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Q7TXL6

- PPSE_MYCBO

UniProt

Q7TXL6 - PPSE_MYCBO

Protein

Phthiocerol/phenolphthiocerol synthesis polyketide synthase type I PpsE

Gene

ppsE

Organism
Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 78 (01 Oct 2014)
      Sequence version 1 (01 Oct 2003)
      Previous versions | rss
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    Functioni

    Involved in the elongation of either C22-24 fatty acids or p-hydroxyphenylalkanoic acids by the addition of malonyl-CoA and methylmalonyl-CoA extender units to yield phthiocerol and phenolphthiocerol derivatives, respectively.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 phosphopantetheines covalently.By similarity
    NADP.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei184 – 1841For beta-ketoacyl synthase activityPROSITE-ProRule annotation
    Active sitei641 – 6411For malonyltransferase activityPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi1286 – 133146NADPBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. 3-oxoacyl-[acyl-carrier-protein] synthase activity Source: UniProtKB-EC
    2. oxidoreductase activity Source: UniProtKB-KW

    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

    Keywords - Molecular functioni

    Oxidoreductase, Transferase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    UniPathwayiUPA00094.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phthiocerol/phenolphthiocerol synthesis polyketide synthase type I PpsE
    Alternative name(s):
    Beta-ketoacyl-acyl-carrier-protein synthase I (EC:2.3.1.41)
    Gene namesi
    Name:ppsE
    Ordered Locus Names:Mb2960
    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

    Pathology & Biotechi

    Disruption phenotypei

    Cells lacking this genes abolish the biosynthesis of phthiocerol/phenolphthiocerol dimycocerosate (DIM) and decreased the efficiency with which bacteria infected macrophages derived from monocytes (MDMs).1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 14881488Phthiocerol/phenolphthiocerol synthesis polyketide synthase type I PpsEPRO_0000406951Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei965 – 9651O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation

    Keywords - PTMi

    Phosphopantetheine, Phosphoprotein

    Interactioni

    Protein-protein interaction databases

    STRINGi233413.Mb2960.

    Structurei

    3D structure databases

    ProteinModelPortaliQ7TXL6.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini935 – 100167Acyl carrierPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni6 – 389384Beta-ketoacyl synthaseBy similarityAdd
    BLAST
    Regioni551 – 868318AcyltransferaseBy similarityAdd
    BLAST

    Sequence similaritiesi

    Contains 1 acyl carrier domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG1020.
    HOGENOMiHOG000046292.
    KOiK12444.
    OMAiFDECATA.
    OrthoDBiEOG6QP0WP.

    Family and domain databases

    Gene3Di1.10.1200.10. 1 hit.
    3.40.366.10. 2 hits.
    3.40.47.10. 2 hits.
    InterProiIPR001227. Ac_transferase_dom.
    IPR009081. Acyl_carrier_prot-like.
    IPR014043. Acyl_transferase.
    IPR016035. Acyl_Trfase/lysoPLipase.
    IPR001242. Condensatn.
    IPR018201. Ketoacyl_synth_AS.
    IPR014031. Ketoacyl_synth_C.
    IPR014030. Ketoacyl_synth_N.
    IPR016036. Malonyl_transacylase_ACP-bd.
    IPR020801. PKS_acyl_transferase.
    IPR016039. Thiolase-like.
    IPR016038. Thiolase-like_subgr.
    [Graphical view]
    PfamiPF00698. Acyl_transf_1. 1 hit.
    PF00668. Condensation. 1 hit.
    PF00109. ketoacyl-synt. 1 hit.
    PF02801. Ketoacyl-synt_C. 1 hit.
    PF00550. PP-binding. 1 hit.
    [Graphical view]
    SMARTiSM00827. PKS_AT. 1 hit.
    [Graphical view]
    SUPFAMiSSF47336. SSF47336. 1 hit.
    SSF52151. SSF52151. 2 hits.
    SSF53901. SSF53901. 3 hits.
    SSF55048. SSF55048. 1 hit.
    PROSITEiPS50075. ACP_DOMAIN. 1 hit.
    PS00606. B_KETOACYL_SYNTHASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q7TXL6-1 [UniParc]FASTAAdd to Basket

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    MSIPENAIAV VGMAGRFPGA KDVSAFWSNL RRGKESIVTL SEQELRDAGV     50
    SDKTLADPAY VRRAPLLDGI DEFDAGFFGF PPLAAQVLDP QHRLFLQCAW 100
    HALEDAGADP ARFDGSIGVY GTSSPSGYLL HNLLSHRDPN AVLAEGLNFD 150
    QFSLFLQNDK DFLATRISHA FNLRGPSIAV QTACSSSLVA VHLACLSLLS 200
    GECDMALAGG SSLCIPHRVG YFTSPGSMVS AVGHCRPFDV RADGTVFGSG 250
    VGLVVLKPLA AAIDAGDRIH AVIRGSAINN DGSAKMGYAA PNPAAQADVI 300
    AEAHAVSGID SSTVSYVECH GTGTPLGDPI EIQGLRAAFE VSQTSRSAPC 350
    VLGSVKSNIG HLEVAAGIAG LIKTILCLKN KALPATLHYT SPNPELRLDQ 400
    SPFVVQSKYG PWECDGVRRA GVSSFGVGGT NAHVVLEEAP AEASEVSAHA 450
    EPAGPQVILL SAQTAAALGE SRTALAAALE TQDGPRLSDV AYTLARRRKH 500
    NVTMAAVVHD REHAATVLRA AEHDNVFVGE AAHDGEHGDR ADAAPTSDRV 550
    VFLFPGQGAQ HVGMAKGLYD TEPVFAQHFD TCAAGFRDET GIDLHAEVFD 600
    GTATDLERID RSQPALFTVE YALAKLVDTF GVRAGAYIGY STGEYIAATL 650
    AGVFDLQTAI KTVSLRARLM HESPPGAMVA VALGPDDVTQ YLPPEVELSA 700
    VNDPGNCVVA GPKDQIRALR QRLTEAGIPV RRVRATHAFH TSAMDPMLGQ 750
    FQEFLSRQQL RPPRTPLLSN LTGSWMSDQQ VVDPASWTRQ ISSPIRFADE 800
    LDVVLAAPSR ILVEVGPGGS LTGSAMRHPK WSTTHRTVRL MRHPLQDVDD 850
    RDTFLRALGE LWSAGVEVDW TPRRPAVPHL VSLPGYPFAR QRHWVEPNHT 900
    VWAQAPGANN GSPAGTADGS TAATVDAARN GESQTEVTLQ RIWSQCLGVS 950
    SVDRNANFFD LGGDSLMAIS IAMAAANEGL TITPQDLYEY PTLASLTAAV 1000
    DASFASSGLA KPPEAQANPA VPPNVTYFLD RGLRDTGRCR VPLILRLDPK 1050
    IGLPDIRAVL TAVVNHHDAL RLHLVGNDGI WEQHIAAPAE FTGLSNRSVP 1100
    DGVAAGSPEE RAAVLGILAE LLEDQTDPNA PLAAVHIAAA HGGPHYLCLA 1150
    IHAMVTDDSS RQILATDIVT AFGQRLAGEE ITLEPVSTGW REWSLRCAAL 1200
    ATHPAALDTR SYWIENSTKA TLWLADALPN AHTAHPPRAD ELTKLSSTLS 1250
    VEQTSELDDG RRRFRRSIQT ILLAALGRTI AQTVGEGVVA VELEGEGRSV 1300
    LRPDVDLRRT VGWFTTYYPV PLACATGLGA LAQLDAVHNT LKSVPHYGIG 1350
    YGLLRYVYAP TGRVLGAQRT PDIHFRYAGV IPELPSGDAP VQFDSDMTLP 1400
    VREPIPGMGH AIELRVYRFG GSLHLDWWYD TRRIPAATAE ALERTFPLAL 1450
    SALIQEAIAA EHTEHDDSEI VGEPEAGALV DLSSMDAG 1488
    Length:1,488
    Mass (Da):158,746
    Last modified:October 1, 2003 - v1
    Checksum:i14EC40432DB7F502
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX248333 Genomic DNA. Translation: CDO44227.1.
    RefSeqiNP_856605.1. NC_002945.3.

    Genome annotation databases

    EnsemblBacteriaiCAD96647; CAD96647; Mb2960.
    GeneIDi1092146.
    KEGGimbo:Mb2960.
    PATRICi18008232. VBIMycBov88188_3248.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX248333 Genomic DNA. Translation: CDO44227.1 .
    RefSeqi NP_856605.1. NC_002945.3.

    3D structure databases

    ProteinModelPortali Q7TXL6.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 233413.Mb2960.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAD96647 ; CAD96647 ; Mb2960 .
    GeneIDi 1092146.
    KEGGi mbo:Mb2960.
    PATRICi 18008232. VBIMycBov88188_3248.

    Phylogenomic databases

    eggNOGi COG1020.
    HOGENOMi HOG000046292.
    KOi K12444.
    OMAi FDECATA.
    OrthoDBi EOG6QP0WP.

    Enzyme and pathway databases

    UniPathwayi UPA00094 .

    Family and domain databases

    Gene3Di 1.10.1200.10. 1 hit.
    3.40.366.10. 2 hits.
    3.40.47.10. 2 hits.
    InterProi IPR001227. Ac_transferase_dom.
    IPR009081. Acyl_carrier_prot-like.
    IPR014043. Acyl_transferase.
    IPR016035. Acyl_Trfase/lysoPLipase.
    IPR001242. Condensatn.
    IPR018201. Ketoacyl_synth_AS.
    IPR014031. Ketoacyl_synth_C.
    IPR014030. Ketoacyl_synth_N.
    IPR016036. Malonyl_transacylase_ACP-bd.
    IPR020801. PKS_acyl_transferase.
    IPR016039. Thiolase-like.
    IPR016038. Thiolase-like_subgr.
    [Graphical view ]
    Pfami PF00698. Acyl_transf_1. 1 hit.
    PF00668. Condensation. 1 hit.
    PF00109. ketoacyl-synt. 1 hit.
    PF02801. Ketoacyl-synt_C. 1 hit.
    PF00550. PP-binding. 1 hit.
    [Graphical view ]
    SMARTi SM00827. PKS_AT. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47336. SSF47336. 1 hit.
    SSF52151. SSF52151. 2 hits.
    SSF53901. SSF53901. 3 hits.
    SSF55048. SSF55048. 1 hit.
    PROSITEi PS50075. ACP_DOMAIN. 1 hit.
    PS00606. B_KETOACYL_SYNTHASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-935 / AF2122/97.
    2. "Phthiocerol dimycocerosates of M. tuberculosis participate in macrophage invasion by inducing changes in the organization of plasma membrane lipids."
      Astarie-Dequeker C., Le Guyader L., Malaga W., Seaphanh F.K., Chalut C., Lopez A., Guilhot C.
      PLoS Pathog. 5:E1000289-E1000289(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN THE PHTHIOCEROL AND PHENOLPHTHIOCEROL BIOSYNTHESIS, DISRUPTION PHENOTYPE.
      Strain: BCG / Pasteur.

    Entry informationi

    Entry nameiPPSE_MYCBO
    AccessioniPrimary (citable) accession number: Q7TXL6
    Secondary accession number(s): X2BLX7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 5, 2011
    Last sequence update: October 1, 2003
    Last modified: October 1, 2014
    This is version 78 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