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G8BAW7 (FAS2_CANPC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 16. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
Fatty acid synthase subunit alpha

EC=2.3.1.86

Including the following 3 domains:

  1. Acyl carrier
  2. 3-oxoacyl-[acyl-carrier-protein] reductase
    EC=1.1.1.100
    Alternative name(s):
    Beta-ketoacyl reductase
  3. 3-oxoacyl-[acyl-carrier-protein] synthase
    EC=2.3.1.41
    Alternative name(s):
    Beta-ketoacyl synthase
Gene names
Name:FAS2
ORF Names:CPAR2_807400
OrganismCandida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis) [Complete proteome]
Taxonomic identifier578454 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length1884 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The alpha subunit contains domains for: acyl carrier protein, 3-oxoacyl-[acyl-carrier-protein] reductase, and 3-oxoacyl-[acyl-carrier-protein] synthase. Ref.4

Catalytic activity

Acetyl-CoA + n malonyl-CoA + 2n NADPH = long-chain-acyl-CoA + n CoA + n CO2 + 2n NADP+. HAMAP-Rule MF_00101

Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein]. HAMAP-Rule MF_00101

(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP+ = 3-oxoacyl-[acyl-carrier-protein] + NADPH. HAMAP-Rule MF_00101

Subunit structure

Fatty acid synthase is composed of alpha and beta subunits By similarity.

Induction

Expression significantly elevated by the presence of glucose. Down-regulated by unsaturated fatty acids oleic acid and Tween 80. Up-regulated during in vitro biofilm formation and hypoxic conditions. Ref.3 Ref.4

Disruption phenotype

Essential for growth in fatty acid-free medium, but dispensable in medium with fatty acids. The growth in the presence of fatty acid depends on the type. Able to grow in a concentration-dependent manner in the presence of myristic acid, palmitic acid, or Tween 80 as the fatty acid sources, but unable to grow in the presence of unsaturated fatty like acids stearic acid or oleic acid. Intracellular survival in the murine macrophage line J774.16 is significantly reduced compared to wild type or heterozygous fungal cells. Required for systemic infection in mice. Impaired in its capacity to form biofilms on polysterene and silicone surfaces. Ref.4

Miscellaneous

It can potentially be a fungicidal target. Inhibition of FAS2 by cerulenin impeds the growth of wild-type and heterozygous strains (Ref.4).

Sequence similarities

Belongs to the fungal fatty acid synthetase subunit alpha family.

Contains 1 acyl carrier domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 18841884Fatty acid synthase subunit alpha HAMAP-Rule MF_00101
PRO_0000419251

Regions

Domain142 – 303162Acyl carrier
Region677 – 873197Beta-ketoacyl reductase By similarity
Region1147 – 1361215Beta-ketoacyl synthase By similarity
Region1770 – 17723Acetyl-CoA binding By similarity
Region1815 – 183117Acetyl-CoA binding By similarity
Region1839 – 18424Acetyl-CoA binding By similarity
Region1869 – 18713Acetyl-CoA binding By similarity

Sites

Active site13031For beta-ketoacyl synthase activity By similarity
Metal binding17701Magnesium By similarity
Metal binding17711Magnesium; via carbonyl oxygen By similarity
Metal binding17721Magnesium By similarity
Metal binding18701Magnesium By similarity
Metal binding18711Magnesium; via carbonyl oxygen By similarity
Binding site17961Acetyl-CoA By similarity
Binding site18061Acetyl-CoA By similarity

Amino acid modifications

Modified residue1821O-(pantetheine 4'-phosphoryl)serine By similarity

Sequences

Sequence LengthMass (Da)Tools
G8BAW7 [UniParc].

Last modified January 25, 2012. Version 1.
Checksum: 33DCED9F65C58282

FASTA1,884206,941
        10         20         30         40         50         60 
MKPEIEQELS HTLLTELLAY QFASPVRWIE TQDVFLKQHN TERVIEIGPS PTLAGMASRT 

        70         80         90        100        110        120 
IKAKYQSYDA ALSLQRQVLC YSKDAKEIYY TPDPAEPPAA EEPKAETGKE SAPAASAAAA 

       130        140        150        160        170        180 
AATQPAAAVA PPPQSAGPVE SIPDEPVKAS LLIHVLVAQK LKKPLDAVPM SKAIKDLVNG 

       190        200        210        220        230        240 
KSTVQNEILG DLGKEFGSTP EKPEETPLEE LAEQFQDTFS GSLGKTSTSL IGRLMSSKMP 

       250        260        270        280        290        300 
GGFSITNARK YLESRFGLGP GRQDSVLLTA LCNEPASRLG SEGDAKSFLD TMAQKYASHA 

       310        320        330        340        350        360 
GISLSSPSAG GASSGAGAAV VDSAALDALI AENKKLARQQ LETLARYLQV DLTKGEKAFI 

       370        380        390        400        410        420 
KEKEATTVLQ QELDLWEAEH GEFYAKGIKP VFSPLKSRTY DSYWNWARQD LLSMWFDILF 

       430        440        450        460        470        480 
GKLTSVDRET INQCIQIMNR ANPTLIKFMQ YHVELCPTYR GETYKLGKRL GEQLIENCKQ 

       490        500        510        520        530        540 
ILGQSPVYKD VSRITGPKTT VSAKGDIVYE EANKESVRKF EQYVFEMAQG GSMTKMKQSS 

       550        560        570        580        590        600 
IQEDLARVYK AISKQASRDS KLELQKVYDQ LLKVVEGSTE IETEQTTQDA LAIPTGSNTP 

       610        620        630        640        650        660 
TEEDELSTAS DDDEIASLPD KTSIAQPVSS TIPNKTIPFL HIQSKSESGN WEYDRKLSSI 

       670        680        690        700        710        720 
YLDGLESAAI NGLTFKDKYV LVTGAGAGSI GAEILQGLIS GGAKVIVTTS RYSKKVTEYY 

       730        740        750        760        770        780 
QNMYARYGAA GSTLIVVPFN QGSKQDVDAL VEYIYNDQKK GGLGWDLDVI IPFAAIPENG 

       790        800        810        820        830        840 
NGIDNIDSKS EFAHRIMLTN LLRLLGAVKA RKTTDTRPAQ CILPLSPNHG TFGFDGLYSE 

       850        860        870        880        890        900 
SKISLETLFN RWYSEDWGTK LTICGAIIGW TRGTGLMSAN NIIAEGIEKL GVRTFSQKEM 

       910        920        930        940        950        960 
AFNILGLLTP EIVNLCQEEP VMADLNGGLQ FIDNLKEFTS KLRNDLTETA DIRRAVSIES 

       970        980        990       1000       1010       1020 
AIEQKVVNGD NVDSNYNKVT VRPRANMKFD FPTLKSYDEI KQIAPDLEGM LDLENVVVVT 

      1030       1040       1050       1060       1070       1080 
GFAEVGPWGN ARTRWEMESK GEFSLEGAIE MAWIMGMIKY HNGNLKGKPY SGWIDAKTQT 

      1090       1100       1110       1120       1130       1140 
PVDDKDIKAK YEEEILEHSG IRLIEPELFN GYDPKKKQMI QEVVIQHDLE PFECSKETAE 

      1150       1160       1170       1180       1190       1200 
QYKHEHGDKC EISEIEESGE YSVRILKGAT LFIPKALRFD RLVAGQIPTG WDARTYGIPE 

      1210       1220       1230       1240       1250       1260 
DTINQVDPIT LYVLVATVEA LLSAGITDPY EFYKYVHVSE VGNCSGSGMG GVSALRGMFK 

      1270       1280       1290       1300       1310       1320 
DRYADKPVQN DILQESFINT MSAWVNMLLL SASGPIKTPV GACATAVESV DIGIETILSG 

      1330       1340       1350       1360       1370       1380 
KAKVVMVGGY DDFQEEGSYE FANMNATSSA IDEFKHGRTP KEMSRPTTTT RNGFMEAQGS 

      1390       1400       1410       1420       1430       1440 
GIQVIMSADL ALKMGVPIHA VLAMSATATD KIGRSVPAPG KGILTTAREH HGNLKYPSPL 

      1450       1460       1470       1480       1490       1500 
LNVKYRKRQL SKRLDQIKSW ESSELNYLQE EAHLAKEEFG EEFSEAEFLR ERTEEIYRES 

      1510       1520       1530       1540       1550       1560 
KRQVADAKKQ WGNAFYKSDP RIAPLRGALA TFNLTIDDIG VASFHGTSTV ANDKNESATI 

      1570       1580       1590       1600       1610       1620 
DSMMKHLGRS EGNPVFGVFQ KYLTGHPKGA AGAWMLNGAI QILESGIVPG NRNADNVDKV 

      1630       1640       1650       1660       1670       1680 
LEQYEYVLYP SRSIQTDGIK AVSVTSFGFG QKGAQAVVVH PDYLYAVLDR STYEDYAKRV 

      1690       1700       1710       1720       1730       1740 
TARNKKTYRY MHNAITRNTM FVAKDKAPYS DELTMDVYLD PLARVSKTKN EFVFTKKSVQ 

      1750       1760       1770       1780       1790       1800 
SDKSYVSNIA NSTAKALSSL NKSSKGVGVD VELLSELNID NETFLERNFT PEEIKYCQNS 

      1810       1820       1830       1840       1850       1860 
ANPQASFTGT WSAKEATFKA LGVSSQGGGA SLKEIEIVRD GNGAPQVVLN DNAKAAAKAA 

      1870       1880 
GVKNVNVSIS HDDFQATAVA LSEF 

« Hide

References

« Hide 'large scale' references
[1]"Evolution of pathogenicity and sexual reproduction in eight Candida genomes."
Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S., Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I., Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C., Fitzpatrick D.A., de Groot P.W.J. expand/collapse author list , Harris D., Hoyer L.L., Hube B., Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D., Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T., Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C., Birren B.W., Kellis M., Cuomo C.A.
Nature 459:657-662(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CDC 317 / ATCC MYA-4646.
[2]"Using RNA-seq to determine the transcriptional landscape and the hypoxic response of the pathogenic yeast Candida parapsilosis."
Guida A., Lindstaedt C., Maguire S.L., Ding C., Higgins D.G., Corton N.J., Berriman M., Butler G.
BMC Genomics 12:628-628(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: CDC 317 / ATCC MYA-4646.
[3]"Correlation between biofilm formation and the hypoxic response in Candida parapsilosis."
Rossignol T., Ding C., Guida A., d'Enfert C., Higgins D.G., Butler G.
Eukaryot. Cell 8:550-559(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY HYPOXIA AND BIOFILM FORMATION.
[4]"Fatty acid synthase impacts the pathobiology of Candida parapsilosis in vitro and during mammalian infection."
Nguyen L.N., Trofa D., Nosanchuk J.D.
PLoS ONE 4:E8421-E8421(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION BY CARBON SOURCES, DISRUPTION PHENOTYPE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
HE605205 Genomic DNA. Translation: CCE42191.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

OrthoDBEOG76QFRJ.

Family and domain databases

Gene3D3.40.366.10. 1 hit.
3.40.47.10. 3 hits.
3.40.50.720. 1 hit.
3.90.470.20. 1 hit.
HAMAPMF_00101. AcpS.
InterProIPR008278. 4-PPantetheinyl_Trfase_SF.
IPR001227. Ac_transferase_dom.
IPR002582. ACPS.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR026025. FAS_alpha_yeast.
IPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR016040. NAD(P)-bd_dom.
IPR004568. PPantethiene-prot_Trfase_dom.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
PfamPF01648. ACPS. 1 hit.
PF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
[Graphical view]
PIRSFPIRSF000454. FAS_yeast_alpha. 1 hit.
ProDomPD004282. PPantethiene-prot_Trfase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF52151. SSF52151. 1 hit.
SSF53901. SSF53901. 4 hits.
SSF56214. SSF56214. 1 hit.
TIGRFAMsTIGR00556. pantethn_trn. 1 hit.
PROSITEPS00606. B_KETOACYL_SYNTHASE. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFAS2_CANPC
AccessionPrimary (citable) accession number: G8BAW7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2012
Last sequence update: January 25, 2012
Last modified: February 19, 2014
This is version 16 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families