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Q7TXM0 (PPSA_MYCBO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 81. 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

Names and origin

Protein namesRecommended name:
Phthiocerol/phenolphthiocerol synthesis polyketide synthase type I PpsA
Alternative name(s):
Beta-ketoacyl-acyl-carrier-protein synthase I
EC=2.3.1.41
Gene names
Name:ppsA
Ordered Locus Names:Mb2956
OrganismMycobacterium bovis (strain ATCC BAA-935 / AF2122/97) [Complete proteome] [HAMAP]
Taxonomic identifier233413 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length1876 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 2 phosphopantetheines covalently By similarity.

NADP By similarity.

Pathway

Lipid metabolism; fatty acid biosynthesis.

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 2 acyl carrier domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 18761876Phthiocerol/phenolphthiocerol synthesis polyketide synthase type I PpsA
PRO_0000406945

Regions

Domain7 – 8074Acyl carrier 1
Domain1764 – 183370Acyl carrier 2
Nucleotide binding1492 – 155160NADP By similarity
Region104 – 529426Beta-ketoacyl synthase By similarity
Region624 – 950327Acyltransferase By similarity
Region1491 – 1728238Beta-ketoacyl reductase By similarity

Sites

Active site2731For beta-ketoacyl synthase activity By similarity
Active site7201For malonyltransferase activity By similarity

Amino acid modifications

Modified residue431O-(pantetheine 4'-phosphoryl)serine By similarity
Modified residue17961O-(pantetheine 4'-phosphoryl)serine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7TXM0 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: D44006C79AEF6AAE

FASTA1,876198,848
        10         20         30         40         50         60 
MTGSISGEAD LRHWLIDYLV TNIGCTPDEV DPDLSLADLG VSSRDAVVLS GELSELLGRT 

        70         80         90        100        110        120 
VSPIDFWEHP TINALAAYLA APEPSPDSDA AVKRGARNSL DEPIAVVGMG CRFPGGISCP 

       130        140        150        160        170        180 
EALWDFLCER RSSISQVPPQ RWQPFEGGPP EVAAALARTT RWGSFLPDID AFDAEFFEIS 

       190        200        210        220        230        240 
PSEADKMDPQ QRLLLEVAWE ALEHAGIPPG TLRRSATGVF AGACLSEYGA MASADLSQVD 

       250        260        270        280        290        300 
GWSNSGGAMS IIANRLSYFL DLRGPSVAVD TACSSSLVAI HLACQSLRTQ DCHLAIAAGV 

       310        320        330        340        350        360 
NLLLSPAVFR GFDQVGALSP TGQCRAFDAT ADGFVRGEGA GVVVLKRLTD AQRDGDRVLA 

       370        380        390        400        410        420 
VICGSAVTQD GRSNGLMAPN PAAQMAVLRA AYTNAGMQPS EVDYVEAHGT GTLLGDPIEA 

       430        440        450        460        470        480 
RALGTVLGRG RPEDSPLLIG SVKTNLGHTE AAAGIAGFIK TVLAVQHGQI PPNQHFETAN 

       490        500        510        520        530        540 
PHIPFTDLRM KVVDTQTEWP ATGHPRRAGV SSFGFGGTNA HVVIEQGQEV RPAPGQGLSP 

       550        560        570        580        590        600 
AVSTLVVAGK TMQRVSATAG MLADWMEGPG ADVALADVAH TLNHHRSRQP KFGTVVARDR 

       610        620        630        640        650        660 
TQAIAGLRAL AAGQHAPGVV NPAEGSPGPG TVFVYSGRGS QWAGMGRQLL ADEPAFAAAV 

       670        680        690        700        710        720 
AELEPVFVEQ AGFSLHDVLA NGEELVGIEQ IQLGLIGMQL ALTELWCSYG VQPDLVIGHS 

       730        740        750        760        770        780 
MGEVAAAVVA GALTPAEGLR VTATRSRLMA PLSGQGGMAL LELDAPTTEA LIADFPQVTL 

       790        800        810        820        830        840 
GIYNSPRQTV IAGPTEQIDE LITRVRARDR FASRVNIEVA PHNPAMDALQ PAMRSELADL 

       850        860        870        880        890        900 
TPRTPTIGII STTYADLHTQ PVFDAEHWAT NMRNPVHFQQ AIASAGSGAD GAYHTFIEIS 

       910        920        930        940        950        960 
AHPLLTQAII DTLHSAQPGA RYTSLGTLQR DTDDVVTFRT NLNKAHTIHP PHTPHPPEPH 

       970        980        990       1000       1010       1020 
PPIPTTPWQH TRHWITTKYP AGSVGSAPRA GTLLGQHTTV ATVSASPPSH LWQARLAPDA 

      1030       1040       1050       1060       1070       1080 
KPYQGGHRFH QVEVVPASVV LHTILSAATE LGYSALSEVR FEQPIFADRP RLIQVVADNR 

      1090       1100       1110       1120       1130       1140 
AISLASSPAA GTPSDRWTRH VTAQLSSSPS DSASSLNEHH RANGQPPERA HRDLIPDLAE 

      1150       1160       1170       1180       1190       1200 
LLAMRGIDGL PFSWTVASWT QHSSNLTVAI DLPEALPEGS TGPLLDAAVH LAALSDVADS 

      1210       1220       1230       1240       1250       1260 
RLYVPASIEQ ISLGDVVTGP RSSVTLNRTA HDDDGITVDV TVAAHGEVPS LSMRSLRYRA 

      1270       1280       1290       1300       1310       1320 
LDFGLDVGRA QPPASTGPVE AYCDATNFVH TIDWQPQTVP DATHPGAEQV THPGPVAIIG 

      1330       1340       1350       1360       1370       1380 
DDGAALCETL EGAGYQPAVM SDGVSQARYV VYVADSDPAG ADETDVDFAV RICTEITGLV 

      1390       1400       1410       1420       1430       1440 
RTLAERDADK PAALWILTRG VHESVAPSAL RQSFLWGLAG VIAAEHPELW GGLVDLAIND 

      1450       1460       1470       1480       1490       1500 
DLGEFGPALA ELLAKPSKSI LVRRDGVVLA PALAPVRGEP ARKSLQCRPD AAYLITGGLG 

      1510       1520       1530       1540       1550       1560 
ALGLLMADWL ADRGAHRLVL TGRTPLPPRR DWQLDTLDTE LRRRIDAIRA LEMRGVTVEA 

      1570       1580       1590       1600       1610       1620 
VAADVGCRED VQALLAARDR DGAAPIRGII HAAGITNDQL VTSMTGDAVR QVMWPKIGGS 

      1630       1640       1650       1660       1670       1680 
QVLHDAFPPG SVDFFYLTAS AAGIFGIPGQ GSYAAANSYL DALARARRQQ GCHTMSLDWV 

      1690       1700       1710       1720       1730       1740 
AWRGLGLAAD AQLVSEELAR MGSRDITPSE AFTAWEFVDG YDVAQAVVVP MPAPAGADGS 

      1750       1760       1770       1780       1790       1800 
GANAYLLPAR NWSVMAATEV RSELEQGLRR IIAAELRVPE KELDTDRPFA ELGLNSLMAM 

      1810       1820       1830       1840       1850       1860 
AIRREAEQFV GIELSATMLF NHPTVKSLAS YLAKRVAPHD VSQDNQISAL SSSAGSVLDS 

      1870 
LFDRIESAPP EAERSV 

« 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: CAD96643.1.
RefSeqNP_856601.1. NC_002945.3.

3D structure databases

ProteinModelPortalQ7TXM0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING233413.Mb2956.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD96643; CAD96643; Mb2956.
GeneID1092150.
KEGGmbo:Mb2956.
PATRIC18008224. VBIMycBov88188_3244.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3321.
HOGENOMHOG000046292.
KOK12440.
OMASWAPILD.
OrthoDBEOG6W19KW.
ProtClustDBCLSK792169.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-17242.
UniPathwayUPA00094.

Family and domain databases

Gene3D1.10.1200.10. 2 hits.
3.40.366.10. 2 hits.
3.40.47.10. 2 hits.
3.40.50.720. 1 hit.
InterProIPR001227. Ac_transferase_dom.
IPR009081. Acyl_carrier_prot-like.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
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.
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.
PF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
PF08659. KR. 1 hit.
PF00550. PP-binding. 2 hits.
[Graphical view]
SMARTSM00827. PKS_AT. 1 hit.
SM00822. PKS_KR. 1 hit.
SM00825. PKS_KS. 1 hit.
SM00823. PKS_PP. 2 hits.
[Graphical view]
SUPFAMSSF47336. SSF47336. 2 hits.
SSF52151. SSF52151. 2 hits.
SSF53901. SSF53901. 2 hits.
SSF55048. SSF55048. 1 hit.
PROSITEPS50075. ACP_DOMAIN. 2 hits.
PS00606. B_KETOACYL_SYNTHASE. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePPSA_MYCBO
AccessionPrimary (citable) accession number: Q7TXM0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 5, 2011
Last sequence update: October 1, 2003
Last modified: February 19, 2014
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways