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Q5B7V0

- FAS2_EMENI

UniProt

Q5B7V0 - FAS2_EMENI

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Protein
Fatty acid synthase subunit alpha
Gene
fasA, AN3380
Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed - Annotation score: 5 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.

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 activity By similarity
Metal bindingi1650 – 16501Magnesium By similarity
Metal bindingi1651 – 16511Magnesium; via carbonyl oxygen By similarity
Metal bindingi1652 – 16521Magnesium By similarity
Binding sitei1676 – 16761Acetyl-CoA By similarity
Binding sitei1686 – 16861Acetyl-CoA By similarity
Metal bindingi1754 – 17541Magnesium By similarity
Metal bindingi1755 – 17551Magnesium; via carbonyl oxygen By similarity

GO - Molecular functioni

  1. 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity Source: UniProtKB-EC
  2. 3-oxoacyl-[acyl-carrier-protein] synthase activity Source: UniProtKB-EC
  3. fatty acid synthase activity Source: ASPGD
  4. fatty-acyl-CoA synthase activity Source: UniProtKB-EC
  5. holo-[acyl-carrier-protein] synthase activity Source: InterPro
  6. magnesium ion binding Source: InterPro

GO - Biological processi

  1. fatty acid biosynthetic process Source: ASPGD
  2. macromolecule biosynthetic process Source: InterPro
  3. secondary metabolite biosynthetic process Source: ASPGD
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: Chromosome VI

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 17711771Fatty acid synthase subunit alpha
PRO_0000419253Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei181 – 1811O-(pantetheine 4'-phosphoryl)serine By 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.

Protein-protein interaction databases

STRINGi162425.CADANIAP00009660.

Structurei

3D structure databases

ProteinModelPortaliQ5B7V0.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni575 – 771197Beta-ketoacyl reductase By similarity
Add
BLAST
Regioni1041 – 1255215Beta-ketoacyl synthase By similarity
Add
BLAST
Regioni1650 – 16523Acetyl-CoA binding By similarity
Regioni1695 – 171117Acetyl-CoA binding By similarity
Add
BLAST
Regioni1719 – 17224Acetyl-CoA binding By similarity
Regioni1753 – 17553Acetyl-CoA binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG4982.
HOGENOMiHOG000177974.
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.
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]
PfamiPF01648. ACPS. 1 hit.
PF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000454. FAS_yeast_alpha. 1 hit.
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

MAISSTADLA PSRKARGSES NDRALKLFIE LLSVETQQQL FRGEPCIQRF     50
VEIGPRTILS TMAKRSASIQ KDQRSSASCY SPEFLSYHDN QPEILYQYQN 100
DQAIYPLSQP TQPQFEPTSP SHLTKRSPSP SKALPMSAIP SAELTLQAGH 150
VILAMTAQKL RRRFDQVPVE KTIRDLSGGK STLQNELTGD LVAEFGRVPE 200
GVEDQPLSSL AESFQPEFSG IPGKAMSTLI SRFISGKMPA GFNQSAIQEY 250
LNSRWGLTKS HATIPLCFAP TMEPARRLAN ADEARAYLDD LVEKHAAFQG 300
ISLVPSNQVA DGHESLAPVV MNVADVDEMN KRTKLYRAQF DSLASYLGVD 350
YFASEKAMSE SESRIAELEE TIRLLNTELD EQFIKGIKPS FNIKQVRKYD 400
SWWNWSREEL IRLLNEICQD SSSACPPDME NRLQNLLNKW DANCSEIVRA 450
HLIGLQSRSS APMNKLQLIL EEIFTLGNQT LSIDPLFVHN LPPMGPQTII 500
TDAGCLEYHE LPRQISHYPE AMAYGPPWPQ GHTSAPFIHI KTREDGQDWM 550
YDSKATSIYH AMLDVGVTTG LTFTHKAVLV TGAGPSSIAA SVIQGLLSGG 600
ARIIVTTSRS ISQSADFYQQ MYRQYGAKGS SLSLFPFNQA SKQDCEQLVQ 650
HIYGPDSPTD GDLDYILPFA AIPQVGEPDA FGGRQELALR AMLVNILRLI 700
GFVRQEKERL RIENRPTMIV LPMSCNEGTF GGDGLYSEAK IGLKALFNRF 750
YSENWSKYLT ICGAVIGWTR GTAIMQTSNA VAEEVEKLGV ITFTQAEMAF 800
NILALMTPAL TALAEDTPIY ADLTGGLGSM WNIKQEISAA RKRISERQIL 850
QIAIAEEDAR EQAMICSAST DVESGLPTTR HARLGLQFPP LPDVNEGYPN 900
IEGMIDLTRI PVIVGYSELG PWGNARTRWE IEHRGDFSLE GYIEMAWIMG 950
LIKHVDGHAK GRPYVGWVDA DTETPIQDYE VPHKYHKHIM AHAGLRLIKP 1000
TKLDSYDPSR KELLHEVAVE EDLAPFETSK STAEAFKLRH GDCVTLLPIA 1050
DSDNCRVYIK KGAVLMIPKA VPFDQVVAGR IPEGWDPARY GIPEEIVQQV 1100
DVTTLYALCC VSEAFLSAGI KDPYEIYQYI HVSELANCLG SGGGPMKVIQ 1150
NMYRDRFLDR QIRGDIILEH FVNTMGAWVN MLLLSATGPL KTPVGACATA 1200
IESLDIGCEA IQNGRCKVAV VGGCDDYGEE LAFEFANIKA TANSTEELSK 1250
GRTPADISRP TASSRSGFAE SAGCGVQILM SAALAIEMGL PIYGVVAYTH 1300
MASDQIGRSI PAPGKGILTA ARENGQAKES PLLDLNFRRA VFDAEVALIN 1350
KSHPKQATTL KPDHSETSNA ASLRIRDAQN RWANNIRLSD PSISPIRASL 1400
ATWGLTVDDI KVVSMHGTST KANEVNEGNV INTQMRHLGR QMGNPLLAVC 1450
QKSLTGHPKA GAGAWQLNGC LQMMQENIVP GNRNADNIDK QLREFEHIVY 1500
PMESLRVPEI KATLLTSFGF GQKGAINIMV SPRYLFASLS NSDYEDYRSR 1550
TTKRQRSATP TFVSRIMKNN LVQVKTRPPW NDPEAMQNFF LDPNSRVVDG 1600
QITRAPRTAY KHQDISVPQS AAVSVNEALH AMLATTDHSS PAASASVGVD 1650
VEEISSINVD NPIFISRNFT LLERDYCLSA PDPRASFAGR WVAKEAAFKS 1700
LQTTSTGAGT AMDQIEILEV GGIPKVVRLT SQLHGHAHEV AFAQGITNIQ 1750
ITISHCNNTA IAVALALRKN D 1771
Length:1,771
Mass (Da):194,939
Last modified:April 26, 2005 - v1
Checksum:iAFD90A5A2137EED1
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AACD01000055 Genomic DNA. Translation: EAA63348.1 .
BN001306 Genomic DNA. Translation: CBF82822.1 .
RefSeqi XP_660984.1. XM_655892.1.

3D structure databases

ProteinModelPortali Q5B7V0.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 162425.CADANIAP00009660.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADANIAT00009660 ; CADANIAP00009660 ; CADANIAG00009660 .
GeneIDi 2874362.
KEGGi ani:AN3380.2.

Phylogenomic databases

eggNOGi COG4982.
HOGENOMi HOG000177974.
OMAi CCVSEAF.
OrthoDBi EOG7BGHV1.

Family and domain databases

Gene3Di 3.40.47.10. 2 hits.
3.40.50.720. 1 hit.
3.90.470.20. 1 hit.
InterProi IPR008278. 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 ]
Pfami PF01648. ACPS. 1 hit.
PF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
[Graphical view ]
PIRSFi PIRSF000454. FAS_yeast_alpha. 1 hit.
ProDomi PD004282. PPantethiene-prot_Trfase. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SUPFAMi SSF53901. SSF53901. 3 hits.
SSF56214. SSF56214. 1 hit.
TIGRFAMsi TIGR00556. pantethn_trn. 1 hit.
PROSITEi PS00606. B_KETOACYL_SYNTHASE. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: February 19, 2014
This is version 68 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