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Protein

Fatty acid synthase subunit alpha

Gene

fasA

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

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 (By similarity).By similarity

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 sitei1197 – 11971For beta-ketoacyl synthase activityPROSITE-ProRule annotation
Metal bindingi1650 – 16501MagnesiumBy similarity
Metal bindingi1651 – 16511Magnesium; via carbonyl oxygenBy similarity
Metal bindingi1652 – 16521MagnesiumBy similarity
Binding sitei1676 – 16761Acetyl-CoABy similarity
Binding sitei1686 – 16861Acetyl-CoABy similarity
Metal bindingi1754 – 17541MagnesiumBy similarity
Metal bindingi1755 – 17551Magnesium; via carbonyl oxygenBy similarity

GO - Molecular functioni

GO - Biological processi

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)
Gene namesi
Name:fasA
ORF Names:AN3380
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000000560 Componenti: Chromosome VI

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 17711771Fatty acid synthase subunit alphaPRO_0000419253Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Expressioni

Inductioni

Induced by oleic acid and stearic acid, but not by linoleic acid.1 Publication

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliQ5B7V0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni575 – 771197Beta-ketoacyl reductaseBy similarityAdd
BLAST
Regioni1041 – 1255215Beta-ketoacyl synthaseBy similarityAdd
BLAST
Regioni1650 – 16523Acetyl-CoA bindingBy similarity
Regioni1695 – 171117Acetyl-CoA bindingBy similarityAdd
BLAST
Regioni1719 – 17224Acetyl-CoA bindingBy similarity
Regioni1753 – 17553Acetyl-CoA bindingBy similarity

Sequence similaritiesi

Contains 1 acyl carrier domain.Curated

Phylogenomic databases

eggNOGiCOG4982.
HOGENOMiHOG000177974.
InParanoidiQ5B7V0.
KOiK00667.
OMAiCCVSEAF.
OrthoDBiEOG7BGHV1.

Family and domain databases

Gene3Di3.40.47.10. 2 hits.
3.40.50.720. 1 hit.
3.90.470.20. 1 hit.
InterProiIPR008278. 4-PPantetheinyl_Trfase_SF.
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.
[Graphical view]
PfamiPF01648. ACPS. 1 hit.
PF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
[Graphical view]
ProDomiPD004282. PPantethiene-prot_Trfase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF53901. SSF53901. 3 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.

Q5B7V0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAISSTADLA PSRKARGSES NDRALKLFIE LLSVETQQQL FRGEPCIQRF
60 70 80 90 100
VEIGPRTILS TMAKRSASIQ KDQRSSASCY SPEFLSYHDN QPEILYQYQN
110 120 130 140 150
DQAIYPLSQP TQPQFEPTSP SHLTKRSPSP SKALPMSAIP SAELTLQAGH
160 170 180 190 200
VILAMTAQKL RRRFDQVPVE KTIRDLSGGK STLQNELTGD LVAEFGRVPE
210 220 230 240 250
GVEDQPLSSL AESFQPEFSG IPGKAMSTLI SRFISGKMPA GFNQSAIQEY
260 270 280 290 300
LNSRWGLTKS HATIPLCFAP TMEPARRLAN ADEARAYLDD LVEKHAAFQG
310 320 330 340 350
ISLVPSNQVA DGHESLAPVV MNVADVDEMN KRTKLYRAQF DSLASYLGVD
360 370 380 390 400
YFASEKAMSE SESRIAELEE TIRLLNTELD EQFIKGIKPS FNIKQVRKYD
410 420 430 440 450
SWWNWSREEL IRLLNEICQD SSSACPPDME NRLQNLLNKW DANCSEIVRA
460 470 480 490 500
HLIGLQSRSS APMNKLQLIL EEIFTLGNQT LSIDPLFVHN LPPMGPQTII
510 520 530 540 550
TDAGCLEYHE LPRQISHYPE AMAYGPPWPQ GHTSAPFIHI KTREDGQDWM
560 570 580 590 600
YDSKATSIYH AMLDVGVTTG LTFTHKAVLV TGAGPSSIAA SVIQGLLSGG
610 620 630 640 650
ARIIVTTSRS ISQSADFYQQ MYRQYGAKGS SLSLFPFNQA SKQDCEQLVQ
660 670 680 690 700
HIYGPDSPTD GDLDYILPFA AIPQVGEPDA FGGRQELALR AMLVNILRLI
710 720 730 740 750
GFVRQEKERL RIENRPTMIV LPMSCNEGTF GGDGLYSEAK IGLKALFNRF
760 770 780 790 800
YSENWSKYLT ICGAVIGWTR GTAIMQTSNA VAEEVEKLGV ITFTQAEMAF
810 820 830 840 850
NILALMTPAL TALAEDTPIY ADLTGGLGSM WNIKQEISAA RKRISERQIL
860 870 880 890 900
QIAIAEEDAR EQAMICSAST DVESGLPTTR HARLGLQFPP LPDVNEGYPN
910 920 930 940 950
IEGMIDLTRI PVIVGYSELG PWGNARTRWE IEHRGDFSLE GYIEMAWIMG
960 970 980 990 1000
LIKHVDGHAK GRPYVGWVDA DTETPIQDYE VPHKYHKHIM AHAGLRLIKP
1010 1020 1030 1040 1050
TKLDSYDPSR KELLHEVAVE EDLAPFETSK STAEAFKLRH GDCVTLLPIA
1060 1070 1080 1090 1100
DSDNCRVYIK KGAVLMIPKA VPFDQVVAGR IPEGWDPARY GIPEEIVQQV
1110 1120 1130 1140 1150
DVTTLYALCC VSEAFLSAGI KDPYEIYQYI HVSELANCLG SGGGPMKVIQ
1160 1170 1180 1190 1200
NMYRDRFLDR QIRGDIILEH FVNTMGAWVN MLLLSATGPL KTPVGACATA
1210 1220 1230 1240 1250
IESLDIGCEA IQNGRCKVAV VGGCDDYGEE LAFEFANIKA TANSTEELSK
1260 1270 1280 1290 1300
GRTPADISRP TASSRSGFAE SAGCGVQILM SAALAIEMGL PIYGVVAYTH
1310 1320 1330 1340 1350
MASDQIGRSI PAPGKGILTA ARENGQAKES PLLDLNFRRA VFDAEVALIN
1360 1370 1380 1390 1400
KSHPKQATTL KPDHSETSNA ASLRIRDAQN RWANNIRLSD PSISPIRASL
1410 1420 1430 1440 1450
ATWGLTVDDI KVVSMHGTST KANEVNEGNV INTQMRHLGR QMGNPLLAVC
1460 1470 1480 1490 1500
QKSLTGHPKA GAGAWQLNGC LQMMQENIVP GNRNADNIDK QLREFEHIVY
1510 1520 1530 1540 1550
PMESLRVPEI KATLLTSFGF GQKGAINIMV SPRYLFASLS NSDYEDYRSR
1560 1570 1580 1590 1600
TTKRQRSATP TFVSRIMKNN LVQVKTRPPW NDPEAMQNFF LDPNSRVVDG
1610 1620 1630 1640 1650
QITRAPRTAY KHQDISVPQS AAVSVNEALH AMLATTDHSS PAASASVGVD
1660 1670 1680 1690 1700
VEEISSINVD NPIFISRNFT LLERDYCLSA PDPRASFAGR WVAKEAAFKS
1710 1720 1730 1740 1750
LQTTSTGAGT AMDQIEILEV GGIPKVVRLT SQLHGHAHEV AFAQGITNIQ
1760 1770
ITISHCNNTA IAVALALRKN D
Length:1,771
Mass (Da):194,939
Last modified:April 26, 2005 - v1
Checksum:iAFD90A5A2137EED1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AACD01000055 Genomic DNA. Translation: EAA63348.1.
BN001306 Genomic DNA. Translation: CBF82822.1.
RefSeqiXP_660984.1. XM_655892.1.

Genome annotation databases

EnsemblFungiiCADANIAT00009660; CADANIAP00009660; CADANIAG00009660.
GeneIDi2874362.
KEGGiani:AN3380.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AACD01000055 Genomic DNA. Translation: EAA63348.1.
BN001306 Genomic DNA. Translation: CBF82822.1.
RefSeqiXP_660984.1. XM_655892.1.

3D structure databases

ProteinModelPortaliQ5B7V0.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANIAT00009660; CADANIAP00009660; CADANIAG00009660.
GeneIDi2874362.
KEGGiani:AN3380.2.

Phylogenomic databases

eggNOGiCOG4982.
HOGENOMiHOG000177974.
InParanoidiQ5B7V0.
KOiK00667.
OMAiCCVSEAF.
OrthoDBiEOG7BGHV1.

Family and domain databases

Gene3Di3.40.47.10. 2 hits.
3.40.50.720. 1 hit.
3.90.470.20. 1 hit.
InterProiIPR008278. 4-PPantetheinyl_Trfase_SF.
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.
[Graphical view]
PfamiPF01648. ACPS. 1 hit.
PF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
[Graphical view]
ProDomiPD004282. PPantethiene-prot_Trfase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF53901. SSF53901. 3 hits.
SSF56214. SSF56214. 1 hit.
TIGRFAMsiTIGR00556. pantethn_trn. 1 hit.
PROSITEiPS00606. B_KETOACYL_SYNTHASE. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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.
    , 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.

Entry informationi

Entry nameiFAS2_EMENI
AccessioniPrimary (citable) accession number: Q5B7V0
Secondary accession number(s): C8VHP2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2012
Last sequence update: April 26, 2005
Last modified: July 22, 2015
This is version 74 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

Complete proteome, Multifunctional enzyme, Reference proteome

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.