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Q7TXK8

- MSL7_MYCBO

UniProt

Q7TXK8 - MSL7_MYCBO

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Protein

Phenolphthiocerol synthesis polyketide synthase type I Pks15/1

Gene

pks15/1

Organism
Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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).1 Publication

Catalytic activityi

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

Cofactori

Binds 1 phosphopantetheine covalently.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei216 – 2161For beta-ketoacyl synthase activityPROSITE-ProRule annotation
Active sitei670 – 6701For acyltransferase activityPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1536 – 155318NADPBy similarityAdd
BLAST
Nucleotide bindingi1725 – 174016NADPBy similarityAdd
BLAST

GO - Molecular functioni

  1. 3-oxoacyl-[acyl-carrier-protein] synthase activity Source: UniProtKB-EC
  2. cofactor binding Source: InterPro
  3. oxidoreductase activity Source: InterPro
  4. phosphopantetheine binding Source: InterPro
  5. zinc ion binding Source: InterPro

GO - Biological processi

  1. Actinobacterium-type cell wall biogenesis Source: UniProtKB
  2. fatty acid biosynthetic process Source: UniProtKB-UniPathway
  3. lipid biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17228.
UniPathwayiUPA00094.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:pks15/1
Synonyms:msl7, pks1
Ordered Locus Names:Mb2971c
OrganismiMycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Taxonomic identifieri233413 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
ProteomesiUP000001419: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. polyketide synthase complex Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

Disruption of pks15/1 abolishes the production of phenolphthiocerol.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 21122112Phenolphthiocerol synthesis polyketide synthase type I Pks15/1PRO_0000406362Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2045 – 20451O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Interactioni

Protein-protein interaction databases

STRINGi233413.Mb2971c.

Structurei

3D structure databases

ProteinModelPortaliQ7TXK8.
SMRiQ7TXK8. Positions 18-921.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2012 – 208271Acyl carrierPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni42 – 471430Beta-ketoacyl synthaseBy similarityAdd
BLAST
Regioni579 – 893315AcyltransferaseBy similarityAdd
BLAST
Regioni941 – 1101161DehydrataseBy similarityAdd
BLAST
Regioni1406 – 1711306EnoylreductaseBy similarityAdd
BLAST
Regioni1724 – 1905182Beta-ketoacyl reductaseBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the beta-ketoacyl-ACP synthases family.Curated
Contains 1 acyl carrier domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG3321.
HOGENOMiHOG000046292.
KOiK12430.
OMAiHAHAVES.
OrthoDBiEOG6QP0WP.

Family and domain databases

Gene3Di1.10.1200.10. 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.
InterProiIPR001227. 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]
PfamiPF00698. 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]
SMARTiSM00827. 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]
SUPFAMiSSF101173. SSF101173. 1 hit.
SSF47336. SSF47336. 1 hit.
SSF50129. SSF50129. 1 hit.
SSF52151. SSF52151. 2 hits.
SSF53901. SSF53901. 1 hit.
SSF55048. SSF55048. 1 hit.
PROSITEiPS50075. ACP_DOMAIN. 1 hit.
PS00606. B_KETOACYL_SYNTHASE. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7TXK8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MIEEQRTMSV EGADQQSEKL FHYLKKVAVE LDETRARLRE YEQRATEPVA
60 70 80 90 100
VVGIGCRFPG GVDGPDGLWD VVSAGRDVVS EFPTDRGWDV EGLYDPDPDA
110 120 130 140 150
EGKTYTRWGA FLDDATGFDA GFFGIAPSEV LAMDPQQRLM LEVSWEALEH
160 170 180 190 200
AGIDPLSLRG SATGVYTGIF AASYGNRDTG GLQGYGLTGT SISVASGRVS
210 220 230 240 250
YVLGLQGPAV SVDTACSSSL VAIHWAMSSL RSGECDLALA GGVTVMGLPS
260 270 280 290 300
IFVGFSRQRG LAADGRCKAF AAAADGTGWG EGAGVVVLER LSDARRLGHS
310 320 330 340 350
VLAVVRGSAV NQDGASNGLT APNGLAQQRV IQAALANAGL SAADVDVVEA
360 370 380 390 400
HGTATTLGDP IEAQALLSTY GQGRPAEQPL WVGSIKSNMG HTQAAAGVAG
410 420 430 440 450
VIKMVQAMRH GVMPATLHVD EPSPRVDWTS GAVSVLTEAR EWSVDGRPRR
460 470 480 490 500
AAVSSFGISG TNAHLILEEA PVPAPAEAPV EASESTGGPR PSMVPWVISA
510 520 530 540 550
RSAEALTAQA GRLMAHVQAN PGLDPIDVGC SLASRSVFEH RAVVVGASRE
560 570 580 590 600
QLIAGLAGLA AGEPGAGVAV GQPGSVGKTV VVFPGQGAQR IGMGRELYGE
610 620 630 640 650
LPVFAQAFDA VADELDRHLR LPLRDVIWGA DADLLDSTEF AQPALFAVEV
660 670 680 690 700
ASFAVLRDWG VLPDFVMGHS VGELAAAHAA GVLTLADAAM LVVARGRLMQ
710 720 730 740 750
ALPAGGAMVA VAASEDEVEP LLGEGVGIAA INAPESVVIS GAQAAANAIA
760 770 780 790 800
DRFAAQGRRV HQLAVSHAFH SPLMEPMLEE FARVAARVQA REPQLGLVSN
810 820 830 840 850
VTGELAGPDF GSAQYWVDHV RRPVRFADSA RHLQTLGATH FIEAGPGSGL
860 870 880 890 900
TGSIEQSLAP AEAMVVSMLG KDRPELASAL GAAGQVFTTG VPVQWSAVFA
910 920 930 940 950
GSGGRRVQLP TYAFQRRRFW ETPGADGPAD AAGLGLGATE HALLGAVVER
960 970 980 990 1000
PDSDEVVLTG RLSLADQPWL ADHVVNGVVL FPGAGFVELV IRAGDEVGCA
1010 1020 1030 1040 1050
LIEELVLAAP LVMHPGVGVQ VQVVVGAADE SGHRAVSVYS RGDQSQGWLL
1060 1070 1080 1090 1100
NAEGMLGVAA AETPMDLSVW PPEGAESVDI SDGYAQLAER GYAYGPAFQG
1110 1120 1130 1140 1150
LVAIWRRGSE LFAEVVAPGE AGVAVDRMGM HPAVLDAVLH ALGLAVEKTQ
1160 1170 1180 1190 1200
ASTETRLPFC WRGVSLHAGG AGRVRARFAS AGADAISVDV CDATGLPVLT
1210 1220 1230 1240 1250
VRSLVTRPIT AEQLRAAVTA AGGASDQGPL EVVWSPISVV SGGANGSAPP
1260 1270 1280 1290 1300
APVSWADFCA GSDGDASVVV WELESAGGQA SSVVGSVYAA THTALEVLQS
1310 1320 1330 1340 1350
WLGADRAATL VVLTHGGVGL AGEDISDLAA AAVWGMARSA QAENPGRIVL
1360 1370 1380 1390 1400
IDTDAAVDAS VLAGVGEPQL LVRGGTVHAP RLSPAPALLA LPAAESAWRL
1410 1420 1430 1440 1450
AAGGGGTLED LVIQPCPEVQ APLQAGQVRV AVAAVGVNFR DVVAALGMYP
1460 1470 1480 1490 1500
GQAPPLGAEG AGVVLETGPE VTDLAVGDAV MGFLGGAGPL AVVDQQLVTR
1510 1520 1530 1540 1550
VPQGWSFAQA AAVPVVFLTA WYGLADLAEI KAGESVLIHA GTGGVGMAAV
1560 1570 1580 1590 1600
QLARQWGVEV FVTASRGKWD TLRAMGFDDD HIGDSRTCEF EEKFLAVTEG
1610 1620 1630 1640 1650
RGVDVVLDSL AGEFVDASLR LLVRGGRFLE MGKTDIRDAQ EIAANYPGVQ
1660 1670 1680 1690 1700
YRAFDLSEAG PARMQEMLAE VRELFDTREL HRLPVTTWDV RCAPAAFRFM
1710 1720 1730 1740 1750
SQARHIGKVV LTMPSALADR LADGTVVITG ATGAVGGVLA RHLVGAYGVR
1760 1770 1780 1790 1800
HLVLASRRGD RAEGAAELAA DLTEAGAKGQ VVACDVADRA AVAGLFAQLS
1810 1820 1830 1840 1850
REYPPVRGVI HAAGVLDDAV ITSLTPDRID TVLRAKVDAA WNLHQATSDL
1860 1870 1880 1890 1900
DLSMFVLCSS IAATVGSPGQ GNYSAANAFL DGLAAHRQAA GLAGISLAWG
1910 1920 1930 1940 1950
LWEQPGGMTA HLSSRDLARM SRSGLAPMSP AEAVELFDAA LAIDHPLAVA
1960 1970 1980 1990 2000
TLLDRAALDA RAQAGALPAL FSGLARRPRR RQIDDTGDAT SSKSALAQRL
2010 2020 2030 2040 2050
HGLAADEQLE LLVGLVCLQA AAVLGRPSAE DVDPDTEFGD LGFDSLTAVE
2060 2070 2080 2090 2100
LRNRLKTATG LTLPPTVIFD HPTPTAVAEY VAQQMSGSRP TESGDPTSQV
2110
VEPAAAEVSV HA
Length:2,112
Mass (Da):218,304
Last modified:October 1, 2003 - v1
Checksum:iDCB5FA31A58A2785
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX248333 Genomic DNA. Translation: CDO44238.1.
RefSeqiNP_856616.1. NC_002945.3.

Genome annotation databases

EnsemblBacteriaiCAD96658; CAD96658; Mb2971c.
GeneIDi1092134.
KEGGimbo:Mb2971c.
PATRICi18008262. VBIMycBov88188_3263.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX248333 Genomic DNA. Translation: CDO44238.1 .
RefSeqi NP_856616.1. NC_002945.3.

3D structure databases

ProteinModelPortali Q7TXK8.
SMRi Q7TXK8. Positions 18-921.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 233413.Mb2971c.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAD96658 ; CAD96658 ; Mb2971c .
GeneIDi 1092134.
KEGGi mbo:Mb2971c.
PATRICi 18008262. VBIMycBov88188_3263.

Phylogenomic databases

eggNOGi COG3321.
HOGENOMi HOG000046292.
KOi K12430.
OMAi HAHAVES.
OrthoDBi EOG6QP0WP.

Enzyme and pathway databases

UniPathwayi UPA00094 .
BioCyci MetaCyc:MONOMER-17228.

Family and domain databases

Gene3Di 1.10.1200.10. 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.
InterProi IPR001227. 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 ]
Pfami PF00698. 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 ]
SMARTi SM00827. 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 ]
SUPFAMi SSF101173. SSF101173. 1 hit.
SSF47336. SSF47336. 1 hit.
SSF50129. SSF50129. 1 hit.
SSF52151. SSF52151. 2 hits.
SSF53901. SSF53901. 1 hit.
SSF55048. SSF55048. 1 hit.
PROSITEi PS50075. ACP_DOMAIN. 1 hit.
PS00606. B_KETOACYL_SYNTHASE. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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.

Entry informationi

Entry nameiMSL7_MYCBO
AccessioniPrimary (citable) accession number: Q7TXK8
Secondary accession number(s): X2BMA9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 5, 2011
Last sequence update: October 1, 2003
Last modified: October 1, 2014
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3