ID A0A0L1JHY4_ASPNO Unreviewed; 2026 AA.
AC A0A0L1JHY4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Putative fatty acid synthase subunit beta {ECO:0000313|EMBL:KNG91371.1};
GN ORFNames=ANOM_000416 {ECO:0000313|EMBL:KNG91371.1};
OS Aspergillus nomiae NRRL 13137.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG91371.1, ECO:0000313|Proteomes:UP000037505};
RN [1] {ECO:0000313|EMBL:KNG91371.1, ECO:0000313|Proteomes:UP000037505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG91371.1,
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:KNG91371.1}.
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DR EMBL; JNOM01000003; KNG91371.1; -; Genomic_DNA.
DR RefSeq; XP_015412294.1; XM_015545674.1.
DR STRING; 1509407.A0A0L1JHY4; -.
DR GeneID; 26802220; -.
DR OrthoDB; 2417129at2759; -.
DR Proteomes; UP000037505; Unassembled WGS sequence.
DR GO; GO:0005835; C:fatty acid synthase complex; IEA:UniProtKB-UniRule.
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:InterPro.
DR GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:InterPro.
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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; 6.10.60.10; -; 1.
DR Gene3D; 6.20.240.10; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
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; 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; 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 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 1644..1945
FT /note="Malonyl-CoA:ACP transacylase (MAT)"
FT /evidence="ECO:0000259|SMART:SM00827"
FT ACT_SITE 268
FT /note="For acetyltransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR005562-1"
FT ACT_SITE 1788
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR005562-1"
SQ SEQUENCE 2026 AA; 224174 MW; E31D66DAC874D037 CRC64;
MASTPSSGSY DLAIVTPSED YSLRSFSLAQ GNIQQTFLVS AQDGAFLDQQ KASFLQNHSK
DQSILALVFA FLQFLLDEDC PPAPLGAFLG AIESQCVRDT NIHDLVMPEP EAKNIIRTYY
RAHAVAGLSP RPAPSGLFTT TNNDAHRILM AFGGQGSTNL VCVDELAELY SLYQPLLEPL
IASVAPALAS LSRDPSTSQH YLGREIDLYS WLTNPESRPD RAFTATAAVS FPIIGLLDMA
HYYVLGKLLN SDSPKRLRSS LQGLTGHSQG IIVAAAVAQA DSWASFLAQA QWAIRLLFWM
GYECHTAAPV SPLSSAAIRD SIEHGEGSPS WLLSVRGLRY PALDALIADC NRRLPESEHV
SIGLINTERN LVVAGTPRSL RGLCLRLREI EADDGQDQSR VPFRQRKPVV HHTFLPVSAP
FHSSHLRAAA DRVKARFPDA SSPKVGDLLT AVFHTRTGQD MREMFSPSTN LIQSLVEAVA
CETVDWPATL QVSRSTPPSH IVLLSSSRLS DLVSEIVDGR GVRIIAGTVL APTDTTTLGG
KAELLTAKPS QAPVPWGDLF KARLVAGPDG KPALETRLSE LLQAPPIITA GMTPTTVHWD
FVAAVMQAGY HVELAGGGYF DAAGMTAAIE KLAVHVPPGR GITCNLIYAS PHSIAFQIPL
IRSMIQRGIP IDGLTIGAGV PSLDVVKEWI QTLGIKHLSL KPGSIAAIYE VIEIAKMHPS
FPIILQWTGG RGGGHHSCED FHEPLLQTYR DIRRCSNLYL VVGSGFGQAD QMHPYITGEW
SLPFGHALMP CDGILIGSRM MVAREAHTST QAKKLILAAA GVPDSEWEQT FKKPTGGVLT
VQSEMGQPIH KLATRGVRLW HEMDRTIFSL PRDKRVAALL ARKPEIIRRL SADFAKPWFG
YNAAGDAVDL EDMTYTEVIA RLIRLVYVSH QHRWIDASYR QLVLDFTYRT LERVSDVVYA
TDKLDLSRPE QFVEQVQQLC PAATTRRLHP DDVRFFLTAC KKRGRKPVNF IPALDEDFEY
WFKKDSLWQS EDVDAIIDQD AERVCILQGP VAVQYSRRED QSAKDILDEI HHGLVDRFEE
ERPQTDRPPL AISEMVSSQI TVTESNTHRI IRPASENLLS VEDWQTFLAS QVTGGVRSVL
TAEQVTRDSQ RQANPLRRVL EPRIGQSVQL PLGGSDLLLV EDTQNRPLVH IKPSGAEEVA
VDFYYYDFLE TPAVLRFTYQ CNSKSLSLVE NLEGRDDRVK LFYAHLWRGR ADLSSHRLSD
VFEGEEITLS SDLHRHLHNA LRHTVPDATA SATTNTLPLE AAIIAAWKPL MEPLFVAELQ
GDLLRLVHLS NSIRYAPGAT PLEVNDVVAT KSQVRAVTIK ETGKTISVEA QILRSQTLVA
TVTSEFFIKG SFSDYETTFS HQDEAATELK VQSAIDEALL RDREWLLLDD PTQSLINKTL
VFRLHTVTRW KDQSTFASLK TTGSIYAKHW NGTEQRVGSV VSELAECHGN PVIDFLQRKG
TVVQEKVPLK HPGLIDNGSR TIRLPFNNAL YSSVSKDYNP IHTSSVFARF ADLPGTITHG
MYTAAVSRAV TECLAADGET GRLRSFSASF VGMVLPGDQL TVRIRHEAMC HGRMVLSVAA
YREGTDEKVL QGEAEVEQRT SAYLFTGQGS QAQSMGMQLY ESSPVARAVW DEVDRRLLDQ
YGWSILNVVR ANPKEITIHF RGARGRRIRD NYLAMRTETR MPDGSTRLEP ILRDLTPKSE
SYTFFDSRGL LYATQFAQPA ILLMEKAAFE DMKANGLIQE GAAFAGHSLG EYGVLASLVD
FLPFEMMMSV VFYRGLVMQF TMERDSNGHT GFSMVAVSPK RVGKYFDEAM LRIVVDLIHR
QSGNLLEIVN FNVEAEQYVC AGHVRNIYVL TGILDLLSQS STGPQLVDSL RRAADPAITD
VAKEIAVHLE KAPQLNNPTE LKRGRATIPL QGIDVPFHSS HLRSGVSVYR RFLEERIQAE
NVQVDRLVGK FIPNVMGKPF AIDRPYLEEA AAVTGSSVLR ELALAA
//
