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G8BAW7

- FAS2_CANPC

UniProt

G8BAW7 - FAS2_CANPC

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Protein

Fatty acid synthase subunit alpha

Gene

FAS2

Organism
Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

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.1 Publication

Catalytic activityi

Acetyl-CoA + n malonyl-CoA + 2n NADPH = long-chain-acyl-CoA + n CoA + n CO2 + 2n NADP+.
Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein].
(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP+ = 3-oxoacyl-[acyl-carrier-protein] + NADPH.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei1303 – 13031For beta-ketoacyl synthase activityBy similarity
Metal bindingi1770 – 17701MagnesiumBy similarity
Metal bindingi1771 – 17711Magnesium; via carbonyl oxygenBy similarity
Metal bindingi1772 – 17721MagnesiumBy similarity
Binding sitei1796 – 17961Acetyl-CoABy similarity
Binding sitei1806 – 18061Acetyl-CoABy similarity
Metal bindingi1870 – 18701MagnesiumBy similarity
Metal bindingi1871 – 18711Magnesium; via carbonyl oxygenBy similarity

GO - Molecular functioni

  1. 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity Source: UniProtKB-EC
  2. 3-oxoacyl-[acyl-carrier-protein] synthase activity Source: UniProtKB-EC
  3. fatty-acyl-CoA synthase activity Source: UniProtKB-EC
  4. holo-[acyl-carrier-protein] synthase activity Source: InterPro
  5. magnesium ion binding Source: InterPro

GO - Biological processi

  1. fatty acid biosynthetic process Source: CGD
  2. macromolecule biosynthetic process Source: InterPro
  3. pathogenesis Source: CGD
  4. single-species biofilm formation on inanimate substrate Source: CGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Transferase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

Magnesium, Metal-binding, NAD, NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Fatty acid synthase subunit alpha (EC:2.3.1.86)
Including the following 3 domains:
Acyl carrier
3-oxoacyl-[acyl-carrier-protein] reductase (EC:1.1.1.100)
Alternative name(s):
Beta-ketoacyl reductase
3-oxoacyl-[acyl-carrier-protein] synthase (EC:2.3.1.41)
Alternative name(s):
Beta-ketoacyl synthase
Gene namesi
Name:FAS2
ORF Names:CPAR2_807400
OrganismiCandida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Taxonomic identifieri578454 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida
ProteomesiUP000005221: Chromosome 8

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 18841884Fatty acid synthase subunit alphaPRO_0000419251Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei182 – 1821O-(pantetheine 4'-phosphoryl)serineBy similarity

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Expressioni

Inductioni

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.2 Publications

Interactioni

Subunit structurei

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini142 – 303162Acyl carrierAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni677 – 873197Beta-ketoacyl reductaseBy similarityAdd
BLAST
Regioni1147 – 1361215Beta-ketoacyl synthaseBy similarityAdd
BLAST
Regioni1770 – 17723Acetyl-CoA bindingBy similarity
Regioni1815 – 183117Acetyl-CoA bindingBy similarityAdd
BLAST
Regioni1839 – 18424Acetyl-CoA bindingBy similarity
Regioni1869 – 18713Acetyl-CoA bindingBy similarity

Sequence similaritiesi

Contains 1 acyl carrier domain.Curated

Phylogenomic databases

OrthoDBiEOG76QFRJ.

Family and domain databases

Gene3Di3.40.366.10. 1 hit.
3.40.47.10. 3 hits.
3.40.50.720. 1 hit.
3.90.470.20. 1 hit.
HAMAPiMF_00101. AcpS.
InterProiIPR008278. 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]
PfamiPF01648. ACPS. 1 hit.
PF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000454. FAS_yeast_alpha. 1 hit.
ProDomiPD004282. PPantethiene-prot_Trfase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF52151. SSF52151. 1 hit.
SSF53901. SSF53901. 4 hits.
SSF56214. SSF56214. 1 hit.
TIGRFAMsiTIGR00556. pantethn_trn. 1 hit.
PROSITEiPS00606. B_KETOACYL_SYNTHASE. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

G8BAW7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKPEIEQELS HTLLTELLAY QFASPVRWIE TQDVFLKQHN TERVIEIGPS
60 70 80 90 100
PTLAGMASRT IKAKYQSYDA ALSLQRQVLC YSKDAKEIYY TPDPAEPPAA
110 120 130 140 150
EEPKAETGKE SAPAASAAAA AATQPAAAVA PPPQSAGPVE SIPDEPVKAS
160 170 180 190 200
LLIHVLVAQK LKKPLDAVPM SKAIKDLVNG KSTVQNEILG DLGKEFGSTP
210 220 230 240 250
EKPEETPLEE LAEQFQDTFS GSLGKTSTSL IGRLMSSKMP GGFSITNARK
260 270 280 290 300
YLESRFGLGP GRQDSVLLTA LCNEPASRLG SEGDAKSFLD TMAQKYASHA
310 320 330 340 350
GISLSSPSAG GASSGAGAAV VDSAALDALI AENKKLARQQ LETLARYLQV
360 370 380 390 400
DLTKGEKAFI KEKEATTVLQ QELDLWEAEH GEFYAKGIKP VFSPLKSRTY
410 420 430 440 450
DSYWNWARQD LLSMWFDILF GKLTSVDRET INQCIQIMNR ANPTLIKFMQ
460 470 480 490 500
YHVELCPTYR GETYKLGKRL GEQLIENCKQ ILGQSPVYKD VSRITGPKTT
510 520 530 540 550
VSAKGDIVYE EANKESVRKF EQYVFEMAQG GSMTKMKQSS IQEDLARVYK
560 570 580 590 600
AISKQASRDS KLELQKVYDQ LLKVVEGSTE IETEQTTQDA LAIPTGSNTP
610 620 630 640 650
TEEDELSTAS DDDEIASLPD KTSIAQPVSS TIPNKTIPFL HIQSKSESGN
660 670 680 690 700
WEYDRKLSSI YLDGLESAAI NGLTFKDKYV LVTGAGAGSI GAEILQGLIS
710 720 730 740 750
GGAKVIVTTS RYSKKVTEYY QNMYARYGAA GSTLIVVPFN QGSKQDVDAL
760 770 780 790 800
VEYIYNDQKK GGLGWDLDVI IPFAAIPENG NGIDNIDSKS EFAHRIMLTN
810 820 830 840 850
LLRLLGAVKA RKTTDTRPAQ CILPLSPNHG TFGFDGLYSE SKISLETLFN
860 870 880 890 900
RWYSEDWGTK LTICGAIIGW TRGTGLMSAN NIIAEGIEKL GVRTFSQKEM
910 920 930 940 950
AFNILGLLTP EIVNLCQEEP VMADLNGGLQ FIDNLKEFTS KLRNDLTETA
960 970 980 990 1000
DIRRAVSIES AIEQKVVNGD NVDSNYNKVT VRPRANMKFD FPTLKSYDEI
1010 1020 1030 1040 1050
KQIAPDLEGM LDLENVVVVT GFAEVGPWGN ARTRWEMESK GEFSLEGAIE
1060 1070 1080 1090 1100
MAWIMGMIKY HNGNLKGKPY SGWIDAKTQT PVDDKDIKAK YEEEILEHSG
1110 1120 1130 1140 1150
IRLIEPELFN GYDPKKKQMI QEVVIQHDLE PFECSKETAE QYKHEHGDKC
1160 1170 1180 1190 1200
EISEIEESGE YSVRILKGAT LFIPKALRFD RLVAGQIPTG WDARTYGIPE
1210 1220 1230 1240 1250
DTINQVDPIT LYVLVATVEA LLSAGITDPY EFYKYVHVSE VGNCSGSGMG
1260 1270 1280 1290 1300
GVSALRGMFK DRYADKPVQN DILQESFINT MSAWVNMLLL SASGPIKTPV
1310 1320 1330 1340 1350
GACATAVESV DIGIETILSG KAKVVMVGGY DDFQEEGSYE FANMNATSSA
1360 1370 1380 1390 1400
IDEFKHGRTP KEMSRPTTTT RNGFMEAQGS GIQVIMSADL ALKMGVPIHA
1410 1420 1430 1440 1450
VLAMSATATD KIGRSVPAPG KGILTTAREH HGNLKYPSPL LNVKYRKRQL
1460 1470 1480 1490 1500
SKRLDQIKSW ESSELNYLQE EAHLAKEEFG EEFSEAEFLR ERTEEIYRES
1510 1520 1530 1540 1550
KRQVADAKKQ WGNAFYKSDP RIAPLRGALA TFNLTIDDIG VASFHGTSTV
1560 1570 1580 1590 1600
ANDKNESATI DSMMKHLGRS EGNPVFGVFQ KYLTGHPKGA AGAWMLNGAI
1610 1620 1630 1640 1650
QILESGIVPG NRNADNVDKV LEQYEYVLYP SRSIQTDGIK AVSVTSFGFG
1660 1670 1680 1690 1700
QKGAQAVVVH PDYLYAVLDR STYEDYAKRV TARNKKTYRY MHNAITRNTM
1710 1720 1730 1740 1750
FVAKDKAPYS DELTMDVYLD PLARVSKTKN EFVFTKKSVQ SDKSYVSNIA
1760 1770 1780 1790 1800
NSTAKALSSL NKSSKGVGVD VELLSELNID NETFLERNFT PEEIKYCQNS
1810 1820 1830 1840 1850
ANPQASFTGT WSAKEATFKA LGVSSQGGGA SLKEIEIVRD GNGAPQVVLN
1860 1870 1880
DNAKAAAKAA GVKNVNVSIS HDDFQATAVA LSEF
Length:1,884
Mass (Da):206,941
Last modified:January 25, 2012 - v1
Checksum:i33DCED9F65C58282
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
HE605205 Genomic DNA. Translation: CCE42191.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
HE605205 Genomic DNA. Translation: CCE42191.1 .

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

OrthoDBi EOG76QFRJ.

Family and domain databases

Gene3Di 3.40.366.10. 1 hit.
3.40.47.10. 3 hits.
3.40.50.720. 1 hit.
3.90.470.20. 1 hit.
HAMAPi MF_00101. AcpS.
InterProi IPR008278. 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 ]
Pfami PF01648. ACPS. 1 hit.
PF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
[Graphical view ]
PIRSFi PIRSF000454. FAS_yeast_alpha. 1 hit.
ProDomi PD004282. PPantethiene-prot_Trfase. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SUPFAMi SSF52151. SSF52151. 1 hit.
SSF53901. SSF53901. 4 hits.
SSF56214. SSF56214. 1 hit.
TIGRFAMsi TIGR00556. pantethn_trn. 1 hit.
PROSITEi PS00606. B_KETOACYL_SYNTHASE. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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.

Entry informationi

Entry nameiFAS2_CANPC
AccessioniPrimary (citable) accession number: G8BAW7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2012
Last sequence update: January 25, 2012
Last modified: October 29, 2014
This is version 18 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

It can potentially be a fungicidal target. Inhibition of FAS2 by cerulenin impeds the growth of wild-type and heterozygous strains (PubMed:20027295).1 Publication

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3