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P96202

- PPSC_MYCTU

UniProt

P96202 - PPSC_MYCTU

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Protein
Phthiocerol synthesis polyketide synthase type I PpsC
Gene
ppsC, Rv2933
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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].

Cofactori

Binds 1 phosphopantetheines covalently By similarity.
NADP By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei210 – 2101For beta-ketoacyl synthase activity By similarity
Active sitei660 – 6601For malonyltransferase activity By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1803 – 184846NADP By similarity
Add
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
Complete GO annotation...

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
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 21882187Phthiocerol synthesis polyketide synthase type I PpsC
PRO_0000406948Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonine1 Publication
Modified residuei2105 – 21051O-(pantetheine 4'-phosphoryl)serine By similarity

Keywords - PTMi

Acetylation, Phosphopantetheine, Phosphoprotein

Proteomic databases

PRIDEiP96202.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi83332.Rv2933.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiP96202.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2070 – 214273Acyl carrier
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni37 – 465429Beta-ketoacyl synthase By similarity
Add
BLAST
Regioni572 – 890319Acyltransferase By similarity
Add
BLAST
Regioni928 – 1093166Dehydratase By similarity
Add
BLAST
Regioni1467 – 1778312Enoylreductase By similarity
Add
BLAST
Regioni1802 – 1981180Beta-ketoacyl reductase By similarity
Add
BLAST

Sequence similaritiesi

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

« Hide

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 113 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

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