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Q765N2

- FAS2_LACKL

UniProt

Q765N2 - FAS2_LACKL

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Protein

Fatty acid synthase subunit alpha

Gene
FAS2, Sk-FAS2
Organism
Lachancea kluyveri (Yeast) (Saccharomyces kluyveri)
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. In this species, higher amounts of C18 than C16 fatty acids are produced.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 sitei1305 – 13051For beta-ketoacyl synthase activity By similarity
Metal bindingi1774 – 17741Magnesium By similarity
Metal bindingi1775 – 17751Magnesium; via carbonyl oxygen By similarity
Metal bindingi1776 – 17761Magnesium By similarity
Binding sitei1800 – 18001Acetyl-CoA By similarity
Binding sitei1810 – 18101Acetyl-CoA By similarity
Metal bindingi1874 – 18741Magnesium By similarity
Metal bindingi1875 – 18751Magnesium; 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

Enzyme and pathway databases

BRENDAi2.3.1.86. 274780.

Names & Taxonomyi

Protein namesi
Recommended name:
Fatty acid synthase subunit alpha (EC:2.3.1.86)
Alternative name(s):
p190/210
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:FAS2
Synonyms:Sk-FAS2
OrganismiLachancea kluyveri (Yeast) (Saccharomyces kluyveri)
Taxonomic identifieri4934 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeLachancea

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 18881888Fatty acid synthase subunit alphaUniRule annotationPRO_0000419252Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei181 – 1811O-(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.

Structurei

3D structure databases

ProteinModelPortaliQ765N2.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni675 – 874200Beta-ketoacyl reductase By similarityAdd
BLAST
Regioni1149 – 1363215Beta-ketoacyl synthase By similarityAdd
BLAST
Regioni1774 – 17763Acetyl-CoA binding By similarity
Regioni1819 – 183517Acetyl-CoA binding By similarityAdd
BLAST
Regioni1843 – 18464Acetyl-CoA binding By similarity
Regioni1873 – 18753Acetyl-CoA binding By similarity

Domaini

The N-terminal ACP and almost all of the KR domains play an important role in determining the carbon chain length of fatty acids produced.1 Publication

Sequence similaritiesi

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. 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.

Q765N2-1 [UniParc]FASTAAdd to Basket

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MAMKPEVEQE LAHVLLTELL AYQFASPVRW IETQDVFLKD FNTERVVEIG     50
PSPTLAGMAQ RTIKNKYESY DAALSLQRQV LCYSKDAKEI YYTPDPADLA 100
PVEEPNAEEQ TGAAATPAAA AAPAAAAAAP AAPAARPVAE LPDEAVKASL 150
LLHVLVAQKL KKSLEQVPMS KTIKDLVGGK STVQNEILGD LGKEFGSTPE 200
KPEETPLEEL AETFQDTFAG SLGKQSSSLI SRLMSSKMPG GFTITVARKY 250
LQTRWGLGSG RQDSVLLIAL TNEPASRLGG EADAKSFLDS MAQKYASISG 300
VDLSSASAGA SAGAGAGGAG GATIDAAAFE ELTKDQKVMA RQQLEVLARY 350
LKMDLNGGEK KFLQEKNTVA ELQSQLDYLN NELGEYFIQG ISTSFSRKKA 400
RVFDSSWNWA KQALLTLYFQ IIHGVLKNVD REVVTEAINI MNRSNETLIK 450
FMEYHISHCD ENNGENYKLA KTLGHQLIEN CKQVLDMDPV YKDISKPTGP 500
KTNIDKNGNI KYSEEPRAAV RKLSQYVQEM ALGGPLTKES QPTIQEDLTR 550
VYKAINAQAA EHNISDSTKL EFEKLYGELL KFLETSNEID ASATTRLAGV 600
VDDDLDKDST KEVASLPNKS EISKNVSSII PRETVPFLHL KKKLPSCEWA 650
YDRQLSTLFL DGLEKAAING VTFKDKYVLI TGAGAGSIGA EVLQGLVQGG 700
AKVIVTTSRF SKKVTDYYQS IYAQYGAKGS TLVVVPFNQG SKQDVEALID 750
FIYDDEKNGG LGWDLDAVIP FAAIPENGIE LDKIDSKSEF AHRIMLTNIL 800
RMLGSVKKQK SARGIETRPA QVILPLSPNH GTFGGDGMYS ESKLSLETLF 850
NRWHSESWSN QLTICGAIIG WTRGTGLMNA NNIIAEGIEK MGVRTFSQKE 900
MAFNLLGLLI PEVVNLCQRS PVMADLNGGL QFLTDLKEFT GKLRGELTET 950
SEIRKAVSIE TALEHKTVAG ANADAAFAQV EVQPRANIQL EFPTLKPYET 1000
VKKIGSPDLE GLLDLEKVIV VTGFSEVGPW GSSRTRGEME AFGEFSLEGC 1050
VEMSWIMGLI KYHNGNLKGR PYTGWVDSKT NEPVDDKDIK AKDESHVLEH 1100
SGIRLIEPEL FNSYNPEKKQ MIQEVVIEED LEPFEASKET AEQFKHEHGD 1150
KVDIFEIPET GEFSVRLLKG ATLYIPKALR FDRLVAGQIP TGWNAKTYGI 1200
SDDTISQVDP ITLFVLVSVI EAFIASGITD PYEMYKYVHV SEVGNCSGSG 1250
MGGVSALRGM FKDRYKDQPV QNDILQESFI NTMSAWVNML LISSSGPIKT 1300
PVGACATAVE SLDIGVETIL SGKAKICIVG GYDDFQEEGS YEFGNMNATS 1350
NSLDEFDHGR TPAEMSRPAT TTRNGFMEAQ GAGIQVIMNA DLALKMGVPI 1400
YGILALTATA TDKIGRSVPA PGKGILTTAR EHHGNLKFPT PLLDIKYRKR 1450
QLKNREAQIK QWVETELEML KYEAEGIPAE DQETFYAERT EEIKREATRQ 1500
LKSAQAQWGS EFYKNDPRIA PLRGALATYG LTIDDLGVAS FHGTSTKAND 1550
KNESATINEM MKHLGRSEGN PVLGVFQKYL TGHPKGAAGA WMMNGALQIL 1600
NSGIVPGNRN ADNVDKLLQQ FEYILYPSRS LKTDGIKAVS VTSFGFGQKG 1650
AQAVAVHPDF LYAAVDEATY NAYVAKVTAR EKAAYKYFHN GMIHNTLFVS 1700
KEHAPYSDEL EQPVYLDPLA RVSSDKKTGA LVFNGKGIQS SSQFVSEENR 1750
KTATIVSELA KKTAGTDASG VGVDVELIKS INVENDTFIE RNFTEAEIAY 1800
CKKQPSVQSS FAGTWSAKEA VFKSLGVKSQ GGGASLKDIE ITREAGKGPE 1850
VVLHGAAKEA ATKANVKNVK VSISHDDFQS VAVAVSEK 1888
Length:1,888
Mass (Da):206,206
Last modified:July 5, 2004 - v1
Checksum:i6301BD0A025B7919
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB115969 Genomic DNA. Translation: BAD08376.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB115969 Genomic DNA. Translation: BAD08376.1 .

3D structure databases

ProteinModelPortali Q765N2.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BRENDAi 2.3.1.86. 274780.

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. 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

  1. "Cloning and functional characterization of a fatty acid synthase component FAS2 gene from Saccharomyces kluyveri."
    Oura T., Kajiwara S.
    Curr. Genet. 49:393-402(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DOMAIN.
    Strain: NBRC 1893 / Ks-133(+).

Entry informationi

Entry nameiFAS2_LACKL
AccessioniPrimary (citable) accession number: Q765N2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2012
Last sequence update: July 5, 2004
Last modified: February 19, 2014
This is version 65 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