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Q5B7V0 (FAS2_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 68. 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
Gene names
Name:fasA
ORF Names:AN3380
OrganismEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) [Reference proteome]
Taxonomic identifier227321 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length1771 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

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 By similarity.

Catalytic activity

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.

Subunit structure

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

Induction

Induced by oleic acid and stearic acid, but not by linoleic acid. Ref.3

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 – 17711771Fatty acid synthase subunit alpha
PRO_0000419253

Regions

Domain141 – 302162Acyl carrier
Region575 – 771197Beta-ketoacyl reductase By similarity
Region1041 – 1255215Beta-ketoacyl synthase By similarity
Region1650 – 16523Acetyl-CoA binding By similarity
Region1695 – 171117Acetyl-CoA binding By similarity
Region1719 – 17224Acetyl-CoA binding By similarity
Region1753 – 17553Acetyl-CoA binding By similarity

Sites

Active site11971For beta-ketoacyl synthase activity By similarity
Metal binding16501Magnesium By similarity
Metal binding16511Magnesium; via carbonyl oxygen By similarity
Metal binding16521Magnesium By similarity
Metal binding17541Magnesium By similarity
Metal binding17551Magnesium; via carbonyl oxygen By similarity
Binding site16761Acetyl-CoA By similarity
Binding site16861Acetyl-CoA By similarity

Amino acid modifications

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

Sequences

Sequence LengthMass (Da)Tools
Q5B7V0 [UniParc].

Last modified April 26, 2005. Version 1.
Checksum: AFD90A5A2137EED1

FASTA1,771194,939
        10         20         30         40         50         60 
MAISSTADLA PSRKARGSES NDRALKLFIE LLSVETQQQL FRGEPCIQRF VEIGPRTILS 

        70         80         90        100        110        120 
TMAKRSASIQ KDQRSSASCY SPEFLSYHDN QPEILYQYQN DQAIYPLSQP TQPQFEPTSP 

       130        140        150        160        170        180 
SHLTKRSPSP SKALPMSAIP SAELTLQAGH VILAMTAQKL RRRFDQVPVE KTIRDLSGGK 

       190        200        210        220        230        240 
STLQNELTGD LVAEFGRVPE GVEDQPLSSL AESFQPEFSG IPGKAMSTLI SRFISGKMPA 

       250        260        270        280        290        300 
GFNQSAIQEY LNSRWGLTKS HATIPLCFAP TMEPARRLAN ADEARAYLDD LVEKHAAFQG 

       310        320        330        340        350        360 
ISLVPSNQVA DGHESLAPVV MNVADVDEMN KRTKLYRAQF DSLASYLGVD YFASEKAMSE 

       370        380        390        400        410        420 
SESRIAELEE TIRLLNTELD EQFIKGIKPS FNIKQVRKYD SWWNWSREEL IRLLNEICQD 

       430        440        450        460        470        480 
SSSACPPDME NRLQNLLNKW DANCSEIVRA HLIGLQSRSS APMNKLQLIL EEIFTLGNQT 

       490        500        510        520        530        540 
LSIDPLFVHN LPPMGPQTII TDAGCLEYHE LPRQISHYPE AMAYGPPWPQ GHTSAPFIHI 

       550        560        570        580        590        600 
KTREDGQDWM YDSKATSIYH AMLDVGVTTG LTFTHKAVLV TGAGPSSIAA SVIQGLLSGG 

       610        620        630        640        650        660 
ARIIVTTSRS ISQSADFYQQ MYRQYGAKGS SLSLFPFNQA SKQDCEQLVQ HIYGPDSPTD 

       670        680        690        700        710        720 
GDLDYILPFA AIPQVGEPDA FGGRQELALR AMLVNILRLI GFVRQEKERL RIENRPTMIV 

       730        740        750        760        770        780 
LPMSCNEGTF GGDGLYSEAK IGLKALFNRF YSENWSKYLT ICGAVIGWTR GTAIMQTSNA 

       790        800        810        820        830        840 
VAEEVEKLGV ITFTQAEMAF NILALMTPAL TALAEDTPIY ADLTGGLGSM WNIKQEISAA 

       850        860        870        880        890        900 
RKRISERQIL QIAIAEEDAR EQAMICSAST DVESGLPTTR HARLGLQFPP LPDVNEGYPN 

       910        920        930        940        950        960 
IEGMIDLTRI PVIVGYSELG PWGNARTRWE IEHRGDFSLE GYIEMAWIMG LIKHVDGHAK 

       970        980        990       1000       1010       1020 
GRPYVGWVDA DTETPIQDYE VPHKYHKHIM AHAGLRLIKP TKLDSYDPSR KELLHEVAVE 

      1030       1040       1050       1060       1070       1080 
EDLAPFETSK STAEAFKLRH GDCVTLLPIA DSDNCRVYIK KGAVLMIPKA VPFDQVVAGR 

      1090       1100       1110       1120       1130       1140 
IPEGWDPARY GIPEEIVQQV DVTTLYALCC VSEAFLSAGI KDPYEIYQYI HVSELANCLG 

      1150       1160       1170       1180       1190       1200 
SGGGPMKVIQ NMYRDRFLDR QIRGDIILEH FVNTMGAWVN MLLLSATGPL KTPVGACATA 

      1210       1220       1230       1240       1250       1260 
IESLDIGCEA IQNGRCKVAV VGGCDDYGEE LAFEFANIKA TANSTEELSK GRTPADISRP 

      1270       1280       1290       1300       1310       1320 
TASSRSGFAE SAGCGVQILM SAALAIEMGL PIYGVVAYTH MASDQIGRSI PAPGKGILTA 

      1330       1340       1350       1360       1370       1380 
ARENGQAKES PLLDLNFRRA VFDAEVALIN KSHPKQATTL KPDHSETSNA ASLRIRDAQN 

      1390       1400       1410       1420       1430       1440 
RWANNIRLSD PSISPIRASL ATWGLTVDDI KVVSMHGTST KANEVNEGNV INTQMRHLGR 

      1450       1460       1470       1480       1490       1500 
QMGNPLLAVC QKSLTGHPKA GAGAWQLNGC LQMMQENIVP GNRNADNIDK QLREFEHIVY 

      1510       1520       1530       1540       1550       1560 
PMESLRVPEI KATLLTSFGF GQKGAINIMV SPRYLFASLS NSDYEDYRSR TTKRQRSATP 

      1570       1580       1590       1600       1610       1620 
TFVSRIMKNN LVQVKTRPPW NDPEAMQNFF LDPNSRVVDG QITRAPRTAY KHQDISVPQS 

      1630       1640       1650       1660       1670       1680 
AAVSVNEALH AMLATTDHSS PAASASVGVD VEEISSINVD NPIFISRNFT LLERDYCLSA 

      1690       1700       1710       1720       1730       1740 
PDPRASFAGR WVAKEAAFKS LQTTSTGAGT AMDQIEILEV GGIPKVVRLT SQLHGHAHEV 

      1750       1760       1770 
AFAQGITNIQ ITISHCNNTA IAVALALRKN D 

« Hide

References

« Hide 'large scale' references
[1]"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae."
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. expand/collapse author list , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.
Nature 438:1105-1115(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[2]"The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G. expand/collapse author list , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[3]"Two Delta9-stearic acid desaturases are required for Aspergillus nidulans growth and development."
Wilson R.A., Chang P.K., Dobrzyn A., Ntambi J.M., Zarnowski R., Keller N.P.
Fungal Genet. Biol. 41:501-509(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY FATTY ACIDS.
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AACD01000055 Genomic DNA. Translation: EAA63348.1.
BN001306 Genomic DNA. Translation: CBF82822.1.
RefSeqXP_660984.1. XM_655892.1.

3D structure databases

ProteinModelPortalQ5B7V0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING162425.CADANIAP00009660.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00009660; CADANIAP00009660; CADANIAG00009660.
GeneID2874362.
KEGGani:AN3380.2.

Phylogenomic databases

eggNOGCOG4982.
HOGENOMHOG000177974.
OMACCVSEAF.
OrthoDBEOG7BGHV1.

Family and domain databases

Gene3D3.40.47.10. 2 hits.
3.40.50.720. 1 hit.
3.90.470.20. 1 hit.
InterProIPR008278. 4-PPantetheinyl_Trfase_SF.
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]
SUPFAMSSF53901. 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_EMENI
AccessionPrimary (citable) accession number: Q5B7V0
Secondary accession number(s): C8VHP2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2012
Last sequence update: April 26, 2005
Last modified: February 19, 2014
This is version 68 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