ID A0A1F7ZPB5_9EURO Unreviewed; 2092 AA.
AC A0A1F7ZPB5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 28-JAN-2026, entry version 38.
DE RecName: Full=Fatty acid synthase subunit beta {ECO:0000256|ARBA:ARBA00068309};
DE EC=1.3.1.9 {ECO:0000256|ARBA:ARBA00012996};
DE EC=2.3.1.38 {ECO:0000256|ARBA:ARBA00013256};
DE EC=2.3.1.39 {ECO:0000256|ARBA:ARBA00013258};
DE EC=2.3.1.86 {ECO:0000256|ARBA:ARBA00012878};
DE EC=3.1.2.14 {ECO:0000256|ARBA:ARBA00012480};
DE EC=4.2.1.59 {ECO:0000256|ARBA:ARBA00013167};
GN ORFNames=ABOM_009779 {ECO:0000313|EMBL:OGM41294.1};
OS Aspergillus bombycis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=109264 {ECO:0000313|EMBL:OGM41294.1, ECO:0000313|Proteomes:UP000179179};
RN [1] {ECO:0000313|EMBL:OGM41294.1, ECO:0000313|Proteomes:UP000179179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 26010 {ECO:0000313|Proteomes:UP000179179};
RX PubMed=27664179;
RA Moore G.G., Mack B.M., Beltz S.B., Gilbert M.K.;
RT "Draft genome sequence of an aflatoxigenic Aspergillus species, A.
RT bombycis.";
RL Genome Biol. Evol. 0:0-0(2016).
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. {ECO:0000256|ARBA:ARBA00058855}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-[ACP] + H2O = (9Z)-octadecenoate + holo-
CC [ACP] + H(+); 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 Evidence={ECO:0000256|ARBA:ARBA00048536};
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 Evidence={ECO:0000256|ARBA:ARBA00001055};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] +
CC NADH + H(+); 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 Evidence={ECO:0000256|ARBA:ARBA00048572};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + n malonyl-CoA + 2n NADPH + 4n H(+) = a long-
CC chain-acyl-CoA + n CoA + n CO2 + 2n NADP(+).; EC=2.3.1.86;
CC Evidence={ECO:0000256|ARBA:ARBA00048237};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=holo-[ACP] + acetyl-CoA = 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 Evidence={ECO:0000256|ARBA:ARBA00048835};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=holo-[ACP] + malonyl-CoA = malonyl-[ACP] + CoA;
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 Evidence={ECO:0000256|ARBA:ARBA00048462};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005179}.
CC -!- SUBUNIT: [Alpha(6)beta(6)] hexamers of two multifunctional subunits
CC (alpha and beta). {ECO:0000256|ARBA:ARBA00033756}.
CC -!- SIMILARITY: Belongs to the fungal fatty acid synthetase subunit beta
CC family. {ECO:0000256|ARBA:ARBA00010009, ECO:0000256|PIRNR:PIRNR005562}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OGM41294.1}.
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DR EMBL; LYCR01000116; OGM41294.1; -; Genomic_DNA.
DR RefSeq; XP_022385011.1; XM_022536907.1.
DR STRING; 109264.A0A1F7ZPB5; -.
DR GeneID; 34453169; -.
DR OrthoDB; 5417908at2759; -.
DR Proteomes; UP000179179; Unassembled WGS sequence.
DR GO; GO:0005835; C:fatty acid synthase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0019171; F:(3R)-hydroxyacyl-[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-UniRule.
DR GO; GO:0004312; F:fatty acid synthase activity; IEA:InterPro.
DR GO; GO:0016297; F:fatty acyl-[ACP] hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0004321; F:fatty-acyl-CoA synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd03447; FAS_MaoC; 1.
DR FunFam; 1.20.1050.120:FF:000001; Fatty acid synthase beta subunit dehydratase; 1.
DR FunFam; 1.20.930.70:FF:000001; Fatty acid synthase beta subunit dehydratase; 1.
DR FunFam; 3.10.129.10:FF:000017; Fatty acid synthase beta subunit dehydratase; 1.
DR FunFam; 3.20.20.70:FF:000078; Fatty acid synthase beta subunit dehydratase; 1.
DR FunFam; 3.30.1120.100:FF:000001; Fatty acid synthase beta subunit dehydratase; 1.
DR FunFam; 3.10.129.10:FF:000015; Fatty acid synthase subunit beta; 1.
DR FunFam; 3.30.70.3330:FF:000001; Fatty acid synthase subunit beta dehydratase; 1.
DR FunFam; 3.40.366.10:FF:000003; Fatty acid synthase subunit beta dehydratase; 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_dom.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR039569; FAS1-like_DH_region.
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; IPR050830; Fungal_FAS.
DR InterPro; IPR029069; HotDog_dom_sf.
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; PF13452; FAS1_DH_region; 1.
DR Pfam; PF22235; FAS1_thioest_ins; 1.
DR Pfam; PF17951; FAS_meander; 1.
DR Pfam; PF17828; FAS_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; SSF51412; Inosine monophosphate dehydrogenase (IMPDH); 1.
DR SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 2.
PE 3: Inferred from homology;
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR005562};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRNR:PIRNR005562};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR005562};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR005562};
KW Reference proteome {ECO:0000313|Proteomes:UP000179179};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR005562}.
FT DOMAIN 1692..2013
FT /note="Malonyl-CoA:ACP transacylase (MAT)"
FT /evidence="ECO:0000259|SMART:SM00827"
FT ACT_SITE 286
FT /note="For acetyltransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR005562-1"
FT ACT_SITE 1836
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR005562-1"
SQ SEQUENCE 2092 AA; 232118 MW; 5BBB99F12AFBE329 CRC64;
MYGTSTGPQT GINTPRSSQS LRPLILSHGS LEFSFLVPTS LHFQASQLKD TFTASLPEPT
DELAQDDEPS SVAELVARYI GHIATEVEEG EDDAHGTNLE VLKLALNEFE RAFMRGNDVH
AVASALPGIT AKKASVVKAY YAGRAAAGRP TKPYDSALFR AASDEKANIY TVFGGQGNIE
EYFDELREIY TTYPSFVDEL ISSSAQLLLS LSREPEASKL YPKGMDIIQW LQDPDSQPDT
DYLVSAPVSL PLIGLVQLAH FVVTCKALGR EPSEVLERFS GTTGHSQGVV TAAAIASATT
WEGFEKVAKD ALTMLFWIGL RSQQAYPRTS IAPSVLQDSI ENGEGTPTPM LSIRDLPRSA
VQEHIDMTNQ HLPEDRHISI SLVNSARNFV VTGPPLSLYG LNLRLRKVKA PTGLDQNRVP
FTQRKVRFVN RFLPITAPFH SQYLYSAYDR ILEDLEDLEI PAKSLAIPVY GTKTGEDLRE
SGDANIVPAL VRMITHDAVN WEQATVFPGA THIVDFGPGG ISGLGVLTNR NKDGTGVRVV
LAGAMDGTNA EVGYKPELFD RDEHAVKYAI DWVKEYGPRL VKNAAGETFV DTKMSRLLGI
PPIMVAGMTP TTVPWDFVAA TMNAGYHIEL AGGGYYNAKT MTEAVSKIEK TIPPGRGITI
NLIYVNPRAM AWQIPLIGKL RADGVPVEGL TIGAGVPSIE VANEYIETLG IKHIAFKPGS
VDAIQQVINI AKANPKFPVI LQWTGGRGGG HHSFEDFHQP VLQMYSRIRR CENIVLVAGS
GFGGSEDTYP YLSGTWSSRF GYPPMPFDGC LFGSRIMIAK EAHTSKNAKK AIADAPGLDD
QDWEKTYKGS AGGVVTVLSE MGEPIHKLAT RGVLFWHEMD QKIFKLDKAK RVPELKKQRN
YIIKKLNDDF QKVWFGRKAS GETADLEDMT YAEVVHRMVD LMYVKHESRW IDESLKKLTG
DFIHRVEERF TTLEGQPSLL QNYSELNTPY PAVDNILVAY PEAATQLINA QDVQHFLLLC
QRRGQKPVPF VPALDENFEY WFKKDSLWQS EDLEAVVDQD VGRTCILQGP MAAKFSTITD
EPVQDILNGI HQGHIKSLLE DVYSGDETKV PVIEYLGGRL DDSVDEPEID GLTISEDANK
ISYRLSSSPS SDLPELDRWL RLLAGTSYSW RHAIFLADIF VQGHRFQTNP LKRVVAPTSG
MYVEMAYPND PSKTAISVRE PYQSGKLVKT VEVKMNEKNQ ISLTLFEGRT AEGGVVPLTF
LFTYHPESGY APIREVMEGR NDRIKEFYYR VWFGNSDVPF DTPTTATFSG GRETISSQAV
ADFVHAVGNT GEAFVDRPGK EVFAPMDFAI VAGWKAITKP IFPRTIDGDL LKLVHLSNGF
KMVPGAQPLK VGDVLDTTAQ INAVINQESG KMVEVCGTIK RDGKPIMHVT SQFLYRGAYL
DFENTFQRKD EVPMQVHLAS SRDVAILRSK EWFRIDEPDV ELLGQTLTFR LQSLIQFKNK
SVFSHVQTVG QVLLELPTKE IIQVASVDYE AGDSHGNPVV DYLQRNGTSI EQPVYFENPI
PLSGKTPLEL RAPTSNETYA RVSGDYNPIH VSRVFSSYAN LPGTITHGMY TSAAVRSYVE
TWAAENNIGR VRGFHVSLVG MVLPNDMITV KLQHVGMIAG RKIIKVEASN KETEDKVLLG
EAEVEQPVTS YVFTGQGSQE QGMGMELYSS SPVAREVWDR ADRHFMENYG LSIIDIVKNN
PKELTVYFGG PRGKAIRQNY MSMTFESVNA DGSIKSEKIF KEIDENTTSY TYRSPSGLLS
ATQFTQPALT LMEKASFEDM RSKGLVQRDS SFAGHSLGEY SALAALADVM PIESLVSVVF
YRGLTMQVAV ERDEQGRSNY SMCAVNPSRI SKTFNEQALQ YVVENISEQT GWLLEIVNYN
VANMQYVAAG DLRALDCLTN LLNYLKAQNI DIPALMQSMS LEDVKAHLVK IIHECVKQTE
SKPKPITLER GFATIPLRGI DVPFHSTFLR SGVKPFRSFL LKKINKNTID PSKLVGKYIP
NVTARPFELT KEYFEDVYRL TNSPRIANIL ANWEKYEEES ENVSRGGGTT SA
//
