ID A0A0S7DHN5_9EURO Unreviewed; 2092 AA.
AC A0A0S7DHN5;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Beta subunit of fatty acid synthetase {ECO:0000313|EMBL:GIM36486.1};
GN ORFNames=ALT_004368 {ECO:0000313|EMBL:GIM36486.1}, CNMCM8060_003244
GN {ECO:0000313|EMBL:KAF4179381.1};
OS Aspergillus lentulus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=293939 {ECO:0000313|EMBL:GIM36486.1};
RN [1] {ECO:0000313|EMBL:GIM36486.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IFM 54703 {ECO:0000313|EMBL:GIM36486.1};
RA Kusuya Y., Sakai K., Kamei K., Takahashi H., Yaguchi T.;
RT "Draft Genome sequence of the pathogenic filamentous fungus Aspergillus
RT lentulus IFM 54703T.";
RL Genome Announc. 4:e01568-15(2016).
RN [2] {ECO:0000313|EMBL:KAF4179381.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CNM-CM8060 {ECO:0000313|EMBL:KAF4179381.1};
RA dos Santos R.A.C., Steenwyk J.L., Rivero-Menendez O., Mead M.E.,
RA Silva L.P., Bastos R.W., Alastruey-Izquierdo A., Goldman G.H., Rokas A.;
RT "Genomic and phenotypic heterogeneity of clinical isolates of the human
RT pathogens Aspergillus fumigatus, Aspergillus lentulus and Aspergillus
RT fumigatiaffinis.";
RL bioRxiv 0:0-0(2020).
RN [3] {ECO:0000313|EMBL:KAF4179381.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CNM-CM8060 {ECO:0000313|EMBL:KAF4179381.1};
RA Santos R.A.C., Steenwyk J.L., Rivero-Menendez O., Mead M.E., Silva L.P.,
RA Bastos R.W., Alastruey-Izquierdo A., Goldman G.H., Rokas A.;
RL Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00001214};
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 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 Evidence={ECO:0000256|ARBA:ARBA00000175};
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 Evidence={ECO:0000256|ARBA:ARBA00000343};
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 Evidence={ECO:0000256|ARBA:ARBA00001540};
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 Evidence={ECO:0000256|ARBA:ARBA00000936};
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:GIM36486.1}.
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DR EMBL; BCLY01000004; GIM36486.1; -; Genomic_DNA.
DR EMBL; JAAAPS010000019; KAF4179381.1; -; Genomic_DNA.
DR STRING; 293939.A0A0S7DHN5; -.
DR VEuPathDB; FungiDB:TMP_alenIFM54703_2254; -.
DR OrthoDB; 5488314at2759; -.
DR Proteomes; UP000713487; Unassembled WGS sequence.
DR GO; GO:0005835; C:fatty acid synthase complex; IEA:UniProtKB-UniRule.
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:0016297; F:acyl-[acyl-carrier-protein] hydrolase 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:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
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; SSF51412; Inosine monophosphate dehydrogenase (IMPDH); 1.
DR SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR005562};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
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 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; 231950 MW; 93D0EB9DBE5453BB CRC64;
MYGASTGPQT GINTPRSSQS LRPLILTHGS LEFSFLVPTS LHFYASQLKD TFTASLPQPT
DELAQDDEPS SVAELVARYI GHVAREVEEG EDDAQGTCLE VLKLALNEFE RAFMRGNDVH
AVAAALPGIT AKKILVVEAY YAGRAAAGRP TKPYESALFR AASEEKASIY SVFGGQGNIE
EYFDELREIY TTYPSFVEDL ISSSADLLQQ LSREPEASKL YPKGLDVIQW LHDRDSQPDI
DYLVAAPVSL PLIGLVQLAH FVVTCKVLGR QPGEILERFS GTTGHSQGVV TAAAIASATT
WESFEKAAKD ALTMLFWIGL RSQQAYPRTS IAPSVLQDSI ENGEGVPTPM LSIRDLPRSA
VQEHIDTTNQ HLPADRHISI SLVNSARNFV VTGPPLSLYG LNLRLRKVKA PTGLDQNRVP
FTQRKVRFVN RFLPITAPFH SQYLYAAYDR ILEDLEDIEI SAKSLAIPVY DTKTGDDLRQ
SGDANIVPSL VRMITHDAVN WEKATVFQGA THIVDFGPGG ISGLGVLTNR NKDGTGVRVI
LAGAMDGTNA EVGYKPELFD RDEHSVKYAI DWVKEYGPRL VKDATGQTFV DTKMSRLLGI
PPIMVAGMTP TTVPWDFVAA TMNAGYHIEL AGGGYYNGKS MTEAISKIEK TIPPGRGITV
NLIYVNPRAM AWQIPLIGKL RADGVPIEGL TIGAGVPSIE VANEYIETLG IKHIAFKPGS
VDAIQQVINI AKANPKFPVI LQWTGGRGGG HHSFEDFHQP ILQMYSRIRR CENIVLVAGS
GFGGAEDTYP YLSGAWSSSF GYPPMPFDGC LFGSRLMIAK EAHTSKNAKK AIADAPGLDD
KDWEKTYRGP AGGVVTVLSE MGEPIHKLAT RGVLFWHEMD QKIFKLDKAK RVPELKKQRD
YIIKKLNDDF QKVWFGRNAA GEAVDLEDMT YAEVVHRMVE LMYVKHESRW IDASLKKLTG
DFIRRVEERF TAEEGQASLL QNYSELDTPY PAIDNILAAY PEAATQLINA QDVHHFLLLC
QRRGQKPVPF VPALDENFEY WFKKDSLWQS EDLEAVVGQD VGRTCILQGP MAAKFSNTID
EPVQQILDGV HQGHIKGLLQ DVYGGDESKI PVIEYFGGRL HEAVSELDID GLTISEDTNK
ISYRLSSSPS GDLPDLDLWL RLLAGKSYSW RHALFLADVF VQGHRFQTNP MKRIVAPTPG
MYVEVSYPEE PSKTTICVRE PYQSGKLVKT VEVKVNDQGQ ISLTLFEGRT AEGGVVPLSF
LFTYHPEAGY APIREVMDGR NDRIKEFYYR VWFGSKDVPF DTPTTATFSG GRETITAQAV
ADFVHAVGNT GEAFVDRPGK EVFAPMDFAI VVGWQAITKP IFPRTIDGDL LKLVHLSNGF
KMVPGAQPLK VGDVLDTTAQ INAVINQDSG KMVEVCGTIH RDGQPIMHVT SQFLYRGSYL
DFENTFQRKD EVPMQVHLAS SRDVAILRSK EWFRLDEPDV ELLGQTLTFR LQSLIRFKNK
SVFSHVQTVG QVLLELPTKE VIQVATVDYE TGTSHGNPVI DYLQRNGTSI EQPVYFENPI
PLSGKTPLVL RAPASNETYA RVSGDYNPIH VSRVFSSYAN LPGTITHGMY TSAAVRSFVE
TWAAENNIGR VRGFHVSLVG MVLPNDMITV KLQHVGMVAG RKIIKVEASN KETEDKVLLG
EAEVEQPVTS YVFTGQGSQE QGMGMELYSS SPVAREVWDR ADRHFIENYG LSIIDIVKNN
PKELTVYFGG PRGKAIRQNY MSMTFETVNA DGTIKSEKIF KEINEDTTSY TYRSPSGLLS
ATQFTQPALT LMEKASFEDM RSKGLVQRDS SFAGHSLGEY SALAALADVM PIESLVSVVF
YRGLTMQVAV ERDEQGRSNY SMCAVNPSRI SKTFNEQALQ YVVENIAEQT GWLLEIVNYN
VANMQYVAAG DLRALDCLTN LLNYLKAQNI DIPALMQSMS LDDLKAHLVK IIHECVKQTE
SKPRPIVLER GFATIPLKGI DVPFHSTFLR SGVKPFRSFL LKKINKTTID PGKLIGKYIP
NVTARPFEIT KEYFEDVYRL TNSPRIAHIL ANWDKYEEGG ENTSRATGTT NA
//
