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Q7TXL8 (PPSC_MYCBO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phthiocerol/phenolphthiocerol 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:Mb2958
OrganismMycobacterium bovis (strain ATCC BAA-935 / AF2122/97) [Complete proteome] [HAMAP]
Taxonomic identifier233413 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex ›

Protein attributes

Sequence length2188 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the elongation of either C22-24 fatty acids or p-hydroxyphenylalkanoic acids by the addition of malonyl-CoA and methylmalonyl-CoA extender units to yield phthiocerol and phenolphthiocerol derivatives, respectively. Ref.2

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 By similarity.

Disruption phenotype

Cells lacking this genes abolish the production of phenolphthiocerol derivative (mycoside B) and phthiocerol dimycocerosates (DIM) on the cell envelope. Ref.2

Sequence similarities

Contains 1 acyl carrier domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 21882188Phthiocerol/phenolphthiocerol synthesis polyketide synthase type I PpsC
PRO_0000406947

Regions

Domain2074 – 214269Acyl carrier
Nucleotide binding1803 – 184846NADP By similarity
Region37 – 465429Beta-ketoacyl synthase By similarity
Region572 – 890319Acyltransferase By similarity
Region928 – 1093166Dehydratase By similarity
Region1467 – 1778312Enoylreductase By similarity
Region1802 – 1981180Beta-ketoacyl reductase By similarity

Sites

Active site2101For beta-ketoacyl synthase activity By similarity
Active site6601For malonyltransferase activity By similarity

Amino acid modifications

Modified residue21051O-(pantetheine 4'-phosphoryl)serine Potential

Sequences

Sequence LengthMass (Da)Tools
Q7TXL8 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 3C431C011F01F1A2

FASTA2,188230,622
        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

« Hide

References

« Hide 'large scale' references
[1]"The complete genome sequence of Mycobacterium bovis."
Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M., Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B., Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J. expand/collapse author list , Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.
Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-935 / AF2122/97.
[2]"Gene knockout reveals a novel gene cluster for the synthesis of a class of cell wall lipids unique to pathogenic mycobacteria."
Azad A.K., Sirakova T.D., Fernandes N.D., Kolattukudy P.E.
J. Biol. Chem. 272:16741-16745(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN THE PHTHIOCEROL AND PHENOLPHTHIOCEROL BIOSYNTHESIS, DISRUPTION PHENOTYPE.
Strain: ATCC BAA-935 / AF2122/97.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX248344 Genomic DNA. Translation: CAD96645.1.
RefSeqNP_856603.1. NC_002945.3.

3D structure databases

ProteinModelPortalQ7TXL8.
SMRQ7TXL8. Positions 1571-1753.
ModBaseSearch...

Protein-protein interaction databases

STRING233413.Mb2958.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD96645; CAD96645; Mb2958.
GeneID1092148.
KEGGmbo:Mb2958.
PATRIC18008228. VBIMycBov88188_3246.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3321.
HOGENOMHOG000046292.
KOK12442.
OMADRCLSLK.
ProtClustDBCLSK792171.

Enzyme and pathway databases

UniPathwayUPA00094.

Family and domain databases

Gene3D1.10.1200.10. 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.
InterProIPR001227. 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]
PfamPF00698. 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]
SMARTSM00827. 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]
SUPFAMSSF47336. 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.
PROSITEPS50075. ACP_DOMAIN. 1 hit.
PS00606. B_KETOACYL_SYNTHASE. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePPSC_MYCBO
AccessionPrimary (citable) accession number: Q7TXL8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 5, 2011
Last sequence update: October 1, 2003
Last modified: May 29, 2013
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents