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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

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].PROSITE-ProRule annotation

Cofactori

Protein has several cofactor binding sites:

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
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 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 – 158817Combined sources
Beta strandi1598 – 16014Combined sources
Turni1602 – 16054Combined sources
Helixi1607 – 161913Combined sources
Beta strandi1622 – 16298Combined sources
Helixi1630 – 16378Combined sources
Beta strandi1642 – 16465Combined sources
Helixi1652 – 16598Combined sources
Turni1660 – 16623Combined sources
Beta strandi1665 – 16706Combined sources
Helixi1675 – 16828Combined sources
Beta strandi1684 – 16929Combined sources
Helixi1696 – 16983Combined sources
Turni1699 – 17013Combined sources
Beta strandi1703 – 17053Combined sources
Helixi1706 – 17094Combined sources
Turni1710 – 17123Combined sources
Beta strandi1714 – 17174Combined sources
Helixi1720 – 17267Combined sources
Helixi1728 – 174316Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP96202.
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

        10         20         30         40         50
MTAATPDRRA IITEALHKID DLTARLEIAE KSSSEPIAVI GMGCRFPGGV
60 70 80 90 100
NNPEQFWDLL CAGRSGIVRV PAQRWDADAY YCDDHTVPGT ICSTEGGFLT
110 120 130 140 150
SWQPDEFDAE FFSISPREAA AMDPQQRLLI EVAWEALEDA GVPQHTIRGT
160 170 180 190 200
QTSVFVGVTA YDYMLTLAGR LRPVDLDAYI PTGNSANFAA GRLAYILGAR
210 220 230 240 250
GPAVVIDTAC SSSLVAVHLA CQSLRGRESD MALVGGTNLL LSPGPSIACS
260 270 280 290 300
RWGMLSPEGR CKTFDASADG YVRGEGAAVV VLKRLDDAVR DGNRILAVVR
310 320 330 340 350
GSAVNQDGAS SGVTVPNGPA QQALLAKALT SSKLTAADID YVEAHGTGTP
360 370 380 390 400
LGDPIELDSL SKVFSDRAGS DQLVIGSVKT NLGHLEAAAG VAGLMKAVLA
410 420 430 440 450
VHNGYIPRHL NFHQLTPHAS EAASRLRIAA DGIDWPTTGR PRRAGVSSFG
460 470 480 490 500
VSGTNAHVVI EQAPDPMAAA GTEPQRGPVP AVSTLVVFGK TAPRVAATAS
510 520 530 540 550
VLADWLDGPG AAVPLADVAH TLNHHRARQT RFGTVAAVDR RQAVIGLRAL
560 570 580 590 600
AAGQSAPGVV APREGSIGGG TVFVYSGRGS QWAGMGRQLL ADEPAFAAAI
610 620 630 640 650
AELEPEFVAQ GGFSLRDVIA GGKELVGIEQ IQLGLIGMQL ALTALWRSYG
660 670 680 690 700
VTPDAVIGHS MGEVAAAVVA GALTPAQGLR VTAVRSRLMA PLSGQGTMAL
710 720 730 740 750
LELDAEATEA LIADYPEVSL GIYASPRQTV ISGPPLLIDE LIDKVRQQNG
760 770 780 790 800
FATRVNIEVA PHNPAMDALQ PAMRSELADL TPQPPTIPII STTYADLGIS
810 820 830 840 850
LGSGPRFDAE HWATNMRNPV RFHQAIAHAG ADHHTFIEIS AHPLLTHSIS
860 870 880 890 900
DTLRASYDVD NYLSIGTLQR DAHDTLEFHT NLNTTHTTHP PQTPHPPEPH
910 920 930 940 950
PVLPTTPWQH TQHWITATSA AYHRPDTHPL LGVGVTDPTN GTRVWESELD
960 970 980 990 1000
PDLLWLADHV IDDLVVLPGA AYAEIALAAA TDTFAVEQDQ PWMISELDLR
1010 1020 1030 1040 1050
QMLHVTPGTV LVTTLTGDEQ RCQVEIRTRS GSSGWTTHAT ATVARAEPLA
1060 1070 1080 1090 1100
PLDHEGQRRE VTTADLEDQL DPDDLYQRLR GAGQQHGPAF QGIVGLAVTQ
1110 1120 1130 1140 1150
AGVARAQVRL PASARTGSRE FMLHPVMMDI ALQTLGATRT ATDLAGGQDA
1160 1170 1180 1190 1200
RQGPSSNSAL VVPVRFAGVH VYGDITRGVR AVGSLAAAGD RLVGEVVLTD
1210 1220 1230 1240 1250
ANGQPLLVVD EVEMAVLGSG SGATELTNRL FMLEWEPAPL EKTAEATGAL
1260 1270 1280 1290 1300
LLIGDPAAGD PLLPALQSSL RDRITDLELA SAADEATLRA AISRTSWDGI
1310 1320 1330 1340 1350
VVVCPPRAND ESMPDEAQLE LARTRTLLVA SVVETVTRMG ARKSPRLWIV
1360 1370 1380 1390 1400
TRGAAQFDAG ESVTLAQTGL RGIARVLTFE HSELNTTLVD IEPDGTGSLA
1410 1420 1430 1440 1450
ALAEELLAGS EADEVALRDG QRYVNRLVPA PTTTSGDLAA EARHQVVNLD
1460 1470 1480 1490 1500
SSGASRAAVR LQIDQPGRLD ALNVHEVKRG RPQGDQVEVR VVAAGLNFSD
1510 1520 1530 1540 1550
VLKAMGVYPG LDGAAPVIGG ECVGYVTAIG DEVDGVEVGQ RVIAFGPGTF
1560 1570 1580 1590 1600
GTHLGTIADL VVPIPDTLAD NEAATFGVAY LTAWHSLCEV GRLSPGERVL
1610 1620 1630 1640 1650
IHSATGGVGM AAVSIAKMIG ARIYTTAGSD AKREMLSRLG VEYVGDSRSV
1660 1670 1680 1690 1700
DFADEILELT DGYGVDVVLN SLAGEAIQRG VQILAPGGRF IELGKKDVYA
1710 1720 1730 1740 1750
DASLGLAALA KSASFSVVDL DLNLKLQPAR YRQLLQHILQ HVADGKLEVL
1760 1770 1780 1790 1800
PVTAFSLHDA ADAFRLMASG KHTGKIVISI PQHGSIEAIA APPPLPLVSR
1810 1820 1830 1840 1850
DGGYLIVGGM GGLGFVVARW LAEQGAGLIV LNGRSAPSDE VAAAIAELNA
1860 1870 1880 1890 1900
SGSRIEVITG DITEPDTAER LVRAVEDAGF RLAGVVHSAM VLADEIVLNM
1910 1920 1930 1940 1950
TDSAARRVFA PKVTGSWRLH VATAARDVDW WLTFSSAAAL LGTPGQGAYA
1960 1970 1980 1990 2000
AANSWVDGLV AHRRSAGLPA VGINWGPWAD VGRAQFFKDL GVEMINAEQG
2010 2020 2030 2040 2050
LAAMQAVLTA DRGRTGVFSL DARQWFQSFP AVAGSSLFAK LHDSAARKSG
2060 2070 2080 2090 2100
QRRGGGAIRA QLDALDAAER PGHLASAIAD EIRAVLRSGD PIDHHRPLET
2110 2120 2130 2140 2150
LGLDSLMGLE LRNRLEASLG ITLPVALVWA YPTISDLATA LCERMDYATP
2160 2170 2180
AAAQEISDTE PELSDEEMDL LADLVDASEL EAATRGES
Length:2,188
Mass (Da):230,622
Last modified:August 1, 1998 - v2
Checksum:i3C431C011F01F1A2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
InParanoidi P96202.
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: November 26, 2014
This is version 116 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