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Q765N2 (FAS2_LACKL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 65. 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
Alternative name(s):
p190/210

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
Synonyms:Sk-FAS2
OrganismLachancea kluyveri (Yeast) (Saccharomyces kluyveri)
Taxonomic identifier4934 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeLachancea

Protein attributes

Sequence length1888 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. In this species, higher amounts of C18 than C16 fatty acids are produced. Ref.1

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.

Domain

The N-terminal ACP and almost all of the KR domains play an important role in determining the carbon chain length of fatty acids produced. Ref.1

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 – 18881888Fatty acid synthase subunit alpha HAMAP-Rule MF_00101
PRO_0000419252

Regions

Domain141 – 302162Acyl carrier
Region675 – 874200Beta-ketoacyl reductase By similarity
Region1149 – 1363215Beta-ketoacyl synthase By similarity
Region1774 – 17763Acetyl-CoA binding By similarity
Region1819 – 183517Acetyl-CoA binding By similarity
Region1843 – 18464Acetyl-CoA binding By similarity
Region1873 – 18753Acetyl-CoA binding By similarity

Sites

Active site13051For beta-ketoacyl synthase activity By similarity
Metal binding17741Magnesium By similarity
Metal binding17751Magnesium; via carbonyl oxygen By similarity
Metal binding17761Magnesium By similarity
Metal binding18741Magnesium By similarity
Metal binding18751Magnesium; via carbonyl oxygen By similarity
Binding site18001Acetyl-CoA By similarity
Binding site18101Acetyl-CoA By similarity

Amino acid modifications

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

Sequences

Sequence LengthMass (Da)Tools
Q765N2 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 6301BD0A025B7919

FASTA1,888206,206
        10         20         30         40         50         60 
MAMKPEVEQE LAHVLLTELL AYQFASPVRW IETQDVFLKD FNTERVVEIG PSPTLAGMAQ 

        70         80         90        100        110        120 
RTIKNKYESY DAALSLQRQV LCYSKDAKEI YYTPDPADLA PVEEPNAEEQ TGAAATPAAA 

       130        140        150        160        170        180 
AAPAAAAAAP AAPAARPVAE LPDEAVKASL LLHVLVAQKL KKSLEQVPMS KTIKDLVGGK 

       190        200        210        220        230        240 
STVQNEILGD LGKEFGSTPE KPEETPLEEL AETFQDTFAG SLGKQSSSLI SRLMSSKMPG 

       250        260        270        280        290        300 
GFTITVARKY LQTRWGLGSG RQDSVLLIAL TNEPASRLGG EADAKSFLDS MAQKYASISG 

       310        320        330        340        350        360 
VDLSSASAGA SAGAGAGGAG GATIDAAAFE ELTKDQKVMA RQQLEVLARY LKMDLNGGEK 

       370        380        390        400        410        420 
KFLQEKNTVA ELQSQLDYLN NELGEYFIQG ISTSFSRKKA RVFDSSWNWA KQALLTLYFQ 

       430        440        450        460        470        480 
IIHGVLKNVD REVVTEAINI MNRSNETLIK FMEYHISHCD ENNGENYKLA KTLGHQLIEN 

       490        500        510        520        530        540 
CKQVLDMDPV YKDISKPTGP KTNIDKNGNI KYSEEPRAAV RKLSQYVQEM ALGGPLTKES 

       550        560        570        580        590        600 
QPTIQEDLTR VYKAINAQAA EHNISDSTKL EFEKLYGELL KFLETSNEID ASATTRLAGV 

       610        620        630        640        650        660 
VDDDLDKDST KEVASLPNKS EISKNVSSII PRETVPFLHL KKKLPSCEWA YDRQLSTLFL 

       670        680        690        700        710        720 
DGLEKAAING VTFKDKYVLI TGAGAGSIGA EVLQGLVQGG AKVIVTTSRF SKKVTDYYQS 

       730        740        750        760        770        780 
IYAQYGAKGS TLVVVPFNQG SKQDVEALID FIYDDEKNGG LGWDLDAVIP FAAIPENGIE 

       790        800        810        820        830        840 
LDKIDSKSEF AHRIMLTNIL RMLGSVKKQK SARGIETRPA QVILPLSPNH GTFGGDGMYS 

       850        860        870        880        890        900 
ESKLSLETLF NRWHSESWSN QLTICGAIIG WTRGTGLMNA NNIIAEGIEK MGVRTFSQKE 

       910        920        930        940        950        960 
MAFNLLGLLI PEVVNLCQRS PVMADLNGGL QFLTDLKEFT GKLRGELTET SEIRKAVSIE 

       970        980        990       1000       1010       1020 
TALEHKTVAG ANADAAFAQV EVQPRANIQL EFPTLKPYET VKKIGSPDLE GLLDLEKVIV 

      1030       1040       1050       1060       1070       1080 
VTGFSEVGPW GSSRTRGEME AFGEFSLEGC VEMSWIMGLI KYHNGNLKGR PYTGWVDSKT 

      1090       1100       1110       1120       1130       1140 
NEPVDDKDIK AKDESHVLEH SGIRLIEPEL FNSYNPEKKQ MIQEVVIEED LEPFEASKET 

      1150       1160       1170       1180       1190       1200 
AEQFKHEHGD KVDIFEIPET GEFSVRLLKG ATLYIPKALR FDRLVAGQIP TGWNAKTYGI 

      1210       1220       1230       1240       1250       1260 
SDDTISQVDP ITLFVLVSVI EAFIASGITD PYEMYKYVHV SEVGNCSGSG MGGVSALRGM 

      1270       1280       1290       1300       1310       1320 
FKDRYKDQPV QNDILQESFI NTMSAWVNML LISSSGPIKT PVGACATAVE SLDIGVETIL 

      1330       1340       1350       1360       1370       1380 
SGKAKICIVG GYDDFQEEGS YEFGNMNATS NSLDEFDHGR TPAEMSRPAT TTRNGFMEAQ 

      1390       1400       1410       1420       1430       1440 
GAGIQVIMNA DLALKMGVPI YGILALTATA TDKIGRSVPA PGKGILTTAR EHHGNLKFPT 

      1450       1460       1470       1480       1490       1500 
PLLDIKYRKR QLKNREAQIK QWVETELEML KYEAEGIPAE DQETFYAERT EEIKREATRQ 

      1510       1520       1530       1540       1550       1560 
LKSAQAQWGS EFYKNDPRIA PLRGALATYG LTIDDLGVAS FHGTSTKAND KNESATINEM 

      1570       1580       1590       1600       1610       1620 
MKHLGRSEGN PVLGVFQKYL TGHPKGAAGA WMMNGALQIL NSGIVPGNRN ADNVDKLLQQ 

      1630       1640       1650       1660       1670       1680 
FEYILYPSRS LKTDGIKAVS VTSFGFGQKG AQAVAVHPDF LYAAVDEATY NAYVAKVTAR 

      1690       1700       1710       1720       1730       1740 
EKAAYKYFHN GMIHNTLFVS KEHAPYSDEL EQPVYLDPLA RVSSDKKTGA LVFNGKGIQS 

      1750       1760       1770       1780       1790       1800 
SSQFVSEENR KTATIVSELA KKTAGTDASG VGVDVELIKS INVENDTFIE RNFTEAEIAY 

      1810       1820       1830       1840       1850       1860 
CKKQPSVQSS FAGTWSAKEA VFKSLGVKSQ GGGASLKDIE ITREAGKGPE VVLHGAAKEA 

      1870       1880 
ATKANVKNVK VSISHDDFQS VAVAVSEK 

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References

[1]"Cloning and functional characterization of a fatty acid synthase component FAS2 gene from Saccharomyces kluyveri."
Oura T., Kajiwara S.
Curr. Genet. 49:393-402(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DOMAIN.
Strain: NBRC 1893 / Ks-133(+).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB115969 Genomic DNA. Translation: BAD08376.1.

3D structure databases

ProteinModelPortalQ765N2.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA2.3.1.86. 274780.

Family and domain databases

Gene3D3.40.366.10. 1 hit.
3.40.47.10. 2 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. 3 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_LACKL
AccessionPrimary (citable) accession number: Q765N2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2012
Last sequence update: July 5, 2004
Last modified: February 19, 2014
This is version 65 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