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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, msl7, pks1, Mb2971c
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].

Cofactori

Binds 1 phosphopantetheine covalently By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei216 – 2161For beta-ketoacyl synthase activity By similarity
Active sitei670 – 6701For acyltransferase activity By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1536 – 155318NADP By similarityAdd
BLAST
Nucleotide bindingi1725 – 174016NADP By 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)serine By similarity

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Interactioni

Protein-protein interaction databases

STRINGi233413.Mb2971c.

Structurei

3D structure databases

ProteinModelPortaliQ7TXK8.
SMRiQ7TXK8. Positions 18-921.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2012 – 208271Acyl carrierAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni42 – 471430Beta-ketoacyl synthase By similarityAdd
BLAST
Regioni579 – 893315Acyltransferase By similarityAdd
BLAST
Regioni941 – 1101161Dehydratase By similarityAdd
BLAST
Regioni1406 – 1711306Enoylreductase By similarityAdd
BLAST
Regioni1724 – 1905182Beta-ketoacyl reductase By similarityAdd
BLAST

Sequence similaritiesi

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

MIEEQRTMSV EGADQQSEKL FHYLKKVAVE LDETRARLRE YEQRATEPVA     50
VVGIGCRFPG GVDGPDGLWD VVSAGRDVVS EFPTDRGWDV EGLYDPDPDA 100
EGKTYTRWGA FLDDATGFDA GFFGIAPSEV LAMDPQQRLM LEVSWEALEH 150
AGIDPLSLRG SATGVYTGIF AASYGNRDTG GLQGYGLTGT SISVASGRVS 200
YVLGLQGPAV SVDTACSSSL VAIHWAMSSL RSGECDLALA GGVTVMGLPS 250
IFVGFSRQRG LAADGRCKAF AAAADGTGWG EGAGVVVLER LSDARRLGHS 300
VLAVVRGSAV NQDGASNGLT APNGLAQQRV IQAALANAGL SAADVDVVEA 350
HGTATTLGDP IEAQALLSTY GQGRPAEQPL WVGSIKSNMG HTQAAAGVAG 400
VIKMVQAMRH GVMPATLHVD EPSPRVDWTS GAVSVLTEAR EWSVDGRPRR 450
AAVSSFGISG TNAHLILEEA PVPAPAEAPV EASESTGGPR PSMVPWVISA 500
RSAEALTAQA GRLMAHVQAN PGLDPIDVGC SLASRSVFEH RAVVVGASRE 550
QLIAGLAGLA AGEPGAGVAV GQPGSVGKTV VVFPGQGAQR IGMGRELYGE 600
LPVFAQAFDA VADELDRHLR LPLRDVIWGA DADLLDSTEF AQPALFAVEV 650
ASFAVLRDWG VLPDFVMGHS VGELAAAHAA GVLTLADAAM LVVARGRLMQ 700
ALPAGGAMVA VAASEDEVEP LLGEGVGIAA INAPESVVIS GAQAAANAIA 750
DRFAAQGRRV HQLAVSHAFH SPLMEPMLEE FARVAARVQA REPQLGLVSN 800
VTGELAGPDF GSAQYWVDHV RRPVRFADSA RHLQTLGATH FIEAGPGSGL 850
TGSIEQSLAP AEAMVVSMLG KDRPELASAL GAAGQVFTTG VPVQWSAVFA 900
GSGGRRVQLP TYAFQRRRFW ETPGADGPAD AAGLGLGATE HALLGAVVER 950
PDSDEVVLTG RLSLADQPWL ADHVVNGVVL FPGAGFVELV IRAGDEVGCA 1000
LIEELVLAAP LVMHPGVGVQ VQVVVGAADE SGHRAVSVYS RGDQSQGWLL 1050
NAEGMLGVAA AETPMDLSVW PPEGAESVDI SDGYAQLAER GYAYGPAFQG 1100
LVAIWRRGSE LFAEVVAPGE AGVAVDRMGM HPAVLDAVLH ALGLAVEKTQ 1150
ASTETRLPFC WRGVSLHAGG AGRVRARFAS AGADAISVDV CDATGLPVLT 1200
VRSLVTRPIT AEQLRAAVTA AGGASDQGPL EVVWSPISVV SGGANGSAPP 1250
APVSWADFCA GSDGDASVVV WELESAGGQA SSVVGSVYAA THTALEVLQS 1300
WLGADRAATL VVLTHGGVGL AGEDISDLAA AAVWGMARSA QAENPGRIVL 1350
IDTDAAVDAS VLAGVGEPQL LVRGGTVHAP RLSPAPALLA LPAAESAWRL 1400
AAGGGGTLED LVIQPCPEVQ APLQAGQVRV AVAAVGVNFR DVVAALGMYP 1450
GQAPPLGAEG AGVVLETGPE VTDLAVGDAV MGFLGGAGPL AVVDQQLVTR 1500
VPQGWSFAQA AAVPVVFLTA WYGLADLAEI KAGESVLIHA GTGGVGMAAV 1550
QLARQWGVEV FVTASRGKWD TLRAMGFDDD HIGDSRTCEF EEKFLAVTEG 1600
RGVDVVLDSL AGEFVDASLR LLVRGGRFLE MGKTDIRDAQ EIAANYPGVQ 1650
YRAFDLSEAG PARMQEMLAE VRELFDTREL HRLPVTTWDV RCAPAAFRFM 1700
SQARHIGKVV LTMPSALADR LADGTVVITG ATGAVGGVLA RHLVGAYGVR 1750
HLVLASRRGD RAEGAAELAA DLTEAGAKGQ VVACDVADRA AVAGLFAQLS 1800
REYPPVRGVI HAAGVLDDAV ITSLTPDRID TVLRAKVDAA WNLHQATSDL 1850
DLSMFVLCSS IAATVGSPGQ GNYSAANAFL DGLAAHRQAA GLAGISLAWG 1900
LWEQPGGMTA HLSSRDLARM SRSGLAPMSP AEAVELFDAA LAIDHPLAVA 1950
TLLDRAALDA RAQAGALPAL FSGLARRPRR RQIDDTGDAT SSKSALAQRL 2000
HGLAADEQLE LLVGLVCLQA AAVLGRPSAE DVDPDTEFGD LGFDSLTAVE 2050
LRNRLKTATG LTLPPTVIFD HPTPTAVAEY VAQQMSGSRP TESGDPTSQV 2100
VEPAAAEVSV HA 2112
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: June 11, 2014
This is version 84 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

Similar proteinsi