ID A0A0L1ILH5_ASPNO Unreviewed; 2074 AA.
AC A0A0L1ILH5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Sterigmatocystin biosynthesis fatty acid synthase subunit beta {ECO:0000313|EMBL:KNG80436.1};
GN ORFNames=ANOM_011485 {ECO:0000313|EMBL:KNG80436.1};
OS Aspergillus nomiae NRRL 13137.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG80436.1, ECO:0000313|Proteomes:UP000037505};
RN [1] {ECO:0000313|EMBL:KNG80436.1, ECO:0000313|Proteomes:UP000037505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG80436.1,
RC ECO:0000313|Proteomes:UP000037505};
RA Moore M.G., Shannon B.M., Brian M.M.;
RT "The Genome of the Aflatoxigenic Filamentous Fungus Aspergillus nomius.";
RL Submitted (JUN-2014) 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:KNG80436.1}.
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DR EMBL; JNOM01000605; KNG80436.1; -; Genomic_DNA.
DR RefSeq; XP_015401359.1; XM_015556741.1.
DR STRING; 1509407.A0A0L1ILH5; -.
DR GeneID; 26813289; -.
DR OrthoDB; 5488314at2759; -.
DR Proteomes; UP000037505; 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; 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; PF01575; MaoC_dehydratas; 1.
DR Pfam; PF16073; SAT; 1.
DR PIRSF; PIRSF005562; FAS_yeast_beta; 2.
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; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000037505};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR005562}.
FT DOMAIN 1674..1995
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 1818
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR005562-1"
SQ SEQUENCE 2074 AA; 229931 MW; CD8A99B3F4C83B0B CRC64;
MYGSSTGPQT GINTPRSSQS LRPLILSHGS LEFSFLVPTS LHFQASQLKD TFTASLPEPT
DELAQDDEPS SVAELVARYI GHVATEVEEG EDDAHGTNLE VLKLALNEFE RAFMRGNDVH
AVASALPGIT AKKASVVKAY YAGRAAAGRP TKPYDSALFR AASDEKANIY TVFGGQGNIE
EYFDELREIY TTYPSFVDEL IASSAQLLLS LSREPEASKL YPKGMDIIQW LQDPDSQPDT
DYLVSAPVSL PLIGLVQLAH FVVTCKALGR EPSEVLERFS GTTGHSQGVV TAAAIASATT
WESFEKVAKD ALTMLFWIGL RSQQAYPRTS IAPSVLQDSI ENGEGTPTPM LSIRDLPRSA
VQEHIDMTNQ HLPEDRHISI SLVNSARNFV VTGPPLSLYG LNLRLRKVKA PTGLDQNRVP
FTQRKVRFVN RFLPITAPFH SQYLYSAYDR ILEDLEDLEI PAKSLAIPVY GTKTGEDLRE
FGDANIVPAL VRMITHDAVN WEQATVFPRA THIVDFGPGG ISGLGVLTNR NKDGTGVRVV
LAGAMDGTNA EVGYKPELFD RDEHAVKYAI DWVKEYGPRL VKNAAGETFV DTKMSRLLGI
PPIMVAGMTP TTVPWDFVAA TMNAGYHVEL 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 IDGSLKKLTG
DFIRRVEERF TTLGGQPSLL QNYSELNTPY PAVDNILAAY PEAATQLINA QDVQHFLLLC
QRRGQKPVPF VPSLDENFEY 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 DTPTTATFNG GRETISSQAV
ADFVHAVGNT GEASWIALER KSLLLWTSPS SLAGKPLPSP SSLMVPGAQP LKVGDVLDTT
AQINAVINQD SGKMVEVCGT IKRDGKPIMH VTSQFLYRGA YLDFENTFQR KDEVPMQVHL
ASSRDVAILR SKEWFRIDEP DVELLGQTLT FRLESLIRFK NKSVFSHVQT VGQVLLELPT
KEIIQVASVD YEAGDSHGNP VVDYLQRNGT SIEQPVYFEN PIPLSGKTPL ELRAPASNET
YARVSGDYNP IHVSRVFSSY ANLPGTITHG MYTSAAVRSY VETWAAENNI GRVRGFHVSL
VGMVLPNDMV TVKLQHVGMI AGRKIIKVEA SNKETEDKVL LGEAEVEQPV TSYVFTGQGS
QEQGMGMELY SSSPVAREVW DRADRHFMEN YGLSIIDIVK NNPKELTVYF GGPRGKAIRQ
NYMSMTFESV NADGSIKSEK IFKEVDENTT SYTYRSPSGL LSATQFTQPA LTLMEKASFE
DMRSKGLVQR DSSFAGHSLG EYSALAALAD VMPIESLVSV VFYRGLTMQV AVERDEQGRS
NYSMCAVNPS RISKTFNEQA LQYVVENISE QTGWLLEIVN YNVANMQYVA AGDLRALDCL
TNLLNYLKAQ NIDIPALMQS MSLEDVKAHL VKIIHECVKQ TESKPKPIAL ERGFATIPLR
GIDVPFHSTF LRSGVKPFRS FLLKKINKNT IDPSKLVGKY IPNVTARPFE LTKEYFEDVY
RLTNSPRIAN ILANWEKYEE ESENVSRGGG TTSA
//
