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Q765N2

- FAS2_LACKL

UniProt

Q765N2 - FAS2_LACKL

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Protein

Fatty acid synthase subunit alpha

Gene

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+.
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 sitei1305 – 13051For beta-ketoacyl synthase activityBy similarity
Metal bindingi1774 – 17741MagnesiumBy similarity
Metal bindingi1775 – 17751Magnesium; via carbonyl oxygenBy similarity
Metal bindingi1776 – 17761MagnesiumBy similarity
Binding sitei1800 – 18001Acetyl-CoABy similarity
Binding sitei1810 – 18101Acetyl-CoABy similarity
Metal bindingi1874 – 18741MagnesiumBy similarity
Metal bindingi1875 – 18751Magnesium; 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

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 alphaPRO_0000419252Add
BLAST

Amino acid modifications

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

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 reductaseBy similarityAdd
BLAST
Regioni1149 – 1363215Beta-ketoacyl synthaseBy similarityAdd
BLAST
Regioni1774 – 17763Acetyl-CoA bindingBy similarity
Regioni1819 – 183517Acetyl-CoA bindingBy similarityAdd
BLAST
Regioni1843 – 18464Acetyl-CoA bindingBy similarity
Regioni1873 – 18753Acetyl-CoA bindingBy 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

Contains 1 acyl carrier domain.Curated

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

« Hide

        10         20         30         40         50
MAMKPEVEQE LAHVLLTELL AYQFASPVRW IETQDVFLKD FNTERVVEIG
60 70 80 90 100
PSPTLAGMAQ RTIKNKYESY DAALSLQRQV LCYSKDAKEI YYTPDPADLA
110 120 130 140 150
PVEEPNAEEQ TGAAATPAAA AAPAAAAAAP AAPAARPVAE LPDEAVKASL
160 170 180 190 200
LLHVLVAQKL KKSLEQVPMS KTIKDLVGGK STVQNEILGD LGKEFGSTPE
210 220 230 240 250
KPEETPLEEL AETFQDTFAG SLGKQSSSLI SRLMSSKMPG GFTITVARKY
260 270 280 290 300
LQTRWGLGSG RQDSVLLIAL TNEPASRLGG EADAKSFLDS MAQKYASISG
310 320 330 340 350
VDLSSASAGA SAGAGAGGAG GATIDAAAFE ELTKDQKVMA RQQLEVLARY
360 370 380 390 400
LKMDLNGGEK KFLQEKNTVA ELQSQLDYLN NELGEYFIQG ISTSFSRKKA
410 420 430 440 450
RVFDSSWNWA KQALLTLYFQ IIHGVLKNVD REVVTEAINI MNRSNETLIK
460 470 480 490 500
FMEYHISHCD ENNGENYKLA KTLGHQLIEN CKQVLDMDPV YKDISKPTGP
510 520 530 540 550
KTNIDKNGNI KYSEEPRAAV RKLSQYVQEM ALGGPLTKES QPTIQEDLTR
560 570 580 590 600
VYKAINAQAA EHNISDSTKL EFEKLYGELL KFLETSNEID ASATTRLAGV
610 620 630 640 650
VDDDLDKDST KEVASLPNKS EISKNVSSII PRETVPFLHL KKKLPSCEWA
660 670 680 690 700
YDRQLSTLFL DGLEKAAING VTFKDKYVLI TGAGAGSIGA EVLQGLVQGG
710 720 730 740 750
AKVIVTTSRF SKKVTDYYQS IYAQYGAKGS TLVVVPFNQG SKQDVEALID
760 770 780 790 800
FIYDDEKNGG LGWDLDAVIP FAAIPENGIE LDKIDSKSEF AHRIMLTNIL
810 820 830 840 850
RMLGSVKKQK SARGIETRPA QVILPLSPNH GTFGGDGMYS ESKLSLETLF
860 870 880 890 900
NRWHSESWSN QLTICGAIIG WTRGTGLMNA NNIIAEGIEK MGVRTFSQKE
910 920 930 940 950
MAFNLLGLLI PEVVNLCQRS PVMADLNGGL QFLTDLKEFT GKLRGELTET
960 970 980 990 1000
SEIRKAVSIE TALEHKTVAG ANADAAFAQV EVQPRANIQL EFPTLKPYET
1010 1020 1030 1040 1050
VKKIGSPDLE GLLDLEKVIV VTGFSEVGPW GSSRTRGEME AFGEFSLEGC
1060 1070 1080 1090 1100
VEMSWIMGLI KYHNGNLKGR PYTGWVDSKT NEPVDDKDIK AKDESHVLEH
1110 1120 1130 1140 1150
SGIRLIEPEL FNSYNPEKKQ MIQEVVIEED LEPFEASKET AEQFKHEHGD
1160 1170 1180 1190 1200
KVDIFEIPET GEFSVRLLKG ATLYIPKALR FDRLVAGQIP TGWNAKTYGI
1210 1220 1230 1240 1250
SDDTISQVDP ITLFVLVSVI EAFIASGITD PYEMYKYVHV SEVGNCSGSG
1260 1270 1280 1290 1300
MGGVSALRGM FKDRYKDQPV QNDILQESFI NTMSAWVNML LISSSGPIKT
1310 1320 1330 1340 1350
PVGACATAVE SLDIGVETIL SGKAKICIVG GYDDFQEEGS YEFGNMNATS
1360 1370 1380 1390 1400
NSLDEFDHGR TPAEMSRPAT TTRNGFMEAQ GAGIQVIMNA DLALKMGVPI
1410 1420 1430 1440 1450
YGILALTATA TDKIGRSVPA PGKGILTTAR EHHGNLKFPT PLLDIKYRKR
1460 1470 1480 1490 1500
QLKNREAQIK QWVETELEML KYEAEGIPAE DQETFYAERT EEIKREATRQ
1510 1520 1530 1540 1550
LKSAQAQWGS EFYKNDPRIA PLRGALATYG LTIDDLGVAS FHGTSTKAND
1560 1570 1580 1590 1600
KNESATINEM MKHLGRSEGN PVLGVFQKYL TGHPKGAAGA WMMNGALQIL
1610 1620 1630 1640 1650
NSGIVPGNRN ADNVDKLLQQ FEYILYPSRS LKTDGIKAVS VTSFGFGQKG
1660 1670 1680 1690 1700
AQAVAVHPDF LYAAVDEATY NAYVAKVTAR EKAAYKYFHN GMIHNTLFVS
1710 1720 1730 1740 1750
KEHAPYSDEL EQPVYLDPLA RVSSDKKTGA LVFNGKGIQS SSQFVSEENR
1760 1770 1780 1790 1800
KTATIVSELA KKTAGTDASG VGVDVELIKS INVENDTFIE RNFTEAEIAY
1810 1820 1830 1840 1850
CKKQPSVQSS FAGTWSAKEA VFKSLGVKSQ GGGASLKDIE ITREAGKGPE
1860 1870 1880
VVLHGAAKEA ATKANVKNVK VSISHDDFQS VAVAVSEK
Length:1,888
Mass (Da):206,206
Last modified:July 5, 2004 - v1
Checksum:i6301BD0A025B7919
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB115969 Genomic DNA. Translation: BAD08376.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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: October 1, 2014
This is version 66 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