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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+.
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 sitei1279 – 12791For beta-ketoacyl synthase activityBy similarity
Metal bindingi1746 – 17461MagnesiumBy similarity
Metal bindingi1747 – 17471Magnesium; via carbonyl oxygenBy similarity
Metal bindingi1748 – 17481MagnesiumBy similarity
Binding sitei1772 – 17721Acetyl-CoABy similarity
Binding sitei1782 – 17821Acetyl-CoABy similarity
Metal bindingi1844 – 18441MagnesiumBy similarity
Metal bindingi1845 – 18451Magnesium; via carbonyl oxygenBy 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 alphaPRO_0000419254Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei178 – 1781O-(pantetheine 4'-phosphoryl)serineBy 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.
ModBaseiSearch...
MobiDBiSearch...

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 reductaseBy similarityAdd
BLAST
Regioni1123 – 1337215Beta-ketoacyl synthaseBy similarityAdd
BLAST
Regioni1746 – 17483Acetyl-CoA bindingBy similarity
Regioni1791 – 180717Acetyl-CoA bindingBy similarityAdd
BLAST
Regioni1815 – 18184Acetyl-CoA bindingBy similarity
Regioni1843 – 18453Acetyl-CoA bindingBy similarity

Sequence similaritiesi

Contains 1 acyl carrier domain.Curated

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

« Hide

        10         20         30         40         50
MRPEIEQELA HTLLVELLAY QFASPVRWIE TQDVILAEKR TERIVEIGPA
60 70 80 90 100
DTLGGMARRT LASKYEAYDA ATSVQRQILC YNKDAKEIYY DVDPVEEETE
110 120 130 140 150
SAPEAAAAPP TSAAPAAAVV AAPAPAASAP SAGPAAPVED APVTALDIVR
160 170 180 190 200
TLVAQKLKKA LSDVPLNKAI KDLVGGKSTL QNEILGDLGK EFGSTPEKPE
210 220 230 240 250
DTPLDELGAS MQATFNGQLG KQSSSLIARL VSSKMPGGFN ITAVRKYLET
260 270 280 290 300
RWGLGPGRQD GVLLLALTME PASRIGSEPD AKVFLDDVAN KYAANSGISL
310 320 330 340 350
NVPTASGDGG ASAGGMLMDP AAIDALTKDQ RALFKQQLEI IARYLKMDLR
360 370 380 390 400
DGQKAFVASQ ETQKTLQAQL DLWQAEHGDF YASGIEPSFD PLKARVYDSS
410 420 430 440 450
WNWARQDALS MYYDIIFGRL KVVDREIVSQ CIRIMNRSNP LLLEFMQYHI
460 470 480 490 500
DNCPTERGET YQLAKELGEQ LIENCKEVLG VSPVYKDVAV PTGPQTTIDA
510 520 530 540 550
RGNIEYQEVP RASARKLEHY VKQMAEGGPI SEYSNRAKVQ NDLRSVYKLI
560 570 580 590 600
RRQHRLSKSS QLQFNALYKD VVRALSMNEN QIMPQENGST KKPGRNGSVR
610 620 630 640 650
NGSPRAGKVE TIPFLHLKKK NEHGWDYSKK LTGIYLDVLE SAARSGLTFQ
660 670 680 690 700
GKNVLMTGAG AGSIGAEVLQ GLISGGAKVI VTTSRYSREV TEYYQAMYAR
710 720 730 740 750
YGARGSQLVV VPFNQGSKQD VEALVDYIYD TKKGLGWDLD FIVPFAAIPE
760 770 780 790 800
NGREIDSIDS KSELAHRIML TNLLRLLGSV KAQKQANGFE TRPAQVILPL
810 820 830 840 850
SPNHGTFGND GLYSESKLAL ETLFNRWYSE NWSNYLTICG AVIGWTRGTG
860 870 880 890 900
LMSGNNMVAE GVEKLGVRTF SQQEMAFNLL GLMAPAIVNL CQLDPVWADL
910 920 930 940 950
NGGLQFIPDL KDLMTRLRTE IMETSDVRRA VIKETAIENK VVNGEDSEVL
960 970 980 990 1000
YKKVIAEPRA NIKFQFPNLP TWDEDIKPLN ENLKGMVNLD KVVVVTGFSE
1010 1020 1030 1040 1050
VGPWGNSRTR WEMEASGKFS LEGCVEMAWI MGLIRHHNGP IKGKTYSGWV
1060 1070 1080 1090 1100
DSKTGEPVDD KDVKAKYEKY ILEHSGIRLI EPELFKGYDP KKKQLLQEIV
1110 1120 1130 1140 1150
IEEDLEPFEA SKETAEEFKR EHGEKVEIFE VLESGEYTVR LKKGATLLIP
1160 1170 1180 1190 1200
KALQFDRLVA GQVPTGWDAR RYGIPEDIIE QVDPVTLFVL VCTAEAMLSA
1210 1220 1230 1240 1250
GVTDPYEFYK YVHLSEVGNC IGSGIGGTHA LRGMYKDRYL DKPLQKDILQ
1260 1270 1280 1290 1300
ESFINTMSAW VNMLLLSSTG PIKTPVGACA TAVESVDIGY ETIVEGKARV
1310 1320 1330 1340 1350
CFVGGFDDFQ EEGSYEFANM KATSNAEDEF AHGRTPQEMS RPTTTTRAGF
1360 1370 1380 1390 1400
MESQGCGMQL IMSAQLALDM GVPIYGIIAL TTTATDKIGR SVPAPGQGVL
1410 1420 1430 1440 1450
TTARENPGKF PSPLLDIKYR RRQLELRKRQ IREWQESELL YLQEEAEAIK
1460 1470 1480 1490 1500
AQNPADFVVE EYLQERAQHI NREAIRQEKD AQFSLGNNFW KQDSRIAPLR
1510 1520 1530 1540 1550
GALATWGLTV DEIGVASFHG TSTVANDKNE SDVICQQMKH LGRKKGNALL
1560 1570 1580 1590 1600
GIFQKYLTGH PKGAAGAWMF NGCLQVLDSG LVPGNRNADN VDKVMEKFDY
1610 1620 1630 1640 1650
IVYPSRSIQT DGIKAFSVTS FGFGQKGAQV IGIHPKYLYA TLDRAQFEAY
1660 1670 1680 1690 1700
RAKVETRQKK AYRYFHNGLV NNSIFVAKNK APYEDELQSK VFLNPDYRVA
1710 1720 1730 1740 1750
ADKKTSELKY PPKPPVATDA GSESTKAVIE SLAKAHATEN SKIGVDVESI
1760 1770 1780 1790 1800
DSINISNETF IERILPASEQ QYCQNAPSPQ SSFAGRWSAK EAVFKSLGVC
1810 1820 1830 1840 1850
SKGAGAPLKD IEIENDSNGA PTLHGVAAEA AKEAGVKHIS VSISHSDMQA

VAVAISQF
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: October 1, 2014
This is version 86 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