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 24-JAN-2024, entry version 146. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 284591.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; HFMDNYG; -. DR OrthoDB; 5488314at2759; -. 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:0004317; F:(3R)-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity; IEA:InterPro. 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:0004312; F:fatty acid synthase activity; IEA:InterPro. DR GO; GO:0004321; F:fatty-acyl-CoA synthase activity; IEA:UniProtKB-EC. DR GO; GO:0004320; F:oleoyl-[acyl-carrier-protein] hydrolase activity; IEA:RHEA. DR GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IBA:GO_Central. DR CDD; cd03447; FAS_MaoC; 1. DR Gene3D; 1.20.1050.120; -; 1. DR Gene3D; 1.20.930.70; -; 1. DR Gene3D; 3.30.1120.100; -; 1. DR Gene3D; 3.30.70.3330; -; 1. DR Gene3D; 6.10.140.1400; -; 1. DR Gene3D; 6.10.60.10; -; 1. DR Gene3D; 6.20.240.10; -; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 2. DR Gene3D; 3.10.129.10; Hotdog Thioesterase; 2. DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 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 PANTHER; PTHR10982:SF21; FATTY ACID SYNTHASE SUBUNIT BETA; 1. DR PANTHER; PTHR10982; MALONYL COA-ACYL CARRIER PROTEIN TRANSACYLASE; 1. DR Pfam; PF00698; Acyl_transf_1; 1. DR Pfam; PF08354; Fas1-AflB-like_hel; 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; FabD/lysophospholipase-like; 2. DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1. DR SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 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 //