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Protein

Fatty acid synthase subunit alpha

Gene

FAS2

Organism
Candida albicans (Yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Protein inferred from homologyi

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.

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 sitei1304 – 13041For beta-ketoacyl synthase activityBy similarity
Metal bindingi1771 – 17711MagnesiumBy similarity
Metal bindingi1772 – 17721Magnesium; via carbonyl oxygenBy similarity
Metal bindingi1773 – 17731MagnesiumBy similarity
Binding sitei1797 – 17971Acetyl-CoABy similarity
Binding sitei1807 – 18071Acetyl-CoABy similarity
Metal bindingi1871 – 18711MagnesiumBy similarity
Metal bindingi1872 – 18721Magnesium; 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: UniProtKB-KW
  2. macromolecule biosynthetic process Source: InterPro
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
OrganismiCandida albicans (Yeast)
Taxonomic identifieri5476 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 18851885Fatty acid synthase subunit alphaPRO_0000180284Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei181 – 1811O-(pantetheine 4'-phosphoryl)serineBy similarity

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Interactioni

Subunit structurei

[Alpha6beta6] hexamers of two multifunctional subunits (alpha and beta).

Structurei

3D structure databases

ProteinModelPortaliP43098.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini141 – 302162Acyl carrierAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1157 – 1885729Beta-ketoacyl synthaseAdd
BLAST
Regioni1771 – 17733Acetyl-CoA bindingBy similarity
Regioni1816 – 183217Acetyl-CoA bindingBy similarityAdd
BLAST
Regioni1840 – 18434Acetyl-CoA bindingBy similarity
Regioni1870 – 18723Acetyl-CoA bindingBy similarity

Sequence similaritiesi

Contains 1 acyl carrier domain.Curated

Phylogenomic databases

eggNOGiCOG4982.

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. Ppantetheine-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.

P43098-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKPEIEQELS HTLLTELLAY QFASPVRWIE TQDVFLKQHN TERIIEIGPS
60 70 80 90 100
PTLAGMANRT IKAKYESYDA ALSLQRQVLC YSKDAKEIYY KPDPADLAPK
110 120 130 140 150
ETPKQEESTP SAPAAATPTP AAAAAPTPAP APASAGPVES IPDEPVKANL
160 170 180 190 200
LIHVLVAQKL KKPLDAVPMT KAIKDLVNGK STVQNEILGD LGKEFGSTPE
210 220 230 240 250
KPEDTPLEEL AEQFQDSFSG QLGKTSTSLI GRLMSSKMPG GFSITTARKY
260 270 280 290 300
LESRFGLGAG RQDSVLLMAL TNEPANRLGS EADAKTFFDG IAQKYASSAG
310 320 330 340 350
ISLSSGAGSG AGAANSGGAV VDSAALDALT AENKKLAKQQ LEVLARYLQS
360 370 380 390 400
RLKQGSLKSF IKEKEASAVL QKELDLWEAE HGEFYAKGIQ PTFSALKSRT
410 420 430 440 450
YDSYWNWARQ DVLSMYFDII FGKLTSVDRE TINQCIQIMN RANPTLIKFM
460 470 480 490 500
QYHIDHCPEY KGETYKLAKR LGQQLIDNCK QVLTEDPVYK DVSRITGPKT
510 520 530 540 550
KVSAKGNIEY EETQKDSVRK FEQYVYEMAQ GGAMTKVSQP TIQEDLARVY
560 570 580 590 600
KAISKQASKD SKLELQRVYE DLLKVVESSK EIETEQLTKD ILQAATVPTT
610 620 630 640 650
PTEEVDDPCT PSSDDEIASL PDKTSIIQPV SSTIPSQTIP FLHIQKKTKD
660 670 680 690 700
GWEYNKKLSS LYLDGLESAA INGLTFKDKY VLVTGAGAGS IGAEILQGLI
710 720 730 740 750
SGGAKVIVTT SRFSKKVTEY YQNMYARYGA AGSTLIVVPF NQGSKQDVDA
760 770 780 790 800
LVQYIYDEPK KGGLGWDLDA IIPFAAIPEN GNGLDNIDSK SEFAHRIMLT
810 820 830 840 850
NLLRLLGAVK SKKPTDTRPA QCILPLSPNH GTFGFDGLYS ESKISLETLF
860 870 880 890 900
NRWYSEDWGS KLTVCGAVIG WTRGTGLMSA NNIIAEGIEK LGVRTFSQKE
910 920 930 940 950
MAFNILGLLT PEIVQLCQEE PVMADLNGGL QFIDNLKDFT SKLRTDLLET
960 970 980 990 1000
ADIRRAVSIE SAIEQKVVNG DNVDANYSKV MVEPRANMKF DFPTLKSYDE
1010 1020 1030 1040 1050
IKQIAPELEG MLDLENVVVV TGFAEVGPWG NSRTRWEMEA YGEFSLEGAI
1060 1070 1080 1090 1100
EMAWIMGFIK YHNGNLQGKP YSGWVDAKTQ TPIDEKDIKS KYEEEILEHS
1110 1120 1130 1140 1150
GIRLIEPELF NGYDPKKKQM IQEIVVQHDL EPFECSKETA EQYKHEHGEK
1160 1170 1180 1190 1200
CEIFEIEESG EYTVRILKGA TLYVPKALRF DRLVAGQIPT GWDARTYGIP
1210 1220 1230 1240 1250
EDTISQVDPI TLYVLVATVE ALLSAGITDP YEFYKYVHVS EVGNCSGSGM
1260 1270 1280 1290 1300
GGVSALRGMF KDRYADKPVQ NDILQESFIN TMSAWVNMLL LSSSGPIKTP
1310 1320 1330 1340 1350
VGACATAVES VDIGIETILS GKAKVVLVGG YDDFQEEGSY EFANMNATSN
1360 1370 1380 1390 1400
SIEEFKHGRT PKEMSRPTTT TRNGFMEAQG SGIQVIMTAD LALKMGVPIH
1410 1420 1430 1440 1450
AVLAMTATAT DKIGRSVPAP GKGILTTARE HHGNLKYPSP LLNIKYRKRQ
1460 1470 1480 1490 1500
LNKRLEQIKS WEETELSYLQ EEAELAKEEF GDEFSMHEFL KERTEEVYRE
1510 1520 1530 1540 1550
SKRQVSDAKK QWGNSFYKSD PRIAPLRGAL AAFNLTIDDI GVASFHGTST
1560 1570 1580 1590 1600
VANDKNESAT INNMMKHLGR SEGNPVFGVF QKYLTGHPKG AAGAWMLNGA
1610 1620 1630 1640 1650
IQILESGLVP GNRNADNVDK LLEQYEYVLY PSRSIQTDGI KAVSVTSFGF
1660 1670 1680 1690 1700
GQKGAQAVVV HPDYLFAVLD RSTYEEYATK VSARNKKTYR YMHNAITRNT
1710 1720 1730 1740 1750
MFVAKDKAPY SDELEQPVYL DPLARVEENK KKLVFSDKTI QSNQSYVGEV
1760 1770 1780 1790 1800
AQKTAKALST LNKSSKGVGV DVELLSAINI DNETFIERNF TGNEVEYCLN
1810 1820 1830 1840 1850
TAHPQASFTG TWSAKEAVFK ALGVESKGAG ASLIDIEITR DVNGAPKVIL
1860 1870 1880
HGEAKKAAAK AGVKNVNISI SHDDFQATAV ALSEF
Length:1,885
Mass (Da):207,589
Last modified:November 1, 1995 - v1
Checksum:i4835D57F362372E0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L29063 Genomic DNA. Translation: AAA34345.1.
PIRiJC4086.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L29063 Genomic DNA. Translation: AAA34345.1.
PIRiJC4086.

3D structure databases

ProteinModelPortaliP43098.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiCOG4982.

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. Ppantetheine-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]
ProtoNetiSearch...

Publicationsi

  1. "Analysis and expression of the Candida albicans FAS2 gene."
    Southard S.B., Cihlar R.L.
    Gene 156:133-138(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 4918.

Entry informationi

Entry nameiFAS2_CANAX
AccessioniPrimary (citable) accession number: P43098
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: January 7, 2015
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Multifunctional enzyme

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.