SATGVYTGIF AASYGNRDTG 

       190        200        210        220        230        240 
GLQGYGLTGT SISVASGRVS YVLGLQGPAV SVDTACSSSL VAIHWAMSSL RSGECDLALA 

       250        260        270        280        290        300 
GGVTVMGLPS IFVGFSRQRG LAADGRCKAF AAAADGTGWG EGAGVVVLER LSDARRLGHS 

       310        320        330        340        350        360 
VLAVVRGSAV NQDGASNGLT APNGLAQQRV IQAALANAGL SAADVDVVEA HGTATTLGDP 

       370        380        390        400        410        420 
IEAQALLSTY GQGRPAEQPL WVGSIKSNMG HTQAAAGVAG VIKMVQAMRH GVMPATLHVD 

       430        440        450        460        470        480 
EPSPRVDWTS GAVSVLTEAR EWSVDGRPRR AAVSSFGISG TNAHLILEEA PVPAPAEAPV 

       490        500        510        520        530        540 
EASESTGGPR PSMVPWVISA RSAEALTAQA GRLMAHVQAN PGLDPIDVGC SLASRSVFEH 

       550        560        570        580        590        600 
RAVVVGASRE QLIAGLAGLA AGEPGAGVAV GQPGSVGKTV VVFPGQGAQR IGMGRELYGE 

       610        620        630        640        650        660 
LPVFAQAFDA VADELDRHLR LPLRDVIWGA DADLLDSTEF AQPALFAVEV ASFAVLRDWG 

       670        680        690        700        710        720 
VLPDFVMGHS VGELAAAHAA GVLTLADAAM LVVARGRLMQ ALPAGGAMVA VAASEDEVEP 

       730        740        750        760        770        780 
LLGEGVGIAA INAPESVVIS GAQAAANAIA DRFAAQGRRV HQLAVSHAFH SPLMEPMLEE 

       790        800        810        820        830        840 
FARVAARVQA REPQLGLVSN VTGELAGPDF GSAQYWVDHV RRPVRFADSA RHLQTLGATH 

       850        860        870        880        890        900 
FIEAGPGSGL TGSIEQSLAP AEAMVVSMLG KDRPELASAL GAAGQVFTTG VPVQWSAVFA 

       910        920        930        940        950        960 
GSGGRRVQLP TYAFQRRRFW ETPGADGPAD AAGLGLGATE HALLGAVVER PDSDEVVLTG 

       970        980        990       1000       1010       1020 
RLSLADQPWL ADHVVNGVVL FPGAGFVELV IRAGDEVGCA LIEELVLAAP LVMHPGVGVQ 

      1030       1040       1050       1060       1070       1080 
VQVVVGAADE SGHRAVSVYS RGDQSQGWLL NAEGMLGVAA AETPMDLSVW PPEGAESVDI 

      1090       1100       1110       1120       1130       1140 
SDGYAQLAER GYAYGPAFQG LVAIWRRGSE LFAEVVAPGE AGVAVDRMGM HPAVLDAVLH 

      1150       1160       1170       1180       1190       1200 
ALGLAVEKTQ ASTETRLPFC WRGVSLHAGG AGRVRARFAS AGADAISVDV CDATGLPVLT 

      1210       1220       1230       1240       1250       1260 
VRSLVTRPIT AEQLRAAVTA AGGASDQGPL EVVWSPISVV SGGANGSAPP APVSWADFCA 

      1270       1280       1290       1300       1310       1320 
GSDGDASVVV WELESAGGQA SSVVGSVYAA THTALEVLQS WLGADRAATL VVLTHGGVGL 

      1330       1340       1350       1360       1370       1380 
AGEDISDLAA AAVWGMARSA QAENPGRIVL IDTDAAVDAS VLAGVGEPQL LVRGGTVHAP 

      1390       1400       1410       1420       1430       1440 
RLSPAPALLA LPAAESAWRL AAGGGGTLED LVIQPCPEVQ APLQAGQVRV AVAAVGVNFR 

      1450       1460       1470       1480       1490       1500 
DVVAALGMYP GQAPPLGAEG AGVVLETGPE VTDLAVGDAV MGFLGGAGPL AVVDQQLVTR 

      1510       1520       1530       1540       1550       1560 
VPQGWSFAQA AAVPVVFLTA WYGLADLAEI KAGESVLIHA GTGGVGMAAV QLARQWGVEV 

      1570       1580       1590       1600       1610       1620 
FVTASRGKWD TLRAMGFDDD HIGDSRTCEF EEKFLAVTEG RGVDVVLDSL AGEFVDASLR 

      1630       1640       1650       1660       1670       1680 
LLVRGGRFLE MGKTDIRDAQ EIAANYPGVQ YRAFDLSEAG PARMQEMLAE VRELFDTREL 

      1690       1700       1710       1720       1730       1740 
HRLPVTTWDV RCAPAAFRFM SQARHIGKVV LTMPSALADR LADGTVVITG ATGAVGGVLA 

      1750       1760       1770       1780       1790       1800 
RHLVGAYGVR HLVLASRRGD RAEGAAELAA DLTEAGAKGQ VVACDVADRA AVAGLFAQLS 

      1810       1820       1830       1840       1850       1860 
REYPPVRGVI HAAGVLDDAV ITSLTPDRID TVLRAKVDAA WNLHQATSDL DLSMFVLCSS 

      1870       1880       1890       1900       1910       1920 
IAATVGSPGQ GNYSAANAFL DGLAAHRQAA GLAGISLAWG LWEQPGGMTA HLSSRDLARM 

      1930       1940       1950       1960       1970       1980 
SRSGLAPMSP AEAVELFDAA LAIDHPLAVA TLLDRAALDA RAQAGALPAL FSGLARRPRR 

      1990       2000       2010       2020       2030       2040 
RQIDDTGDAT SSKSALAQRL HGLAADEQLE LLVGLVCLQA AAVLGRPSAE DVDPDTEFGD 

      2050       2060       2070       2080       2090       2100 
LGFDSLTAVE LRNRLKTATG LTLPPTVIFD HPTPTAVAEY VAQQMSGSRP TESGDPTSQV 

      2110 
VEPAAAEVSV HA 

« Hide

References

« Hide 'large scale' references
[1]"The complete genome sequence of Mycobacterium bovis."
Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M., Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B., Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J. expand/collapse author list , Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.
Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-935 / AF2122/97.
[2]"Role of the pks15/1 gene in the biosynthesis of phenolglycolipids in the Mycobacterium tuberculosis complex. Evidence that all strains synthesize glycosylated p-hydroxybenzoic methyl esters and that strains devoid of phenolglycolipids harbor a frameshift mutation in the pks15/1 gene."
Constant P., Perez E., Malaga W., Laneelle M.A., Saurel O., Daffe M., Guilhot C.
J. Biol. Chem. 277:38148-38158(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHENOLPHTHIOCEROL BIOSYNTHESIS, DISRUPTION PHENOTYPE.
Strain: ATCC BAA-935 / AF2122/97.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX248333 Genomic DNA. Translation: CDO44238.1.
RefSeqNP_856616.1. NC_002945.3.

3D structure databases

ProteinModelPortalQ7TXK8.
SMRQ7TXK8. Positions 18-921.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING233413.Mb2971c.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD96658; CAD96658; Mb2971c.
GeneID1092134.
KEGGmbo:Mb2971c.
PATRIC18008262. VBIMycBov88188_3263.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3321.
HOGENOMHOG000046292.
KOK12430.
OMAHAHAVES.
OrthoDBEOG6QP0WP.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-17228.
UniPathwayUPA00094.

Family and domain databases

Gene3D1.10.1200.10. 1 hit.
3.40.366.10. 2 hits.
3.40.47.10. 2 hits.
3.40.50.720. 2 hits.
3.90.180.10. 1 hit.
InterProIPR001227. Ac_transferase_dom.
IPR009081. Acyl_carrier_prot-like.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR013149. ADH_C.
IPR013154. ADH_GroES-like.
IPR011032. GroES-like.
IPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR016036. Malonyl_transacylase_ACP-bd.
IPR016040. NAD(P)-bd_dom.
IPR020842. PKS/FAS_KR.
IPR020801. PKS_acyl_transferase.
IPR020841. PKS_Beta-ketoAc_synthase_dom.
IPR020807. PKS_dehydratase.
IPR020843. PKS_ER.
IPR013968. PKS_KR.
IPR020806. PKS_PP-bd.
IPR015083. Polyketide_synth_docking.
IPR006162. PPantetheine_attach_site.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
PfamPF00698. Acyl_transf_1. 1 hit.
PF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
PF08990. Docking. 1 hit.
PF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
PF08659. KR. 1 hit.
PF00550. PP-binding. 1 hit.
[Graphical view]
SMARTSM00827. PKS_AT. 1 hit.
SM00826. PKS_DH. 1 hit.
SM00829. PKS_ER. 1 hit.
SM00822. PKS_KR. 1 hit.
SM00825. PKS_KS. 1 hit.
SM00823. PKS_PP. 1 hit.
[Graphical view]
SUPFAMSSF101173. SSF101173. 1 hit.
SSF47336. SSF47336. 1 hit.
SSF50129. SSF50129. 1 hit.
SSF52151. SSF52151. 2 hits.
SSF53901. SSF53901. 1 hit.
SSF55048. SSF55048. 1 hit.
PROSITEPS50075. ACP_DOMAIN. 1 hit.
PS00606. B_KETOACYL_SYNTHASE. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMSL7_MYCBO
AccessionPrimary (citable) accession number: Q7TXK8
Secondary accession number(s): X2BMA9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 5, 2011
Last sequence update: October 1, 2003
Last modified: June 11, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways