FAS2_LACKL
ID FAS2_LACKL Reviewed; 1888 AA.
AC Q765N2;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Fatty acid synthase subunit alpha;
DE EC=2.3.1.86;
DE AltName: Full=p190/210;
DE Includes:
DE RecName: Full=Acyl carrier;
DE Includes:
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase;
DE EC=1.1.1.100;
DE AltName: Full=Beta-ketoacyl reductase;
DE Includes:
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase;
DE EC=2.3.1.41;
DE AltName: Full=Beta-ketoacyl synthase;
GN Name=FAS2; Synonyms=Sk-FAS2;
OS Lachancea kluyveri (Yeast) (Saccharomyces kluyveri).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=4934;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DOMAIN.
RC STRAIN=NBRC 1893 / Ks-133(+);
RX PubMed=16479401; DOI=10.1007/s00294-006-0063-4;
RA Oura T., Kajiwara S.;
RT "Cloning and functional characterization of a fatty acid synthase component
RT FAS2 gene from Saccharomyces kluyveri.";
RL Curr. Genet. 49:393-402(2006).
CC -!- FUNCTION: Fatty acid synthetase catalyzes the formation of long-chain
CC fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The alpha subunit
CC contains domains for: acyl carrier protein, 3-oxoacyl-[acyl-carrier-
CC protein] reductase, and 3-oxoacyl-[acyl-carrier-protein] synthase. In
CC this species, higher amounts of C18 than C16 fatty acids are produced.
CC {ECO:0000269|PubMed:16479401}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + 2n H(+) + n malonyl-CoA + 2n NADPH = a long-chain
CC fatty acyl-CoA + n CO2 + n CoA + H2O + 2n NADP(+);
CC Xref=Rhea:RHEA:22896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:83139; EC=2.3.1.86;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP]
CC + CO2 + holo-[ACP]; Xref=Rhea:RHEA:22836, Rhea:RHEA-COMP:9623,
CC Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:14125,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78776, ChEBI:CHEBI:138651;
CC EC=2.3.1.41;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+)
CC + NADPH; Xref=Rhea:RHEA:17397, Rhea:RHEA-COMP:9916, Rhea:RHEA-
CC COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:78776, ChEBI:CHEBI:78827; EC=1.1.1.100;
CC -!- SUBUNIT: Fatty acid synthase is composed of alpha and beta subunits.
CC {ECO:0000250}.
CC -!- DOMAIN: The N-terminal ACP and almost all of the KR domains play an
CC important role in determining the carbon chain length of fatty acids
CC produced. {ECO:0000269|PubMed:16479401}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Fungal fatty acid
CC synthetase subunit alpha family. {ECO:0000305}.
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DR EMBL; AB115969; BAD08376.1; -; Genomic_DNA.
DR AlphaFoldDB; Q765N2; -.
DR SMR; Q765N2; -.
DR PRIDE; Q765N2; -.
DR BRENDA; 2.3.1.86; 6897.
DR GO; GO:0005835; C:fatty acid synthase complex; IEA:InterPro.
DR GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0004321; F:fatty-acyl-CoA synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.90.470.20; -; 1.
DR HAMAP; MF_00101; AcpS; 1.
DR InterPro; IPR008278; 4-PPantetheinyl_Trfase_dom.
DR InterPro; IPR037143; 4-PPantetheinyl_Trfase_dom_sf.
DR InterPro; IPR002582; ACPS.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR040899; Fas_alpha_ACP.
DR InterPro; IPR026025; FAS_alpha_yeast.
DR InterPro; IPR041550; FASI_helical.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR004568; Ppantetheine-prot_Trfase_dom.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF01648; ACPS; 1.
DR Pfam; PF18325; Fas_alpha_ACP; 1.
DR Pfam; PF18314; FAS_I_H; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR PIRSF; PIRSF000454; FAS_yeast_alpha; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
DR SUPFAM; SSF56214; SSF56214; 1.
DR TIGRFAMs; TIGR00556; pantethn_trn; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 3: Inferred from homology;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; Magnesium; Metal-binding; Multifunctional enzyme; NAD;
KW NADP; Oxidoreductase; Phosphopantetheine; Phosphoprotein; Transferase.
FT CHAIN 1..1888
FT /note="Fatty acid synthase subunit alpha"
FT /id="PRO_0000419252"
FT DOMAIN 146..221
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 98..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 675..874
FT /note="Beta-ketoacyl reductase"
FT /evidence="ECO:0000250"
FT REGION 1149..1363
FT /note="Beta-ketoacyl synthase"
FT /evidence="ECO:0000250"
FT ACT_SITE 1305
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000250"
FT BINDING 1774..1776
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250"
FT BINDING 1774
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1775
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1776
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1800
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250"
FT BINDING 1810
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250"
FT BINDING 1819..1829
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250"
FT BINDING 1843..1846
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250"
FT BINDING 1873..1875
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250"
FT BINDING 1874
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1875
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 181
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 1888 AA; 206206 MW; 6301BD0A025B7919 CRC64;
MAMKPEVEQE LAHVLLTELL AYQFASPVRW IETQDVFLKD FNTERVVEIG PSPTLAGMAQ
RTIKNKYESY DAALSLQRQV LCYSKDAKEI YYTPDPADLA PVEEPNAEEQ TGAAATPAAA
AAPAAAAAAP AAPAARPVAE LPDEAVKASL LLHVLVAQKL KKSLEQVPMS KTIKDLVGGK
STVQNEILGD LGKEFGSTPE KPEETPLEEL AETFQDTFAG SLGKQSSSLI SRLMSSKMPG
GFTITVARKY LQTRWGLGSG RQDSVLLIAL TNEPASRLGG EADAKSFLDS MAQKYASISG
VDLSSASAGA SAGAGAGGAG GATIDAAAFE ELTKDQKVMA RQQLEVLARY LKMDLNGGEK
KFLQEKNTVA ELQSQLDYLN NELGEYFIQG ISTSFSRKKA RVFDSSWNWA KQALLTLYFQ
IIHGVLKNVD REVVTEAINI MNRSNETLIK FMEYHISHCD ENNGENYKLA KTLGHQLIEN
CKQVLDMDPV YKDISKPTGP KTNIDKNGNI KYSEEPRAAV RKLSQYVQEM ALGGPLTKES
QPTIQEDLTR VYKAINAQAA EHNISDSTKL EFEKLYGELL KFLETSNEID ASATTRLAGV
VDDDLDKDST KEVASLPNKS EISKNVSSII PRETVPFLHL KKKLPSCEWA YDRQLSTLFL
DGLEKAAING VTFKDKYVLI TGAGAGSIGA EVLQGLVQGG AKVIVTTSRF SKKVTDYYQS
IYAQYGAKGS TLVVVPFNQG SKQDVEALID FIYDDEKNGG LGWDLDAVIP FAAIPENGIE
LDKIDSKSEF AHRIMLTNIL RMLGSVKKQK SARGIETRPA QVILPLSPNH GTFGGDGMYS
ESKLSLETLF NRWHSESWSN QLTICGAIIG WTRGTGLMNA NNIIAEGIEK MGVRTFSQKE
MAFNLLGLLI PEVVNLCQRS PVMADLNGGL QFLTDLKEFT GKLRGELTET SEIRKAVSIE
TALEHKTVAG ANADAAFAQV EVQPRANIQL EFPTLKPYET VKKIGSPDLE GLLDLEKVIV
VTGFSEVGPW GSSRTRGEME AFGEFSLEGC VEMSWIMGLI KYHNGNLKGR PYTGWVDSKT
NEPVDDKDIK AKDESHVLEH SGIRLIEPEL FNSYNPEKKQ MIQEVVIEED LEPFEASKET
AEQFKHEHGD KVDIFEIPET GEFSVRLLKG ATLYIPKALR FDRLVAGQIP TGWNAKTYGI
SDDTISQVDP ITLFVLVSVI EAFIASGITD PYEMYKYVHV SEVGNCSGSG MGGVSALRGM
FKDRYKDQPV QNDILQESFI NTMSAWVNML LISSSGPIKT PVGACATAVE SLDIGVETIL
SGKAKICIVG GYDDFQEEGS YEFGNMNATS NSLDEFDHGR TPAEMSRPAT TTRNGFMEAQ
GAGIQVIMNA DLALKMGVPI YGILALTATA TDKIGRSVPA PGKGILTTAR EHHGNLKFPT
PLLDIKYRKR QLKNREAQIK QWVETELEML KYEAEGIPAE DQETFYAERT EEIKREATRQ
LKSAQAQWGS EFYKNDPRIA PLRGALATYG LTIDDLGVAS FHGTSTKAND KNESATINEM
MKHLGRSEGN PVLGVFQKYL TGHPKGAAGA WMMNGALQIL NSGIVPGNRN ADNVDKLLQQ
FEYILYPSRS LKTDGIKAVS VTSFGFGQKG AQAVAVHPDF LYAAVDEATY NAYVAKVTAR
EKAAYKYFHN GMIHNTLFVS KEHAPYSDEL EQPVYLDPLA RVSSDKKTGA LVFNGKGIQS
SSQFVSEENR KTATIVSELA KKTAGTDASG VGVDVELIKS INVENDTFIE RNFTEAEIAY
CKKQPSVQSS FAGTWSAKEA VFKSLGVKSQ GGGASLKDIE ITREAGKGPE VVLHGAAKEA
ATKANVKNVK VSISHDDFQS VAVAVSEK
