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P78615 (FAS2_EMEND) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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:fasA
OrganismEmericella nidulans (Aspergillus nidulans)
Taxonomic identifier162425 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length1858 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. 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.

Disruption phenotype

Unable to grow on minimal medium unless supplemented with myristic acid. 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 – 18581858Fatty acid synthase subunit alpha HAMAP-Rule MF_00101
PRO_0000419254

Regions

Domain138 – 299162Acyl carrier
Region651 – 848198Beta-ketoacyl reductase By similarity
Region1123 – 1337215Beta-ketoacyl synthase By similarity
Region1746 – 17483Acetyl-CoA binding By similarity
Region1791 – 180717Acetyl-CoA binding By similarity
Region1815 – 18184Acetyl-CoA binding By similarity
Region1843 – 18453Acetyl-CoA binding By similarity

Sites

Active site12791For beta-ketoacyl synthase activity By similarity
Metal binding17461Magnesium By similarity
Metal binding17471Magnesium; via carbonyl oxygen By similarity
Metal binding17481Magnesium By similarity
Metal binding18441Magnesium By similarity
Metal binding18451Magnesium; via carbonyl oxygen By similarity
Binding site17721Acetyl-CoA By similarity
Binding site17821Acetyl-CoA By similarity

Amino acid modifications

Modified residue1781O-(pantetheine 4'-phosphoryl)serine By similarity

Sequences

Sequence LengthMass (Da)Tools
P78615 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 3D961E8716C9E24D

FASTA1,858204,732
        10         20         30         40         50         60 
MRPEIEQELA HTLLVELLAY QFASPVRWIE TQDVILAEKR TERIVEIGPA DTLGGMARRT 

        70         80         90        100        110        120 
LASKYEAYDA ATSVQRQILC YNKDAKEIYY DVDPVEEETE SAPEAAAAPP TSAAPAAAVV 

       130        140        150        160        170        180 
AAPAPAASAP SAGPAAPVED APVTALDIVR TLVAQKLKKA LSDVPLNKAI KDLVGGKSTL 

       190        200        210        220        230        240 
QNEILGDLGK EFGSTPEKPE DTPLDELGAS MQATFNGQLG KQSSSLIARL VSSKMPGGFN 

       250        260        270        280        290        300 
ITAVRKYLET RWGLGPGRQD GVLLLALTME PASRIGSEPD AKVFLDDVAN KYAANSGISL 

       310        320        330        340        350        360 
NVPTASGDGG ASAGGMLMDP AAIDALTKDQ RALFKQQLEI IARYLKMDLR DGQKAFVASQ 

       370        380        390        400        410        420 
ETQKTLQAQL DLWQAEHGDF YASGIEPSFD PLKARVYDSS WNWARQDALS MYYDIIFGRL 

       430        440        450        460        470        480 
KVVDREIVSQ CIRIMNRSNP LLLEFMQYHI DNCPTERGET YQLAKELGEQ LIENCKEVLG 

       490        500        510        520        530        540 
VSPVYKDVAV PTGPQTTIDA RGNIEYQEVP RASARKLEHY VKQMAEGGPI SEYSNRAKVQ 

       550        560        570        580        590        600 
NDLRSVYKLI RRQHRLSKSS QLQFNALYKD VVRALSMNEN QIMPQENGST KKPGRNGSVR 

       610        620        630        640        650        660 
NGSPRAGKVE TIPFLHLKKK NEHGWDYSKK LTGIYLDVLE SAARSGLTFQ GKNVLMTGAG 

       670        680        690        700        710        720 
AGSIGAEVLQ GLISGGAKVI VTTSRYSREV TEYYQAMYAR YGARGSQLVV VPFNQGSKQD 

       730        740        750        760        770        780 
VEALVDYIYD TKKGLGWDLD FIVPFAAIPE NGREIDSIDS KSELAHRIML TNLLRLLGSV 

       790        800        810        820        830        840 
KAQKQANGFE TRPAQVILPL SPNHGTFGND GLYSESKLAL ETLFNRWYSE NWSNYLTICG 

       850        860        870        880        890        900 
AVIGWTRGTG LMSGNNMVAE GVEKLGVRTF SQQEMAFNLL GLMAPAIVNL CQLDPVWADL 

       910        920        930        940        950        960 
NGGLQFIPDL KDLMTRLRTE IMETSDVRRA VIKETAIENK VVNGEDSEVL YKKVIAEPRA 

       970        980        990       1000       1010       1020 
NIKFQFPNLP TWDEDIKPLN ENLKGMVNLD KVVVVTGFSE VGPWGNSRTR WEMEASGKFS 

      1030       1040       1050       1060       1070       1080 
LEGCVEMAWI MGLIRHHNGP IKGKTYSGWV DSKTGEPVDD KDVKAKYEKY ILEHSGIRLI 

      1090       1100       1110       1120       1130       1140 
EPELFKGYDP KKKQLLQEIV IEEDLEPFEA SKETAEEFKR EHGEKVEIFE VLESGEYTVR 

      1150       1160       1170       1180       1190       1200 
LKKGATLLIP KALQFDRLVA GQVPTGWDAR RYGIPEDIIE QVDPVTLFVL VCTAEAMLSA 

      1210       1220       1230       1240       1250       1260 
GVTDPYEFYK YVHLSEVGNC IGSGIGGTHA LRGMYKDRYL DKPLQKDILQ ESFINTMSAW 

      1270       1280       1290       1300       1310       1320 
VNMLLLSSTG PIKTPVGACA TAVESVDIGY ETIVEGKARV CFVGGFDDFQ EEGSYEFANM 

      1330       1340       1350       1360       1370       1380 
KATSNAEDEF AHGRTPQEMS RPTTTTRAGF MESQGCGMQL IMSAQLALDM GVPIYGIIAL 

      1390       1400       1410       1420       1430       1440 
TTTATDKIGR SVPAPGQGVL TTARENPGKF PSPLLDIKYR RRQLELRKRQ IREWQESELL 

      1450       1460       1470       1480       1490       1500 
YLQEEAEAIK AQNPADFVVE EYLQERAQHI NREAIRQEKD AQFSLGNNFW KQDSRIAPLR 

      1510       1520       1530       1540       1550       1560 
GALATWGLTV DEIGVASFHG TSTVANDKNE SDVICQQMKH LGRKKGNALL GIFQKYLTGH 

      1570       1580       1590       1600       1610       1620 
PKGAAGAWMF NGCLQVLDSG LVPGNRNADN VDKVMEKFDY IVYPSRSIQT DGIKAFSVTS 

      1630       1640       1650       1660       1670       1680 
FGFGQKGAQV IGIHPKYLYA TLDRAQFEAY RAKVETRQKK AYRYFHNGLV NNSIFVAKNK 

      1690       1700       1710       1720       1730       1740 
APYEDELQSK VFLNPDYRVA ADKKTSELKY PPKPPVATDA GSESTKAVIE SLAKAHATEN 

      1750       1760       1770       1780       1790       1800 
SKIGVDVESI DSINISNETF IERILPASEQ QYCQNAPSPQ SSFAGRWSAK EAVFKSLGVC 

      1810       1820       1830       1840       1850 
SKGAGAPLKD IEIENDSNGA PTLHGVAAEA AKEAGVKHIS VSISHSDMQA VAVAISQF 

« Hide

References

[1]"Aspergillus has distinct fatty acid synthases for primary and secondary metabolism."
Brown D.W., Adams T.H., Keller N.P.
Proc. Natl. Acad. Sci. U.S.A. 93:14873-14877(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE.
Strain: FGSC 89.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U75347 Genomic DNA. Translation: AAB41493.1.

3D structure databases

ProteinModelPortalP78615.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING162425.CADANIAP00001194.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG4982.

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. 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_EMEND
AccessionPrimary (citable) accession number: P78615
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2012
Last sequence update: May 1, 1997
Last modified: February 19, 2014
This is version 84 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