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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
 
 
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