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P43098 (FAS2_CANAX) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 101. 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
OrganismCandida albicans (Yeast)
Taxonomic identifier5476 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length1885 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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. HAMAP-Rule MF_00101

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

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

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 – 18851885Fatty acid synthase subunit alpha HAMAP-Rule MF_00101
PRO_0000180284

Regions

Domain141 – 302162Acyl carrier
Region1157 – 1885729Beta-ketoacyl synthase HAMAP-Rule MF_00101
Region1771 – 17733Acetyl-CoA binding By similarity
Region1816 – 183217Acetyl-CoA binding By similarity
Region1840 – 18434Acetyl-CoA binding By similarity
Region1870 – 18723Acetyl-CoA binding By similarity

Sites

Active site13041For beta-ketoacyl synthase activity By similarity
Metal binding17711Magnesium By similarity
Metal binding17721Magnesium; via carbonyl oxygen By similarity
Metal binding17731Magnesium By similarity
Metal binding18711Magnesium By similarity
Metal binding18721Magnesium; via carbonyl oxygen By similarity
Binding site17971Acetyl-CoA By similarity
Binding site18071Acetyl-CoA By similarity

Amino acid modifications

Modified residue1811O-(pantetheine 4'-phosphoryl)serine By similarity

Sequences

Sequence LengthMass (Da)Tools
P43098 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 4835D57F362372E0

FASTA1,885207,589
        10         20         30         40         50         60 
MKPEIEQELS HTLLTELLAY QFASPVRWIE TQDVFLKQHN TERIIEIGPS PTLAGMANRT 

        70         80         90        100        110        120 
IKAKYESYDA ALSLQRQVLC YSKDAKEIYY KPDPADLAPK ETPKQEESTP SAPAAATPTP 

       130        140        150        160        170        180 
AAAAAPTPAP APASAGPVES IPDEPVKANL LIHVLVAQKL KKPLDAVPMT KAIKDLVNGK 

       190        200        210        220        230        240 
STVQNEILGD LGKEFGSTPE KPEDTPLEEL AEQFQDSFSG QLGKTSTSLI GRLMSSKMPG 

       250        260        270        280        290        300 
GFSITTARKY LESRFGLGAG RQDSVLLMAL TNEPANRLGS EADAKTFFDG IAQKYASSAG 

       310        320        330        340        350        360 
ISLSSGAGSG AGAANSGGAV VDSAALDALT AENKKLAKQQ LEVLARYLQS RLKQGSLKSF 

       370        380        390        400        410        420 
IKEKEASAVL QKELDLWEAE HGEFYAKGIQ PTFSALKSRT YDSYWNWARQ DVLSMYFDII 

       430        440        450        460        470        480 
FGKLTSVDRE TINQCIQIMN RANPTLIKFM QYHIDHCPEY KGETYKLAKR LGQQLIDNCK 

       490        500        510        520        530        540 
QVLTEDPVYK DVSRITGPKT KVSAKGNIEY EETQKDSVRK FEQYVYEMAQ GGAMTKVSQP 

       550        560        570        580        590        600 
TIQEDLARVY KAISKQASKD SKLELQRVYE DLLKVVESSK EIETEQLTKD ILQAATVPTT 

       610        620        630        640        650        660 
PTEEVDDPCT PSSDDEIASL PDKTSIIQPV SSTIPSQTIP FLHIQKKTKD GWEYNKKLSS 

       670        680        690        700        710        720 
LYLDGLESAA INGLTFKDKY VLVTGAGAGS IGAEILQGLI SGGAKVIVTT SRFSKKVTEY 

       730        740        750        760        770        780 
YQNMYARYGA AGSTLIVVPF NQGSKQDVDA LVQYIYDEPK KGGLGWDLDA IIPFAAIPEN 

       790        800        810        820        830        840 
GNGLDNIDSK SEFAHRIMLT NLLRLLGAVK SKKPTDTRPA QCILPLSPNH GTFGFDGLYS 

       850        860        870        880        890        900 
ESKISLETLF NRWYSEDWGS KLTVCGAVIG WTRGTGLMSA NNIIAEGIEK LGVRTFSQKE 

       910        920        930        940        950        960 
MAFNILGLLT PEIVQLCQEE PVMADLNGGL QFIDNLKDFT SKLRTDLLET ADIRRAVSIE 

       970        980        990       1000       1010       1020 
SAIEQKVVNG DNVDANYSKV MVEPRANMKF DFPTLKSYDE IKQIAPELEG MLDLENVVVV 

      1030       1040       1050       1060       1070       1080 
TGFAEVGPWG NSRTRWEMEA YGEFSLEGAI EMAWIMGFIK YHNGNLQGKP YSGWVDAKTQ 

      1090       1100       1110       1120       1130       1140 
TPIDEKDIKS KYEEEILEHS GIRLIEPELF NGYDPKKKQM IQEIVVQHDL EPFECSKETA 

      1150       1160       1170       1180       1190       1200 
EQYKHEHGEK CEIFEIEESG EYTVRILKGA TLYVPKALRF DRLVAGQIPT GWDARTYGIP 

      1210       1220       1230       1240       1250       1260 
EDTISQVDPI TLYVLVATVE ALLSAGITDP YEFYKYVHVS EVGNCSGSGM GGVSALRGMF 

      1270       1280       1290       1300       1310       1320 
KDRYADKPVQ NDILQESFIN TMSAWVNMLL LSSSGPIKTP VGACATAVES VDIGIETILS 

      1330       1340       1350       1360       1370       1380 
GKAKVVLVGG YDDFQEEGSY EFANMNATSN SIEEFKHGRT PKEMSRPTTT TRNGFMEAQG 

      1390       1400       1410       1420       1430       1440 
SGIQVIMTAD LALKMGVPIH AVLAMTATAT DKIGRSVPAP GKGILTTARE HHGNLKYPSP 

      1450       1460       1470       1480       1490       1500 
LLNIKYRKRQ LNKRLEQIKS WEETELSYLQ EEAELAKEEF GDEFSMHEFL KERTEEVYRE 

      1510       1520       1530       1540       1550       1560 
SKRQVSDAKK QWGNSFYKSD PRIAPLRGAL AAFNLTIDDI GVASFHGTST VANDKNESAT 

      1570       1580       1590       1600       1610       1620 
INNMMKHLGR SEGNPVFGVF QKYLTGHPKG AAGAWMLNGA IQILESGLVP GNRNADNVDK 

      1630       1640       1650       1660       1670       1680 
LLEQYEYVLY PSRSIQTDGI KAVSVTSFGF GQKGAQAVVV HPDYLFAVLD RSTYEEYATK 

      1690       1700       1710       1720       1730       1740 
VSARNKKTYR YMHNAITRNT MFVAKDKAPY SDELEQPVYL DPLARVEENK KKLVFSDKTI 

      1750       1760       1770       1780       1790       1800 
QSNQSYVGEV AQKTAKALST LNKSSKGVGV DVELLSAINI DNETFIERNF TGNEVEYCLN 

      1810       1820       1830       1840       1850       1860 
TAHPQASFTG TWSAKEAVFK ALGVESKGAG ASLIDIEITR DVNGAPKVIL HGEAKKAAAK 

      1870       1880 
AGVKNVNISI SHDDFQATAV ALSEF 

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References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L29063 Genomic DNA. Translation: AAA34345.1.
PIRJC4086.

3D structure databases

ProteinModelPortalP43098.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG4982.

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_CANAX
AccessionPrimary (citable) accession number: P43098
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: February 19, 2014
This is version 101 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