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P78615

- FAS2_EMEND

UniProt

P78615 - FAS2_EMEND

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Protein

Fatty acid synthase subunit alpha

Gene
fasA
Organism
Emericella nidulans (Aspergillus nidulans)
Status
Reviewed - Annotation score: 5 out of 5 - Protein inferred from homologyi

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.1 Publication

Catalytic activityi

Acetyl-CoA + n malonyl-CoA + 2n NADPH = long-chain-acyl-CoA + n CoA + n CO2 + 2n NADP+.UniRule annotation
Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein].UniRule annotation
(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP+ = 3-oxoacyl-[acyl-carrier-protein] + NADPH.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei1279 – 12791For beta-ketoacyl synthase activity By similarity
Metal bindingi1746 – 17461Magnesium By similarity
Metal bindingi1747 – 17471Magnesium; via carbonyl oxygen By similarity
Metal bindingi1748 – 17481Magnesium By similarity
Binding sitei1772 – 17721Acetyl-CoA By similarity
Binding sitei1782 – 17821Acetyl-CoA By similarity
Metal bindingi1844 – 18441Magnesium By similarity
Metal bindingi1845 – 18451Magnesium; 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-acyl-CoA synthase activity Source: UniProtKB-EC
  4. holo-[acyl-carrier-protein] synthase activity Source: InterPro
  5. magnesium ion binding Source: InterPro

GO - Biological processi

  1. fatty acid biosynthetic process Source: UniProtKB-KW
  2. macromolecule biosynthetic process Source: InterPro
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)
Alternative name(s):
Beta-ketoacyl synthase
Gene namesi
Name:fasA
OrganismiEmericella nidulans (Aspergillus nidulans)
Taxonomic identifieri162425 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Pathology & Biotechi

Disruption phenotypei

Unable to grow on minimal medium unless supplemented with myristic acid.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 18581858Fatty acid synthase subunit alphaUniRule annotationPRO_0000419254Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei178 – 1781O-(pantetheine 4'-phosphoryl)serine By similarity

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi162425.CADANIAP00001194.

Structurei

3D structure databases

ProteinModelPortaliP78615.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini138 – 299162Acyl carrierAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni651 – 848198Beta-ketoacyl reductase By similarityAdd
BLAST
Regioni1123 – 1337215Beta-ketoacyl synthase By similarityAdd
BLAST
Regioni1746 – 17483Acetyl-CoA binding By similarity
Regioni1791 – 180717Acetyl-CoA binding By similarityAdd
BLAST
Regioni1815 – 18184Acetyl-CoA binding By similarity
Regioni1843 – 18453Acetyl-CoA binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG4982.

Family and domain databases

Gene3Di3.40.366.10. 1 hit.
3.40.47.10. 2 hits.
3.40.50.720. 1 hit.
3.90.470.20. 1 hit.
HAMAPiMF_00101. AcpS.
InterProiIPR008278. 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]
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]
SUPFAMiSSF52151. SSF52151. 1 hit.
SSF53901. SSF53901. 4 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.

P78615-1 [UniParc]FASTAAdd to Basket

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MRPEIEQELA HTLLVELLAY QFASPVRWIE TQDVILAEKR TERIVEIGPA     50
DTLGGMARRT LASKYEAYDA ATSVQRQILC YNKDAKEIYY DVDPVEEETE 100
SAPEAAAAPP TSAAPAAAVV AAPAPAASAP SAGPAAPVED APVTALDIVR 150
TLVAQKLKKA LSDVPLNKAI KDLVGGKSTL QNEILGDLGK EFGSTPEKPE 200
DTPLDELGAS MQATFNGQLG KQSSSLIARL VSSKMPGGFN ITAVRKYLET 250
RWGLGPGRQD GVLLLALTME PASRIGSEPD AKVFLDDVAN KYAANSGISL 300
NVPTASGDGG ASAGGMLMDP AAIDALTKDQ RALFKQQLEI IARYLKMDLR 350
DGQKAFVASQ ETQKTLQAQL DLWQAEHGDF YASGIEPSFD PLKARVYDSS 400
WNWARQDALS MYYDIIFGRL KVVDREIVSQ CIRIMNRSNP LLLEFMQYHI 450
DNCPTERGET YQLAKELGEQ LIENCKEVLG VSPVYKDVAV PTGPQTTIDA 500
RGNIEYQEVP RASARKLEHY VKQMAEGGPI SEYSNRAKVQ NDLRSVYKLI 550
RRQHRLSKSS QLQFNALYKD VVRALSMNEN QIMPQENGST KKPGRNGSVR 600
NGSPRAGKVE TIPFLHLKKK NEHGWDYSKK LTGIYLDVLE SAARSGLTFQ 650
GKNVLMTGAG AGSIGAEVLQ GLISGGAKVI VTTSRYSREV TEYYQAMYAR 700
YGARGSQLVV VPFNQGSKQD VEALVDYIYD TKKGLGWDLD FIVPFAAIPE 750
NGREIDSIDS KSELAHRIML TNLLRLLGSV KAQKQANGFE TRPAQVILPL 800
SPNHGTFGND GLYSESKLAL ETLFNRWYSE NWSNYLTICG AVIGWTRGTG 850
LMSGNNMVAE GVEKLGVRTF SQQEMAFNLL GLMAPAIVNL CQLDPVWADL 900
NGGLQFIPDL KDLMTRLRTE IMETSDVRRA VIKETAIENK VVNGEDSEVL 950
YKKVIAEPRA NIKFQFPNLP TWDEDIKPLN ENLKGMVNLD KVVVVTGFSE 1000
VGPWGNSRTR WEMEASGKFS LEGCVEMAWI MGLIRHHNGP IKGKTYSGWV 1050
DSKTGEPVDD KDVKAKYEKY ILEHSGIRLI EPELFKGYDP KKKQLLQEIV 1100
IEEDLEPFEA SKETAEEFKR EHGEKVEIFE VLESGEYTVR LKKGATLLIP 1150
KALQFDRLVA GQVPTGWDAR RYGIPEDIIE QVDPVTLFVL VCTAEAMLSA 1200
GVTDPYEFYK YVHLSEVGNC IGSGIGGTHA LRGMYKDRYL DKPLQKDILQ 1250
ESFINTMSAW VNMLLLSSTG PIKTPVGACA TAVESVDIGY ETIVEGKARV 1300
CFVGGFDDFQ EEGSYEFANM KATSNAEDEF AHGRTPQEMS RPTTTTRAGF 1350
MESQGCGMQL IMSAQLALDM GVPIYGIIAL TTTATDKIGR SVPAPGQGVL 1400
TTARENPGKF PSPLLDIKYR RRQLELRKRQ IREWQESELL YLQEEAEAIK 1450
AQNPADFVVE EYLQERAQHI NREAIRQEKD AQFSLGNNFW KQDSRIAPLR 1500
GALATWGLTV DEIGVASFHG TSTVANDKNE SDVICQQMKH LGRKKGNALL 1550
GIFQKYLTGH PKGAAGAWMF NGCLQVLDSG LVPGNRNADN VDKVMEKFDY 1600
IVYPSRSIQT DGIKAFSVTS FGFGQKGAQV IGIHPKYLYA TLDRAQFEAY 1650
RAKVETRQKK AYRYFHNGLV NNSIFVAKNK APYEDELQSK VFLNPDYRVA 1700
ADKKTSELKY PPKPPVATDA GSESTKAVIE SLAKAHATEN SKIGVDVESI 1750
DSINISNETF IERILPASEQ QYCQNAPSPQ SSFAGRWSAK EAVFKSLGVC 1800
SKGAGAPLKD IEIENDSNGA PTLHGVAAEA AKEAGVKHIS VSISHSDMQA 1850
VAVAISQF 1858
Length:1,858
Mass (Da):204,732
Last modified:May 1, 1997 - v1
Checksum:i3D961E8716C9E24D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U75347 Genomic DNA. Translation: AAB41493.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U75347 Genomic DNA. Translation: AAB41493.1 .

3D structure databases

ProteinModelPortali P78615.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 162425.CADANIAP00001194.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG4982.

Family and domain databases

Gene3Di 3.40.366.10. 1 hit.
3.40.47.10. 2 hits.
3.40.50.720. 1 hit.
3.90.470.20. 1 hit.
HAMAPi MF_00101. AcpS.
InterProi IPR008278. 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 ]
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 SSF52151. SSF52151. 1 hit.
SSF53901. SSF53901. 4 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

  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.

Entry informationi

Entry nameiFAS2_EMEND
AccessioniPrimary (citable) accession number: P78615
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2012
Last sequence update: May 1, 1997
Last modified: June 11, 2014
This is version 85 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

Multifunctional enzyme

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi