FAS2_SCHPO
ID FAS2_SCHPO Reviewed; 1842 AA.
AC Q10289; O14163; P78866; P78973; Q96WT6; Q96WT7; Q96WT8; Q9URI5;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 178.
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=lsd1; ORFNames=SPAC4A8.11c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8769419; DOI=10.1083/jcb.134.4.949;
RA Saitoh S., Takahashi K., Nabeshima K., Yamashita Y., Nakaseko Y.,
RA Hirata A., Yanagida M.;
RT "Aberrant mitosis in fission yeast mutants defective in fatty acid
RT synthetase and acetyl CoA carboxylase.";
RL J. Cell Biol. 134:949-961(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=972 / ATCC 24843, H201, H265, and H518;
RX PubMed=11470243; DOI=10.1016/s1388-1981(01)00134-2;
RA Yokoyama K., Saitoh S., Ishida M., Yamakawa Y., Nakamura K., Inoue K.,
RA Taguchi R., Tokumura A., Nishijima M., Yanagida M., Setaka M.;
RT "Very long-chain fatty-acid-containing phospholipids accumulate in fatty
RT acid synthase temperature-sensitive mutant strains of the fission yeast
RT Schizosaccharomyces pombe fas2/lsd1.";
RL Biochim. Biophys. Acta 1532:223-233(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-215.
RA Koken M.H.M., de Rooij J.;
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PROTEIN SEQUENCE OF 1-20.
RX PubMed=8188691; DOI=10.1016/s0021-9258(17)36760-1;
RA Kaeslin E., Heyer W.-D.;
RT "Schizosaccharomyces pombe fatty acid synthase mediates DNA strand exchange
RT in vitro.";
RL J. Biol. Chem. 269:14103-14110(1994).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1466-1842.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1505-1564.
RC STRAIN=972 / ATCC 24843;
RA Jang Y.-J., Yoo H.-S.;
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-604 AND SER-1412, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
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. This
CC subunit coordinates the binding of the six beta subunits to the enzyme
CC complex.
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: [Alpha(6)beta(6)] hexamers of two multifunctional subunits
CC (alpha and beta).
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Fungal fatty acid
CC synthetase subunit alpha family. {ECO:0000305}.
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DR EMBL; D83412; BAA11913.1; -; Genomic_DNA.
DR EMBL; AB013747; BAB62029.1; -; Genomic_DNA.
DR EMBL; AB013748; BAB62030.1; -; Genomic_DNA.
DR EMBL; AB013749; BAB62031.1; -; Genomic_DNA.
DR EMBL; AB013750; BAB62032.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB11481.1; -; Genomic_DNA.
DR EMBL; U82216; AAB39943.1; -; Genomic_DNA.
DR EMBL; D89216; BAA13877.1; -; mRNA.
DR EMBL; U97396; AAB63888.1; -; mRNA.
DR PIR; A54083; A54083.
DR PIR; T38781; T38781.
DR PIR; T43037; T43037.
DR PIR; T43409; T43409.
DR RefSeq; NP_593823.1; NM_001019252.2.
DR AlphaFoldDB; Q10289; -.
DR SMR; Q10289; -.
DR BioGRID; 280032; 7.
DR IntAct; Q10289; 1.
DR STRING; 4896.SPAC4A8.11c.1; -.
DR iPTMnet; Q10289; -.
DR MaxQB; Q10289; -.
DR PaxDb; Q10289; -.
DR PRIDE; Q10289; -.
DR EnsemblFungi; SPAC4A8.11c.1; SPAC4A8.11c.1:pep; SPAC4A8.11c.
DR GeneID; 2543618; -.
DR KEGG; spo:SPAC4A8.11c; -.
DR PomBase; SPAC4A8.11c; fas2.
DR VEuPathDB; FungiDB:SPAC4A8.11c; -.
DR eggNOG; ENOG502QQJX; Eukaryota.
DR HOGENOM; CLU_000114_0_0_1; -.
DR InParanoid; Q10289; -.
DR OMA; QYHIDHC; -.
DR PhylomeDB; Q10289; -.
DR PRO; PR:Q10289; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005835; C:fatty acid synthase complex; IDA:PomBase.
DR GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; ISO:PomBase.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; ISO:PomBase.
DR GO; GO:0004312; F:fatty acid synthase activity; IDA:PomBase.
DR GO; GO:0004321; F:fatty-acyl-CoA synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; ISO:PomBase.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IDA:PomBase.
DR GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IMP:PomBase.
DR GO; GO:0101026; P:mitotic nuclear membrane biogenesis; IMP:PomBase.
DR GO; GO:1900535; P:palmitic acid biosynthetic process; IMP:PomBase.
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; IPR002347; SDR_fam.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF01648; ACPS; 1.
DR Pfam; PF00106; adh_short; 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 1: Evidence at protein level;
KW Direct protein sequencing; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Magnesium; Metal-binding;
KW Multifunctional enzyme; NAD; NADP; Oxidoreductase; Phosphopantetheine;
KW Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..1842
FT /note="Fatty acid synthase subunit alpha"
FT /id="PRO_0000180286"
FT DOMAIN 145..220
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 101..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1304..1332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION ?..1842
FT /note="Beta-ketoacyl synthase"
FT ACT_SITE 1262
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000250"
FT BINDING 1728..1730
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250"
FT BINDING 1728
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1729
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1730
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1754
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250"
FT BINDING 1764
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250"
FT BINDING 1773..1783
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250"
FT BINDING 1797..1800
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250"
FT BINDING 1827..1829
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250"
FT BINDING 1828
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1829
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 180
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 604
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 1412
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT VARIANT 4
FT /note="E -> V (in strain: H265)"
FT VARIANT 600
FT /note="I -> N (in strain: H518)"
FT VARIANT 1276
FT /note="I -> T (in strain: H201)"
FT CONFLICT 107
FT /note="S -> A (in Ref. 4; AAB39943)"
FT /evidence="ECO:0000305"
FT CONFLICT 422
FT /note="K -> R (in Ref. 1; BAA11913)"
FT /evidence="ECO:0000305"
FT CONFLICT 1586
FT /note="P -> S (in Ref. 6; BAA13877)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1842 AA; 202169 MW; E4019F2D133EE571 CRC64;
MRPEVEQELA HTLLLELLAY QFASPVRWIE TQDVILSPPV SAERIVEIGP SPTLAGMAKR
TLKLKYENMD AALSINREVL CYSKDAREIY YNFEDEVADE PAEAPASTSS TPKVETAAAA
APAATPAPAP AQTSAPAAAL PDEPPKALEV LHTLVAQKLK KSIEEVSPQK SIKDLVGGKS
TLQNEILGDL QKEFGATPEK PEEVPLDELG AIMQSSFNGS LGKQSSSLIS RMISSKMPGG
FNNSAVRGYL GNRYGLGPGR LESVLLLALT MEPASRLGSE ADAKAWLDSV AQKYAARNGV
TLSSPTAEGG SSSGSAAVID EETFKKLTKN NTMLVTQQLE LFARYLNKDL RAGQKAQVAE
KVISDTLRAQ LDLWNEEHGE FYASGIAPIF SPLKARVYDS DWNWARQDAL KMFFDIIFGR
LKHVDTEIVA RCISVMNRSN PTLLEFMQYH IDHCPAEKGE TYQLAKTLGQ QLIDNCKSVI
DAPPVFKNVN HPTAPSTTID ERGNLNYEEI PRPGVRKLTH YVTEMAKGGK LPTESKNKAK
VQNDLARIYR IIKSQNKMSR SSKLQIKQLY GQVLHALSLP LPSSNDEQTP VKETIPFLHI
RKKSVDGNWE FNKSLTGTYL DVLESGAKNG ITYQDKYALV TGAGAGSIGA QIVEGLLAGG
AKVVVTTSRF SRKVTEFYQS LYTRHGSRGS CLIVVPFNQG SKTDVEALID YIYDEKKGLG
WNLDYIVPFA AIPENGREID GIDSRSEFAH RIMLTNILRL LGAVKSQKAS RGMDTRPAQV
ILPLSPNHGT FGNDGLYSES KLGLETLFNR WYSESWANYL TICGAVIGWT RGTGLMAPNN
IVSQGIEKYG VRTFSQSEMA FNILGLMSQK VVDLCQSEPI YANLNGGLEL LPDLKDLSTR
LRTELLETAE IRRAVAAETA FDHSITNGPD SEAVFQKTAI QPRANLKFNF PKLKPYEALS
HLSDLRGMVD LEKVPVVTGF SEVGPWGNSR TRWDMECYGE FSLEGCVEIA WIMGLIKNFN
GKGKDGKPYS GWVDTKTGEP VDDKDVKAKY EKYILEHCGI RIIEAELFHG YNPEKKELLQ
EVVIDHDLEP FEASKEAAHE FKLRHGDQVE IFEIPDSTEW SVRFKRGTSM LIPKALRFDR
FVAGQIPLGW DPKRYGIPDD IISQVDPTTL YVLVSTVEAL VASGITDPYE CYKYIHVSEL
GNTVGSGIGG MSALRGMYKD RWTDKPVQKD ILQESFINTA NAWINMLLLS ASGPIKTPVG
ACATAVESVD AAVDLITSGK ARICISGGYD DFSEEGSYEF ANMGATSNAA KETERGRTPQ
EMSRPATSTR DGFMESQGAG VQIIMQAKLA IEMGVPIHGI VGYVSTAMDK QGRSVPAPGQ
GILTGAREIA TKTPLPIVDL KFRSRQLQRR RSQIGEWAER EYLYLEEELD AMKVQNPDLD
LEAYRIERIN VIKEEVVRQE KEALNTFGNE FWKRDPTIAP IRGALAVWGL TIDDLGVASF
HGTSTKANEK NECDVIDSQL THLGRSKGNA VYGVFQKYLT GHSKGGAGAW MLNGALQILR
SGFVPGNRNA DNIDEYLARF DRVMFPSEGI QTDGIKAASV TAFGFGQVGG QVIVIHPDYI
YGVIDEATYN AYKAKTAARY KASYRYTHDA LVYNNLVRAK DSPPYTKEQE KAVYLNPLAR
ASKSKAGTWT FPATLPAESD ISKTNETTRT LQSLTTSLTN SNENVGVDVE LVSAISIDNE
TFIERNFTDT ERKYCFAAPN PQASFAGRWS AKEAVFKSLG ISGKGAAAPL KDIEIISSES
GAPEVVLHGE AAKAATTAGV KSVSVSISHD DNQSVSVALA HK
