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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: 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: fatty acid biosynthesis

This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway fatty acid biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei210For beta-ketoacyl synthase activityPROSITE-ProRule annotation1
Active sitei660For malonyltransferase activityPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi1803 – 1848NADPBy similarityAdd BLAST46

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Transferase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciMTBH37RV:G185E-7186-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 lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv2933.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: MTBBASE
  • plasma membrane Source: MTBBASE
  • polyketide synthase complex Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00004069482 – 2188Phthiocerol synthesis polyketide synthase type I PpsCAdd BLAST2187

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylthreonineCombined sources1
Modified residuei2105O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1

Keywords - PTMi

Acetylation, Phosphopantetheine, Phosphoprotein

Proteomic databases

PaxDbiP96202.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi83332.Rv2933.

Structurei

Secondary structure

12188
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni929 – 931Combined sources3
Beta strandi933 – 936Combined sources4
Turni938 – 940Combined sources3
Beta strandi943 – 949Combined sources7
Turni954 – 958Combined sources5
Beta strandi959 – 961Combined sources3
Beta strandi964 – 966Combined sources3
Helixi969 – 983Combined sources15
Beta strandi987 – 990Combined sources4
Beta strandi992 – 999Combined sources8
Beta strandi1009 – 1017Combined sources9
Beta strandi1019 – 1029Combined sources11
Beta strandi1031 – 1033Combined sources3
Beta strandi1035 – 1045Combined sources11
Beta strandi1068 – 1070Combined sources3
Helixi1072 – 1081Combined sources10
Beta strandi1084 – 1086Combined sources3
Turni1088 – 1090Combined sources3
Beta strandi1093 – 1098Combined sources6
Beta strandi1104 – 1108Combined sources5
Helixi1112 – 1115Combined sources4
Helixi1118 – 1120Combined sources3
Helixi1125 – 1133Combined sources9
Helixi1134 – 1136Combined sources3
Helixi1139 – 1143Combined sources5
Beta strandi1159 – 1171Combined sources13
Helixi1175 – 1177Combined sources3
Beta strandi1180 – 1187Combined sources8
Beta strandi1192 – 1199Combined sources8
Beta strandi1205 – 1218Combined sources14
Helixi1572 – 1587Combined sources16
Turni1588 – 1591Combined sources4
Beta strandi1598 – 1601Combined sources4
Turni1602 – 1605Combined sources4
Helixi1607 – 1619Combined sources13
Beta strandi1622 – 1629Combined sources8
Helixi1630 – 1638Combined sources9
Beta strandi1642 – 1646Combined sources5
Helixi1652 – 1659Combined sources8
Turni1660 – 1662Combined sources3
Beta strandi1665 – 1670Combined sources6
Helixi1675 – 1682Combined sources8
Beta strandi1684 – 1692Combined sources9
Helixi1696 – 1699Combined sources4
Beta strandi1703 – 1705Combined sources3
Helixi1706 – 1709Combined sources4
Turni1710 – 1712Combined sources3
Beta strandi1714 – 1717Combined sources4
Helixi1720 – 1726Combined sources7
Helixi1728 – 1743Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PQWX-ray2.66A/B1559-1755[»]
4OKIX-ray1.50A/B1558-1750[»]
4OOCX-ray2.70A921-1222[»]
4P7PX-ray2.90A921-1222[»]
5CF7X-ray1.60A921-1222[»]
ProteinModelPortaliP96202.
SMRiP96202.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP96202.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2070 – 2142Acyl carrierPROSITE-ProRule annotationAdd BLAST73

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni37 – 465Beta-ketoacyl synthaseBy similarityAdd BLAST429
Regioni572 – 890AcyltransferaseBy similarityAdd BLAST319
Regioni928 – 1093DehydrataseBy similarityAdd BLAST166
Regioni1467 – 1778EnoylreductaseBy similarityAdd BLAST312
Regioni1802 – 1981Beta-ketoacyl reductaseBy similarityAdd BLAST180

Sequence similaritiesi

Contains 1 acyl carrier domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410XNPJ. LUCA.
HOGENOMiHOG000046292.
InParanoidiP96202.
KOiK12442.
OMAiMISEIDW.
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.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR013154. ADH_N.
IPR011032. GroES-like.
IPR032821. KAsynt_C_assoc.
IPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR016036. Malonyl_transacylase_ACP-bd.
IPR016040. NAD(P)-bd_dom.
IPR020801. PKS_acyl_transferase.
IPR020841. PKS_Beta-ketoAc_synthase_dom.
IPR020807. PKS_dehydratase.
IPR020843. PKS_ER.
IPR013968. PKS_KR.
IPR020806. PKS_PP-bd.
IPR009081. PP-bd_ACP.
IPR006162. Ppantetheine_attach_site.
IPR016039. Thiolase-like.
[Graphical view]
PfamiPF00698. Acyl_transf_1. 1 hit.
PF08240. ADH_N. 1 hit.
PF16197. KAsynt_C_assoc. 1 hit.
PF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
PF08659. KR. 1 hit.
PF00550. PP-binding. 1 hit.
PF14765. PS-DH. 1 hit.
[Graphical view]
SMARTiSM00827. PKS_AT. 1 hit.
SM00826. PKS_DH. 1 hit.
SM00829. PKS_ER. 1 hit.
SM00825. PKS_KS. 1 hit.
SM00823. PKS_PP. 1 hit.
[Graphical view]
SUPFAMiSSF47336. SSF47336. 1 hit.
SSF50129. SSF50129. 1 hit.
SSF51735. SSF51735. 3 hits.
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.
WP_003414837.1. NZ_KK339370.1.

Genome annotation databases

EnsemblBacteriaiCCP45736; CCP45736; Rv2933.
GeneIDi887686.
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.
PIRiA70984.
RefSeqiNP_217449.1. NC_000962.3.
WP_003414837.1. NZ_KK339370.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PQWX-ray2.66A/B1559-1755[»]
4OKIX-ray1.50A/B1558-1750[»]
4OOCX-ray2.70A921-1222[»]
4P7PX-ray2.90A921-1222[»]
5CF7X-ray1.60A921-1222[»]
ProteinModelPortaliP96202.
SMRiP96202.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv2933.

Proteomic databases

PaxDbiP96202.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP45736; CCP45736; Rv2933.
GeneIDi887686.
KEGGimtu:Rv2933.
mtv:RVBD_2933.
PATRICi18155111. VBIMycTub87468_3269.

Organism-specific databases

TubercuListiRv2933.

Phylogenomic databases

eggNOGiENOG410XNPJ. LUCA.
HOGENOMiHOG000046292.
InParanoidiP96202.
KOiK12442.
OMAiMISEIDW.
PhylomeDBiP96202.

Enzyme and pathway databases

UniPathwayiUPA00094.
BioCyciMTBH37RV:G185E-7186-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP96202.

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.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR013154. ADH_N.
IPR011032. GroES-like.
IPR032821. KAsynt_C_assoc.
IPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR016036. Malonyl_transacylase_ACP-bd.
IPR016040. NAD(P)-bd_dom.
IPR020801. PKS_acyl_transferase.
IPR020841. PKS_Beta-ketoAc_synthase_dom.
IPR020807. PKS_dehydratase.
IPR020843. PKS_ER.
IPR013968. PKS_KR.
IPR020806. PKS_PP-bd.
IPR009081. PP-bd_ACP.
IPR006162. Ppantetheine_attach_site.
IPR016039. Thiolase-like.
[Graphical view]
PfamiPF00698. Acyl_transf_1. 1 hit.
PF08240. ADH_N. 1 hit.
PF16197. KAsynt_C_assoc. 1 hit.
PF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
PF08659. KR. 1 hit.
PF00550. PP-binding. 1 hit.
PF14765. PS-DH. 1 hit.
[Graphical view]
SMARTiSM00827. PKS_AT. 1 hit.
SM00826. PKS_DH. 1 hit.
SM00829. PKS_ER. 1 hit.
SM00825. PKS_KS. 1 hit.
SM00823. PKS_PP. 1 hit.
[Graphical view]
SUPFAMiSSF47336. SSF47336. 1 hit.
SSF50129. SSF50129. 1 hit.
SSF51735. SSF51735. 3 hits.
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]
ProtoNetiSearch...

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 30, 2016
This is version 132 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.