FAS1_YARLI
ID FAS1_YARLI Reviewed; 2086 AA.
AC P34229; Q6CEK0;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 2.
DT 03-AUG-2022, entry version 141.
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; OrderedLocusNames=YALI0B15059g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 32338 / CX-161-1B;
RX PubMed=2034224; DOI=10.1007/bf00273618;
RA Koettig H., Rottner G., Beck K.-F., Schweizer M., Schweizer E.;
RT "The pentafunctional FAS1 genes of Saccharomyces cerevisiae and Yarrowia
RT lipolytica are co-linear and considerably longer than previously
RT estimated.";
RL Mol. Gen. Genet. 226:310-314(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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).
CC -!- SIMILARITY: Belongs to the fungal fatty acid synthetase subunit beta
CC family. {ECO:0000305}.
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DR EMBL; X59690; CAA42211.1; -; Genomic_DNA.
DR EMBL; CR382128; CAG83163.1; -; Genomic_DNA.
DR PIR; S15999; S15999.
DR RefSeq; XP_500912.1; XM_500912.1.
DR AlphaFoldDB; P34229; -.
DR SMR; P34229; -.
DR STRING; 4952.CAG83163; -.
DR PRIDE; P34229; -.
DR EnsemblFungi; CAG83163; CAG83163; YALI0_B15059g.
DR GeneID; 2907339; -.
DR KEGG; yli:YALI0B15059g; -.
DR VEuPathDB; FungiDB:YALI0_B15059g; -.
DR HOGENOM; CLU_000114_5_0_1; -.
DR InParanoid; P34229; -.
DR OMA; LTHRNKD; -.
DR Proteomes; UP000001300; Chromosome B.
DR GO; GO:0005835; C:fatty acid synthase complex; IBA:GO_Central.
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; IEA:UniProtKB-EC.
DR GO; GO:0004313; F:[acyl-carrier-protein] S-acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IEA:UniProtKB-EC.
DR GO; GO:0016631; F:enoyl-[acyl-carrier-protein] reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0004321; F:fatty-acyl-CoA synthase activity; IEA:UniProtKB-EC.
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:0042759; P:long-chain fatty acid biosynthetic process; IBA:GO_Central.
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 3: Inferred from homology;
KW Fatty acid biosynthesis; Fatty acid metabolism; Hydrolase;
KW Lipid biosynthesis; Lipid metabolism; Lyase; Multifunctional enzyme; NAD;
KW NADP; Oxidoreductase; Reference proteome; Transferase.
FT CHAIN 1..2086
FT /note="Fatty acid synthase subunit beta"
FT /id="PRO_0000180283"
FT DOMAIN 1550..1680
FT /note="MaoC-like"
FT REGION 1..480
FT /note="Acetyltransferase"
FT REGION 492..879
FT /note="Enoyl reductase"
FT REGION 1166..1657
FT /note="Dehydratase"
FT REGION 1658..1879
FT /note="Malonyl/palmitoyl transferase"
FT ACT_SITE 286
FT /note="For acetyltransferase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 1842
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000250"
FT CONFLICT 1..11
FT /note="MYPTTGVNTPQ -> M (in Ref. 1; CAA42211)"
FT /evidence="ECO:0000305"
FT CONFLICT 529..530
FT /note="HK -> TR (in Ref. 1; CAA42211)"
FT /evidence="ECO:0000305"
FT CONFLICT 1240
FT /note="V -> G (in Ref. 1; CAA42211)"
FT /evidence="ECO:0000305"
FT CONFLICT 1612
FT /note="H -> Q (in Ref. 1; CAA42211)"
FT /evidence="ECO:0000305"
FT CONFLICT 2077
FT /note="N -> D (in Ref. 1; CAA42211)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2086 AA; 231342 MW; 060F6CEA44F235B2 CRC64;
MYPTTGVNTP QSAASLRPLV LSHGQTEHSL LVPTSLYINC TTLRDQFYAS LPPATEDKAD
DDEPSSSTEL LAAFLGFTAK TVEEEPGPYD DVLSLVLNEF ETRYLRGNDI HAVASSLLQD
EDVPTTVGKI KRVIRAYYAA RIACNRPIKA HSSALFRAAS EDSDNVSLYA IFGGQGNTED
YFEELREIYD IYQGLVGDFI RECGAQLLAL SRDHIAAEKI YTKGFDIVKW LEHPETIPDF
EYLISAPISV PIIGVIQLAH YAVTCRVLGL NPGQVRDNLK GATGHSQGLI TAIAISASDS
WDEFYNSASR ILKIFFFIGV RVQQAYPSTF LPPSTLEDSV KQGEGKPTPM LSIRDLSLNQ
VQEFVDATNL HLPEDKQIVV SLINGPRNVV VTGPPQSLYG LCLVLRKQKA ETGLDQSRVP
HSQRKLKFTH RFLPITSPFH SYLLEKSTDL IINDLESSGV EFVSSELKVP VYDTFDGSVL
SQLPKGIVSR LVNLITHLPV KWEKATQFQA SHIVDFGPGG ASGLGLLTHK NKDGTGVRTI
LAGVIDQPLE FGFKQELFDR QESSIVFAQN WAKEFSPKLV KISSTNEVYV DTKFSRLTGR
APIMVAGMTP TTVNPKFVAA TMNSGYHIEL GGGGYFAPGM MTKALEHIEK NTPPGSGITI
NLIYVNPRLI QWGIPLIQEL RQKGFPIEGL TIGAGVPSLE VANEWIQDLG VKHIAFKPGS
IEAISSVIRI AKANPDFPII LQWTGGRGGG HHSFEDFHAP ILQMYSKIRR CSNIVLIAGS
GFGASTDSYP YLTGSWSRDF DYPPMPFDGI LVGSRVMVAK EAFTSLGAKQ LIVDSPGVED
SEWEKTYDKP TGGVITVLSE MGEPIHKLAT RGVLFWHEMD KTVFSLPKKK RLEVLKSKRA
YIIKRLNDDF QKTWFAKNAQ GQVCDLEDLT YAEVIQRLVD LMYVKKESRW IDVTLRNLAG
TFIRRVEERF STETGASSVL QSFSELDSEP EKVVERVFEL FPASTTQIIN AQDKDHFLML
CLNPMQKPVP FIPVLDDNFE FFFKKDSLWQ CEDLAAVVDE DVGRICILQG PVAVKHSKIV
NEPVKEILDS MHEGHIKQLL EDGEYAGNMA NIPQVECFGG KPAQNFGDVA LDSVMVLDDL
NKTVFKIETG TSALPSAADW FSLLAGDKNS WRQVFLSTDT IVQTTKMISN PLHRLLEPIA
GLQVEIEHPD EPENTVISAF EPINGKVTKV LELRKGAGDV ISLQLIEARG VDRVPVALPL
EFKYQPQIGY APIVEVMTDR NTRIKEFYWK LWFGQDSKFE IDTDITEEII GDDVTISGKA
IADFVHAVGN KGEAFVGRST SAGTVFAPMD FAIVLGWKAI IKAIFPRAID ADILRLVHLS
NGFKMMPGAD PLQMGDVVSA TAKIDTVKNS ATGKTVAVRG LLTRDGKPVM EVVSEFFYRG
EFSDFQNTFE RREEVPMQLT LKDAKAVAIL CSKEWFEYNG DDTKDLEGKT IVFRNSSFIK
YKNETVFSSV HTTGKVLMEL PSKEVIEIAT VNYQAGESHG NPVIDYLERN GTTIEQPVEF
EKPIPLSKAD DLLSFKAPSS NEPYAGVSGD YNPIHVSRAF ASYASLPGTI THGMYSSAAV
RSLIEVWAAE NNVSRVRAFS CQFQGMVLPN DEIVTRLEHV GMINGRKIIK VTSTNRETEA
VVLSGEAEVE QPISTFVFTG QGSQEQGMGM DLYASSEVAK KVWDKADEHF LQNYGFSIIK
IVVENPKELD IHFGGPKGKK IRDNYISMMF ETIDEKTGNL ISEKIFKEID ETTDSFTFKS
PTGLLSATQF TQPALTLMEK ASFEDMKAKG LVPVDATFAG HSLGEYSALA SLGDVMPIES
LVDVVFYRGM TMQVAVPRDA QGRSNYGMCA VNPSRISTTF NDAALRFVVD HISEQTKWLL
EIVNYNVENS QYVTAGDLRA LDTLTNVLNV LKLEKINIDK LLESLPLEKV KEHLSEIVTE
VAKKSVAKPQ PIELERGFAV IPLKGISVPF HSSYLRNGVK PFQNFLVKKV PKNAVKPANL
IGKYIPNLTA KPFEITKEYF EEVYKLTGSE KVKSIINNWE SYESKQ
