P96202 (PPSC_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	ppsC
Ordered Locus Names:	Rv2933

Organism

Mycobacterium tuberculosis

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	2188 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 activity	Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl- [acyl-carrier-protein] + CO2 + [acyl-carrier-protein].
Cofactor	Binds 1 phosphopantetheines covalently By similarity. NADP By similarity.
Pathway	Lipid metabolism; fatty acid biosynthesis.
Subunit structure	Homodimer. Ref.3
Miscellaneous	Was identified as a high-confidence drug target.
Sequence similarities	Contains 1 acyl carrier domain.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Ligand	NADP Phosphopantetheine
Molecular function	Oxidoreductase Transferase
Technical term	3D-structure Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological process	DIM/DIP cell wall layer assembly Inferred from direct assay. Source: MTBBASE fatty acid biosynthetic process Inferred from direct assay. Source: MTBBASE phenolic phthiocerol biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB phthiocerol biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	cytosol Inferred from direct assay. Source: MTBBASE plasma membrane Inferred from direct assay. Source: MTBBASE polyketide synthase complex Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	3-oxoacyl-[acyl-carrier-protein] synthase activity Inferred from electronic annotation. Source: EC acyl carrier activity Inferred from electronic annotation. Source: InterPro cofactor binding Inferred from electronic annotation. Source: InterPro nucleotide binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity Inferred from electronic annotation. Source: UniProtKB-KW phosphopantetheine binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 2188

2188

Phthiocerol synthesis polyketide synthase type I PpsC

PRO_0000406948

Regions

Domain

2070 – 2142

73

Acyl carrier

Nucleotide binding

1803 – 1848

46

NADP By similarity

Region

37 – 465

429

Beta-ketoacyl synthase By similarity

Region

572 – 890

319

Acyltransferase By similarity

Region

928 – 1093

166

Dehydratase By similarity

Region

1467 – 1778

312

Enoylreductase By similarity

Region

1802 – 1981

180

Beta-ketoacyl reductase By similarity

Sites

Active site

210

1

For beta-ketoacyl synthase activity By similarity

Active site

660

1

For malonyltransferase activity By similarity

Amino acid modifications

Modified residue

2105

1

O-(pantetheine 4'-phosphoryl)serine By similarity

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

2188

Helix Strand Turn

Details...

Helix

1572 – 1575

4

Helix

1579 – 1588

10

Beta strand

1598 – 1601

4

Helix

1611 – 1618

8

Beta strand

1622 – 1625

4

Helix

1630 – 1637

8

Helix

1652 – 1659

8

Beta strand

1667 – 1670

4

Turn

1676 – 1678

3

Beta strand

1690 – 1692

3

Helix

1696 – 1698

3

Turn

1699 – 1701

3

Helix

1707 – 1709

3

Turn

1710 – 1712

3

Beta strand

1714 – 1717

4

Helix

1720 – 1726

7

Helix

1728 – 1743

16

Sequences

	Sequence		Length	Mass (Da)
	P96202 [UniParc]. Last modified August 1, 1998. Version 2. Checksum: 3C431C011F01F1A2	FASTA	2,188	230,622
	10 20 30 40 50 60 MTAATPDRRA IITEALHKID DLTARLEIAE KSSSEPIAVI GMGCRFPGGV NNPEQFWDLL 70 80 90 100 110 120 CAGRSGIVRV PAQRWDADAY YCDDHTVPGT ICSTEGGFLT SWQPDEFDAE FFSISPREAA 130 140 150 160 170 180 AMDPQQRLLI EVAWEALEDA GVPQHTIRGT QTSVFVGVTA YDYMLTLAGR LRPVDLDAYI 190 200 210 220 230 240 PTGNSANFAA GRLAYILGAR GPAVVIDTAC SSSLVAVHLA CQSLRGRESD MALVGGTNLL 250 260 270 280 290 300 LSPGPSIACS RWGMLSPEGR CKTFDASADG YVRGEGAAVV VLKRLDDAVR DGNRILAVVR 310 320 330 340 350 360 GSAVNQDGAS SGVTVPNGPA QQALLAKALT SSKLTAADID YVEAHGTGTP LGDPIELDSL 370 380 390 400 410 420 SKVFSDRAGS DQLVIGSVKT NLGHLEAAAG VAGLMKAVLA VHNGYIPRHL NFHQLTPHAS 430 440 450 460 470 480 EAASRLRIAA DGIDWPTTGR PRRAGVSSFG VSGTNAHVVI EQAPDPMAAA GTEPQRGPVP 490 500 510 520 530 540 AVSTLVVFGK TAPRVAATAS VLADWLDGPG AAVPLADVAH TLNHHRARQT RFGTVAAVDR 550 560 570 580 590 600 RQAVIGLRAL AAGQSAPGVV APREGSIGGG TVFVYSGRGS QWAGMGRQLL ADEPAFAAAI 610 620 630 640 650 660 AELEPEFVAQ GGFSLRDVIA GGKELVGIEQ IQLGLIGMQL ALTALWRSYG VTPDAVIGHS 670 680 690 700 710 720 MGEVAAAVVA GALTPAQGLR VTAVRSRLMA PLSGQGTMAL LELDAEATEA LIADYPEVSL 730 740 750 760 770 780 GIYASPRQTV ISGPPLLIDE LIDKVRQQNG FATRVNIEVA PHNPAMDALQ PAMRSELADL 790 800 810 820 830 840 TPQPPTIPII STTYADLGIS LGSGPRFDAE HWATNMRNPV RFHQAIAHAG ADHHTFIEIS 850 860 870 880 890 900 AHPLLTHSIS DTLRASYDVD NYLSIGTLQR DAHDTLEFHT NLNTTHTTHP PQTPHPPEPH 910 920 930 940 950 960 PVLPTTPWQH TQHWITATSA AYHRPDTHPL LGVGVTDPTN GTRVWESELD PDLLWLADHV 970 980 990 1000 1010 1020 IDDLVVLPGA AYAEIALAAA TDTFAVEQDQ PWMISELDLR QMLHVTPGTV LVTTLTGDEQ 1030 1040 1050 1060 1070 1080 RCQVEIRTRS GSSGWTTHAT ATVARAEPLA PLDHEGQRRE VTTADLEDQL DPDDLYQRLR 1090 1100 1110 1120 1130 1140 GAGQQHGPAF QGIVGLAVTQ AGVARAQVRL PASARTGSRE FMLHPVMMDI ALQTLGATRT 1150 1160 1170 1180 1190 1200 ATDLAGGQDA RQGPSSNSAL VVPVRFAGVH VYGDITRGVR AVGSLAAAGD RLVGEVVLTD 1210 1220 1230 1240 1250 1260 ANGQPLLVVD EVEMAVLGSG SGATELTNRL FMLEWEPAPL EKTAEATGAL LLIGDPAAGD 1270 1280 1290 1300 1310 1320 PLLPALQSSL RDRITDLELA SAADEATLRA AISRTSWDGI VVVCPPRAND ESMPDEAQLE 1330 1340 1350 1360 1370 1380 LARTRTLLVA SVVETVTRMG ARKSPRLWIV TRGAAQFDAG ESVTLAQTGL RGIARVLTFE 1390 1400 1410 1420 1430 1440 HSELNTTLVD IEPDGTGSLA ALAEELLAGS EADEVALRDG QRYVNRLVPA PTTTSGDLAA 1450 1460 1470 1480 1490 1500 EARHQVVNLD SSGASRAAVR LQIDQPGRLD ALNVHEVKRG RPQGDQVEVR VVAAGLNFSD 1510 1520 1530 1540 1550 1560 VLKAMGVYPG LDGAAPVIGG ECVGYVTAIG DEVDGVEVGQ RVIAFGPGTF GTHLGTIADL 1570 1580 1590 1600 1610 1620 VVPIPDTLAD NEAATFGVAY LTAWHSLCEV GRLSPGERVL IHSATGGVGM AAVSIAKMIG 1630 1640 1650 1660 1670 1680 ARIYTTAGSD AKREMLSRLG VEYVGDSRSV DFADEILELT DGYGVDVVLN SLAGEAIQRG 1690 1700 1710 1720 1730 1740 VQILAPGGRF IELGKKDVYA DASLGLAALA KSASFSVVDL DLNLKLQPAR YRQLLQHILQ 1750 1760 1770 1780 1790 1800 HVADGKLEVL PVTAFSLHDA ADAFRLMASG KHTGKIVISI PQHGSIEAIA APPPLPLVSR 1810 1820 1830 1840 1850 1860 DGGYLIVGGM GGLGFVVARW LAEQGAGLIV LNGRSAPSDE VAAAIAELNA SGSRIEVITG 1870 1880 1890 1900 1910 1920 DITEPDTAER LVRAVEDAGF RLAGVVHSAM VLADEIVLNM TDSAARRVFA PKVTGSWRLH 1930 1940 1950 1960 1970 1980 VATAARDVDW WLTFSSAAAL LGTPGQGAYA AANSWVDGLV AHRRSAGLPA VGINWGPWAD 1990 2000 2010 2020 2030 2040 VGRAQFFKDL GVEMINAEQG LAAMQAVLTA DRGRTGVFSL DARQWFQSFP AVAGSSLFAK 2050 2060 2070 2080 2090 2100 LHDSAARKSG QRRGGGAIRA QLDALDAAER PGHLASAIAD EIRAVLRSGD PIDHHRPLET 2110 2120 2130 2140 2150 2160 LGLDSLMGLE LRNRLEASLG ITLPVALVWA YPTISDLATA LCERMDYATP AAAQEISDTE 2170 2180 PELSDEEMDL LADLVDASEL EAATRGES

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G. Nature 393:537-544(1998) [PubMed: 9634230] [Abstract] 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: 19099550] [Abstract] Cited for: IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
[3]	"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BX842581 Genomic DNA. Translation: CAB06099.1.

PIR

A70984.

RefSeq

NP_217449.1. NC_000962.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1PQW	X-ray	2.66	A/B	1559-1755	[»]

ProteinModelPortal

P96202.

SMR

P96202. Positions 1571-1753.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBMYCT00000002654; EBMYCP00000002654; EBMYCG00000002652.

GeneID

887686.

GenomeReviews

Gene locus Rv2933 in contig AL123456_GR.

KEGG

mtu:Rv2933.

PATRIC

18155111. VBIMycTub87468_3269.

Organism-specific databases

TubercuList

Rv2933.

Phylogenomic databases

GeneTree

EBGT00070000032455.

HOGENOM

HBG669988.

OMA

DRCLSLK.

PhylomeDB

P96202.

ProtClustDB

CLSK792171.

Family and domain databases

InterPro

IPR001227. Ac_transferase_dom.
IPR009081. Acyl_carrier_prot-like.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR013149. ADH_C.
IPR013154. ADH_GroES-like.
IPR000794. Beta-ketoacyl_synthase.
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.
IPR006163. Phsphopanteth-bd.
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]

Gene3D

G3DSA:3.40.366.10. Ac_transferase_reg. 2 hits.
G3DSA:1.10.1200.10. ACP_like. 1 hit.
G3DSA:3.40.50.720. NAD(P)-bd. 2 hits.
G3DSA:3.40.47.10. Thiolase-like_subgr. 2 hits.

KO

K12442.

PANTHER

PTHR11712. Ketoacyl_synth. 1 hit.

Pfam

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]

SMART

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]

SUPFAM

SSF47336. ACP_like. 1 hit.
SSF52151. Acyl_Trfase/lysoPlipase. 1 hit.
SSF50129. GroES_like. 1 hit.
SSF55048. Malonyl_transacylase_ACP-bd. 1 hit.
SSF53901. Thiolase-like. 1 hit.

PROSITE

PS50075. ACP_DOMAIN. 1 hit.
PS00606. B_KETOACYL_SYNTHASE. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

PPSC_MYCTU

Accession

Primary (citable) accession number: P96202

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 5, 2011
Last sequence update:	August 1, 1998
Last modified:	January 25, 2012
This is version 91 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program