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P96202

- PPSC_MYCTU

UniProt

P96202 - PPSC_MYCTU

Protein

Phthiocerol synthesis polyketide synthase type I PpsC

Gene

ppsC

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 2 (01 Aug 1998)
      Previous versions | rss
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    Functioni

    Involved in the elongation of either C22-24 fatty acids by the addition of malonyl-CoA and methylmalonyl-CoA extender units to yield phthiocerol derivatives.By similarity

    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 sitei210 – 2101For beta-ketoacyl synthase activityPROSITE-ProRule annotation
    Active sitei660 – 6601For malonyltransferase activityPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi1803 – 184846NADPBy similarityAdd
    BLAST

    GO - Molecular functioni

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

    GO - Biological processi

    1. Actinobacterium-type cell wall biogenesis Source: UniProtKB
    2. DIM/DIP cell wall layer assembly Source: MTBBASE
    3. fatty acid biosynthetic process Source: MTBBASE
    4. phenolic phthiocerol biosynthetic process Source: UniProtKB
    5. phthiocerol biosynthetic process Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase, Transferase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciMTBRV:RV2933-MONOMER.
    UniPathwayiUPA00094.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phthiocerol synthesis polyketide synthase type I PpsC
    Alternative name(s):
    Beta-ketoacyl-acyl-carrier-protein synthase I (EC:2.3.1.41)
    Gene namesi
    Name:ppsC
    Ordered Locus Names:Rv2933
    OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
    Taxonomic identifieri83332 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
    ProteomesiUP000001584: Chromosome

    Organism-specific databases

    TubercuListiRv2933.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: MTBBASE
    2. plasma membrane Source: MTBBASE
    3. polyketide synthase complex Source: UniProtKB

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 21882187Phthiocerol synthesis polyketide synthase type I PpsCPRO_0000406948Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylthreonine1 Publication
    Modified residuei2105 – 21051O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation

    Keywords - PTMi

    Acetylation, Phosphopantetheine, Phosphoprotein

    Proteomic databases

    PRIDEiP96202.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi83332.Rv2933.

    Structurei

    Secondary structure

    1
    2188
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi1572 – 158817
    Beta strandi1598 – 16014
    Turni1602 – 16054
    Helixi1607 – 161913
    Beta strandi1622 – 16298
    Helixi1630 – 16378
    Beta strandi1642 – 16465
    Helixi1652 – 16598
    Turni1660 – 16623
    Beta strandi1665 – 16706
    Helixi1675 – 16828
    Beta strandi1684 – 16929
    Helixi1696 – 16983
    Turni1699 – 17013
    Beta strandi1703 – 17053
    Helixi1706 – 17094
    Turni1710 – 17123
    Beta strandi1714 – 17174
    Helixi1720 – 17267
    Helixi1728 – 174316

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1PQWX-ray2.66A/B1559-1755[»]
    ProteinModelPortaliP96202.
    SMRiP96202. Positions 1571-1753.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP96202.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2070 – 214273Acyl carrierPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni37 – 465429Beta-ketoacyl synthaseBy similarityAdd
    BLAST
    Regioni572 – 890319AcyltransferaseBy similarityAdd
    BLAST
    Regioni928 – 1093166DehydrataseBy similarityAdd
    BLAST
    Regioni1467 – 1778312EnoylreductaseBy similarityAdd
    BLAST
    Regioni1802 – 1981180Beta-ketoacyl reductaseBy similarityAdd
    BLAST

    Sequence similaritiesi

    Contains 1 acyl carrier domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG3321.
    HOGENOMiHOG000046292.
    KOiK12442.
    OMAiWCSESEG.
    OrthoDBiEOG6QP0WP.
    PhylomeDBiP96202.

    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.
    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.
    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]
    SUPFAMiSSF47336. SSF47336. 1 hit.
    SSF50129. SSF50129. 1 hit.
    SSF52151. SSF52151. 2 hits.
    SSF53901. SSF53901. 2 hits.
    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P96202-1 [UniParc]FASTAAdd to Basket

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    MTAATPDRRA IITEALHKID DLTARLEIAE KSSSEPIAVI GMGCRFPGGV     50
    NNPEQFWDLL CAGRSGIVRV PAQRWDADAY YCDDHTVPGT ICSTEGGFLT 100
    SWQPDEFDAE FFSISPREAA AMDPQQRLLI EVAWEALEDA GVPQHTIRGT 150
    QTSVFVGVTA YDYMLTLAGR LRPVDLDAYI PTGNSANFAA GRLAYILGAR 200
    GPAVVIDTAC SSSLVAVHLA CQSLRGRESD MALVGGTNLL LSPGPSIACS 250
    RWGMLSPEGR CKTFDASADG YVRGEGAAVV VLKRLDDAVR DGNRILAVVR 300
    GSAVNQDGAS SGVTVPNGPA QQALLAKALT SSKLTAADID YVEAHGTGTP 350
    LGDPIELDSL SKVFSDRAGS DQLVIGSVKT NLGHLEAAAG VAGLMKAVLA 400
    VHNGYIPRHL NFHQLTPHAS EAASRLRIAA DGIDWPTTGR PRRAGVSSFG 450
    VSGTNAHVVI EQAPDPMAAA GTEPQRGPVP AVSTLVVFGK TAPRVAATAS 500
    VLADWLDGPG AAVPLADVAH TLNHHRARQT RFGTVAAVDR RQAVIGLRAL 550
    AAGQSAPGVV APREGSIGGG TVFVYSGRGS QWAGMGRQLL ADEPAFAAAI 600
    AELEPEFVAQ GGFSLRDVIA GGKELVGIEQ IQLGLIGMQL ALTALWRSYG 650
    VTPDAVIGHS MGEVAAAVVA GALTPAQGLR VTAVRSRLMA PLSGQGTMAL 700
    LELDAEATEA LIADYPEVSL GIYASPRQTV ISGPPLLIDE LIDKVRQQNG 750
    FATRVNIEVA PHNPAMDALQ PAMRSELADL TPQPPTIPII STTYADLGIS 800
    LGSGPRFDAE HWATNMRNPV RFHQAIAHAG ADHHTFIEIS AHPLLTHSIS 850
    DTLRASYDVD NYLSIGTLQR DAHDTLEFHT NLNTTHTTHP PQTPHPPEPH 900
    PVLPTTPWQH TQHWITATSA AYHRPDTHPL LGVGVTDPTN GTRVWESELD 950
    PDLLWLADHV IDDLVVLPGA AYAEIALAAA TDTFAVEQDQ PWMISELDLR 1000
    QMLHVTPGTV LVTTLTGDEQ RCQVEIRTRS GSSGWTTHAT ATVARAEPLA 1050
    PLDHEGQRRE VTTADLEDQL DPDDLYQRLR GAGQQHGPAF QGIVGLAVTQ 1100
    AGVARAQVRL PASARTGSRE FMLHPVMMDI ALQTLGATRT ATDLAGGQDA 1150
    RQGPSSNSAL VVPVRFAGVH VYGDITRGVR AVGSLAAAGD RLVGEVVLTD 1200
    ANGQPLLVVD EVEMAVLGSG SGATELTNRL FMLEWEPAPL EKTAEATGAL 1250
    LLIGDPAAGD PLLPALQSSL RDRITDLELA SAADEATLRA AISRTSWDGI 1300
    VVVCPPRAND ESMPDEAQLE LARTRTLLVA SVVETVTRMG ARKSPRLWIV 1350
    TRGAAQFDAG ESVTLAQTGL RGIARVLTFE HSELNTTLVD IEPDGTGSLA 1400
    ALAEELLAGS EADEVALRDG QRYVNRLVPA PTTTSGDLAA EARHQVVNLD 1450
    SSGASRAAVR LQIDQPGRLD ALNVHEVKRG RPQGDQVEVR VVAAGLNFSD 1500
    VLKAMGVYPG LDGAAPVIGG ECVGYVTAIG DEVDGVEVGQ RVIAFGPGTF 1550
    GTHLGTIADL VVPIPDTLAD NEAATFGVAY LTAWHSLCEV GRLSPGERVL 1600
    IHSATGGVGM AAVSIAKMIG ARIYTTAGSD AKREMLSRLG VEYVGDSRSV 1650
    DFADEILELT DGYGVDVVLN SLAGEAIQRG VQILAPGGRF IELGKKDVYA 1700
    DASLGLAALA KSASFSVVDL DLNLKLQPAR YRQLLQHILQ HVADGKLEVL 1750
    PVTAFSLHDA ADAFRLMASG KHTGKIVISI PQHGSIEAIA APPPLPLVSR 1800
    DGGYLIVGGM GGLGFVVARW LAEQGAGLIV LNGRSAPSDE VAAAIAELNA 1850
    SGSRIEVITG DITEPDTAER LVRAVEDAGF RLAGVVHSAM VLADEIVLNM 1900
    TDSAARRVFA PKVTGSWRLH VATAARDVDW WLTFSSAAAL LGTPGQGAYA 1950
    AANSWVDGLV AHRRSAGLPA VGINWGPWAD VGRAQFFKDL GVEMINAEQG 2000
    LAAMQAVLTA DRGRTGVFSL DARQWFQSFP AVAGSSLFAK LHDSAARKSG 2050
    QRRGGGAIRA QLDALDAAER PGHLASAIAD EIRAVLRSGD PIDHHRPLET 2100
    LGLDSLMGLE LRNRLEASLG ITLPVALVWA YPTISDLATA LCERMDYATP 2150
    AAAQEISDTE PELSDEEMDL LADLVDASEL EAATRGES 2188
    Length:2,188
    Mass (Da):230,622
    Last modified:August 1, 1998 - v2
    Checksum:i3C431C011F01F1A2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL123456 Genomic DNA. Translation: CCP45736.1.
    PIRiA70984.
    RefSeqiNP_217449.1. NC_000962.3.
    YP_006516387.1. NC_018143.2.

    Genome annotation databases

    EnsemblBacteriaiCCP45736; CCP45736; Rv2933.
    GeneIDi13317727.
    887686.
    KEGGimtu:Rv2933.
    mtv:RVBD_2933.
    PATRICi18155111. VBIMycTub87468_3269.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL123456 Genomic DNA. Translation: CCP45736.1 .
    PIRi A70984.
    RefSeqi NP_217449.1. NC_000962.3.
    YP_006516387.1. NC_018143.2.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1PQW X-ray 2.66 A/B 1559-1755 [» ]
    ProteinModelPortali P96202.
    SMRi P96202. Positions 1571-1753.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 83332.Rv2933.

    Proteomic databases

    PRIDEi P96202.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CCP45736 ; CCP45736 ; Rv2933 .
    GeneIDi 13317727.
    887686.
    KEGGi mtu:Rv2933.
    mtv:RVBD_2933.
    PATRICi 18155111. VBIMycTub87468_3269.

    Organism-specific databases

    TubercuListi Rv2933.

    Phylogenomic databases

    eggNOGi COG3321.
    HOGENOMi HOG000046292.
    KOi K12442.
    OMAi WCSESEG.
    OrthoDBi EOG6QP0WP.
    PhylomeDBi P96202.

    Enzyme and pathway databases

    UniPathwayi UPA00094 .
    BioCyci MTBRV:RV2933-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P96202.

    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.
    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.
    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 SSF47336. SSF47336. 1 hit.
    SSF50129. SSF50129. 1 hit.
    SSF52151. SSF52151. 2 hits.
    SSF53901. SSF53901. 2 hits.
    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

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 25618 / H37Rv.
    2. "targetTB: a target identification pipeline for Mycobacterium tuberculosis through an interactome, reactome and genome-scale structural analysis."
      Raman K., Yeturu K., Chandra N.
      BMC Syst. Biol. 2:109-109(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
    3. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
      Strain: ATCC 25618 / H37Rv.
    4. "Putative enoyl reductase domain of polyketide synthase."
      Gogos A., Mu H., Shapiro L.
      Submitted (JUN-2003) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.66 ANGSTROMS) OF 1559-1755, SUBUNIT.
      Strain: ATCC 25618 / H37Rv.

    Entry informationi

    Entry nameiPPSC_MYCTU
    AccessioniPrimary (citable) accession number: P96202
    Secondary accession number(s): L0TBB0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 5, 2011
    Last sequence update: August 1, 1998
    Last modified: October 1, 2014
    This is version 114 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Was identified as a high-confidence drug target.

    Keywords - Technical termi

    3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
      Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3