FAS1_SCHPO
ID FAS1_SCHPO Reviewed; 2073 AA.
AC Q9UUG0; P78799;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 154.
DE RecName: Full=Fatty acid synthase subunit beta;
DE EC=2.3.1.86;
DE Includes:
DE RecName: Full=3-hydroxyacyl-[acyl-carrier-protein] dehydratase;
DE EC=4.2.1.59;
DE Includes:
DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH];
DE EC=1.3.1.9;
DE Includes:
DE RecName: Full=[Acyl-carrier-protein] acetyltransferase;
DE EC=2.3.1.38;
DE Includes:
DE RecName: Full=[Acyl-carrier-protein] malonyltransferase;
DE EC=2.3.1.39;
DE Includes:
DE RecName: Full=S-acyl fatty acid synthase thioesterase;
DE EC=3.1.2.14;
GN Name=fas1; ORFNames=SPAC926.09c;
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], AND SUBUNIT.
RX PubMed=9693066; DOI=10.1006/prep.1998.0914;
RA Niwa H., Katayama E., Yanagida M., Morikawa K.;
RT "Cloning of the fatty acid synthetase beta subunit from fission yeast,
RT coexpression with the alpha subunit, and purification of the intact
RT multifunctional enzyme complex.";
RL Protein Expr. Purif. 13:403-413(1998).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1725-2073.
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1122 AND SER-2073, 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 beta subunit
CC contains domains for: [acyl-carrier-protein] acetyltransferase and
CC malonyltransferase, S-acyl fatty acid synthase thioesterase, enoyl-
CC [acyl-carrier-protein] reductase, and 3-hydroxypalmitoyl-[acyl-carrier-
CC protein] dehydratase.
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=acetyl-CoA + holo-[ACP] = acetyl-[ACP] + CoA;
CC Xref=Rhea:RHEA:41788, Rhea:RHEA-COMP:9621, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78446; EC=2.3.1.38;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=holo-[ACP] + malonyl-CoA = CoA + malonyl-[ACP];
CC Xref=Rhea:RHEA:41792, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449; EC=2.3.1.39;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O;
CC Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] +
CC H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-
CC COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-[ACP] + H2O = (9Z)-octadecenoate + H(+) +
CC holo-[ACP]; Xref=Rhea:RHEA:15057, Rhea:RHEA-COMP:9685, Rhea:RHEA-
CC COMP:9924, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:78783; EC=3.1.2.14;
CC -!- SUBUNIT: [Alpha(6)beta(6)] hexamers of two multifunctional subunits
CC (alpha and beta). {ECO:0000269|PubMed:9693066}.
CC -!- SIMILARITY: Belongs to the fungal fatty acid synthetase subunit beta
CC family. {ECO:0000305}.
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DR EMBL; AB010274; BAA36384.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB54157.1; -; Genomic_DNA.
DR EMBL; D89148; BAA13810.1; -; mRNA.
DR PIR; T39207; T39207.
DR PIR; T42424; T42424.
DR PIR; T43311; T43311.
DR RefSeq; NP_594370.1; NM_001019791.2.
DR AlphaFoldDB; Q9UUG0; -.
DR SMR; Q9UUG0; -.
DR BioGRID; 279916; 16.
DR STRING; 4896.SPAC926.09c.1; -.
DR iPTMnet; Q9UUG0; -.
DR MaxQB; Q9UUG0; -.
DR PaxDb; Q9UUG0; -.
DR PRIDE; Q9UUG0; -.
DR EnsemblFungi; SPAC926.09c.1; SPAC926.09c.1:pep; SPAC926.09c.
DR GeneID; 2543497; -.
DR KEGG; spo:SPAC926.09c; -.
DR PomBase; SPAC926.09c; fas1.
DR VEuPathDB; FungiDB:SPAC926.09c; -.
DR eggNOG; ENOG502QQJX; Eukaryota.
DR HOGENOM; CLU_000114_5_0_1; -.
DR InParanoid; Q9UUG0; -.
DR OMA; LTHRNKD; -.
DR PhylomeDB; Q9UUG0; -.
DR PRO; PR:Q9UUG0; -.
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:0008659; F:(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0008693; F:3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0047451; F:3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0004317; F:3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity; ISO:PomBase.
DR GO; GO:0004313; F:[acyl-carrier-protein] S-acetyltransferase activity; ISO:PomBase.
DR GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; ISO:PomBase.
DR GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; ISO:PomBase.
DR GO; GO:0016631; F:enoyl-[acyl-carrier-protein] reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0004312; F:fatty acid synthase activity; IDA:PomBase.
DR GO; GO:0004321; F:fatty-acyl-CoA synthase activity; NAS:PomBase.
DR GO; GO:0016295; F:myristoyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0004320; F:oleoyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016296; F:palmitoyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IDA:PomBase.
DR GO; GO:0042759; P:long-chain fatty acid biosynthetic process; ISO:PomBase.
DR GO; GO:0046467; P:membrane lipid biosynthetic process; IC:PomBase.
DR Gene3D; 3.20.20.70; -; 2.
DR Gene3D; 3.40.366.10; -; 3.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR016452; Fas1/AflB-like.
DR InterPro; IPR013565; Fas1/AflB-like_central.
DR InterPro; IPR041099; FAS1_N.
DR InterPro; IPR040883; FAS_meander.
DR InterPro; IPR003965; Fatty_acid_synthase.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR039569; MaoC-like_dehydrat_N.
DR InterPro; IPR002539; MaoC-like_dom.
DR InterPro; IPR032088; SAT.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08354; DUF1729; 1.
DR Pfam; PF17951; FAS_meander; 1.
DR Pfam; PF17828; FAS_N; 1.
DR Pfam; PF13452; MaoC_dehydrat_N; 1.
DR Pfam; PF01575; MaoC_dehydratas; 1.
DR Pfam; PF16073; SAT; 1.
DR PIRSF; PIRSF005562; FAS_yeast_beta; 1.
DR PRINTS; PR01483; FASYNTHASE.
DR SMART; SM00827; PKS_AT; 1.
DR SUPFAM; SSF52151; SSF52151; 2.
DR SUPFAM; SSF54637; SSF54637; 2.
PE 1: Evidence at protein level;
KW Fatty acid biosynthesis; Fatty acid metabolism; Hydrolase;
KW Lipid biosynthesis; Lipid metabolism; Lyase; Multifunctional enzyme; NAD;
KW NADP; Oxidoreductase; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..2073
FT /note="Fatty acid synthase subunit beta"
FT /id="PRO_0000180281"
FT DOMAIN 1558..1667
FT /note="MaoC-like"
FT REGION 1..459
FT /note="Acetyltransferase"
FT REGION 470..858
FT /note="Enoyl reductase"
FT REGION 1155..1644
FT /note="Dehydratase"
FT REGION 1645..2073
FT /note="Malonyl/palmitoyl transferase"
FT ACT_SITE 270
FT /note="For acetyltransferase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 1361
FT /note="For dehydratase activity"
FT /evidence="ECO:0000255"
FT ACT_SITE 1828
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000250"
FT MOD_RES 1122
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 2073
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 222
FT /note="P -> R (in Ref. 1; BAA36384)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2073 AA; 230561 MW; D928270838E7C7C4 CRC64;
MVEAEQVHQS LRSLVLSYAH FSPSILIPAS QYLLAAQLRD EFLSLHPAPS AESVEKEGAE
LEFEHELHLL AGFLGLIAAK EEETPGQYTQ LLRIITLEFE RTFLAGNEVH AVVHSLGLNI
PAQKDVVRFY YHSCALIGQT TKFHGSALLD ESSVKLAAIF GGQGYEDYFD ELIELYEVYA
PFAAELIQVL SKHLFTLSQN EQASKVYSKG LNVLDWLAGE RPERDYLVSA PVSLPLVGLT
QLVHFSVTAQ ILGLNPGELA SRFSAASGHS QGIVVAAAVS ASTDSASFME NAKVALTTLF
WIGVRSQQTF PTTTLPPSVV ADSLASSEGN PTPMLAVRDL PIETLNKHIE TTNTHLPEDR
KVSLSLVNGP RSFVVSGPAR SLYGLNLSLR KEKADGQNQS RIPHSKRKLR FINRFLSISV
PFHSPYLAPV RSLLEKDLQG LQFSALKVPV YSTDDAGDLR FEQPSKLLLA LAVMITEKVV
HWEEACGFPD VTHIIDFGPG GISGVGSLTR ANKDGQGVRV IVADSFESLD MGAKFEIFDR
DAKSIEFAPN WVKLYSPKLV KNKLGRVYVD TRLSRMLGLP PLWVAGMTPT SVPWQFCSAI
AKAGFTYELA GGGYFDPKMM REAIHKLSLN IPPGAGICVN VIYINPRTYA WQIPLIRDMV
AEGYPIRGVT IAAGIPSLEV ANELISTLGV QYLCLKPGSV EAVNAVISIA KANPTFPIVL
QWTGGRAGGH HSFEDFHSPI LLTYSAIRRC DNIVLIAGSG FGGADDTEPY LTGEWSAAFK
LPPMPFDGIL FGSRLMVAKE AHTSLAAKEA IVAAKGVDDS EWEKTYDGPT GGIVTVLSEL
GEPIHKLATR GIMFWKELDD TIFSLPRPKR LPALLAKKQY IIKRLNDDFQ KVYFPAHIVE
QVSPEKFKFE AVDSVEDMTY AELLYRAIDL MYVTKEKRWI DVTLRTFTGK LMRRIEERFT
QDVGKTTLIE NFEDLNDPYP VAARFLDAYP EASTQDLNTQ DAQFFYSLCS NPFQKPVPFI
PAIDDTFEFY FKKDSLWQSE DLAAVVGEDV GRVAILQGPM AAKHSTKVNE PAKELLDGIN
ETHIQHFIKK FYAGDEKKIP IVEYFGGVPP VNVSHKSLES VSVTEEAGSK VYKLPEIGSN
SALPSKKLWF ELLAGPEYTW FRAIFTTQRV AKGWKLEHNP VRRIFAPRYG QRAVVKGKDN
DTVVELYETQ SGNYVLAARL SYDGETIVVS MFENRNALKK EVHLDFLFKY EPSAGYSPVS
EILDGRNDRI KHFYWALWFG EEPYPENASI TDTFTGPEVT VTGNMIEDFC RTVGNHNEAY
TKRAIRKRMA PMDFAIVVGW QAITKAIFPK AIDGDLLRLV HLSNSFRMVG SHSLMEGDKV
TTSASIIAIL NNDSGKTVTV KGTVYRDGKE VIEVISRFLY RGTFTDFENT FEHTQETPMQ
LTLATPKDVA VLQSKSWFQL LDPSQDLSGS ILTFRLNSYV RFKDQKVKSS VETKGIVLSE
LPSKAIIQVA SVDFQSVDCH GNPVIEFLKR NGKPIEQPVE FENGGYSVIQ VMDEGYSPVF
VTPPTNSPYA EVSGDYNPIH VSPTFAAFVE LPGTHGITHG MYTSAAARRF VETYAAQNVP
ERVKHYEVTF VNMVLPNTEL ITKLSHTGMI NGRKIIKVEV LNQETSEPVL VGTAEVEQPV
SAYVFTGQGS QEQGMGMDLY ASSPVARKIW DSADKHFLTN YGFSIIDIVK HNPHSITIHF
GGSKGKKIRD NYMAMAYEKL MEDGTSKVVP VFETITKDST SFSFTHPSGL LSATQFTQPA
LTLMEKSAFE DMRSKGLVQN DCAFAGHSLG EYSALSAMGD VLSIEALVDL VFLRGLTMQN
AVHRDELGRS DYGMVAANPS RVSASFTDAA LRFIVDHIGQ QTNLLLEIVN YNVENQQYVV
SGNLLSLSTL GHVLNFLKVQ KIDFEKLKET LTIEQLKEQL TDIVEACHAK TLEQQKKTGR
IELERGYATI PLKIDVPFHS SFLRGGVRMF REYLVKKIFP HQINVAKLRG KYIPNLTAKP
FEISKEYFQN VYDLTGSQRI KKILQNWDEY ESS
