ID A0A0A2VNY9_BEABA Unreviewed; 2103 AA.
AC A0A0A2VNY9;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Fatty acid synthase subunit beta {ECO:0000313|EMBL:KGQ09323.1};
GN ORFNames=BBAD15_g5337 {ECO:0000313|EMBL:KGQ09323.1};
OS Beauveria bassiana D1-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ09323.1, ECO:0000313|Proteomes:UP000030106};
RN [1] {ECO:0000313|EMBL:KGQ09323.1, ECO:0000313|Proteomes:UP000030106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D1-5 {ECO:0000313|EMBL:KGQ09323.1,
RC ECO:0000313|Proteomes:UP000030106};
RA Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J., Lu Y.,
RA Du Q., Sun Z.;
RT "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT bassiana D1-5.";
RL Submitted (OCT-2012) 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 -!- 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:KGQ09323.1}.
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DR EMBL; ANFO01000464; KGQ09323.1; -; Genomic_DNA.
DR STRING; 1245745.A0A0A2VNY9; -.
DR eggNOG; ENOG502QQJX; Eukaryota.
DR HOGENOM; CLU_000114_5_0_1; -.
DR Proteomes; UP000030106; 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; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 2.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
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:UP000030106};
KW Transferase {ECO:0000256|PIRNR:PIRNR005562}.
FT DOMAIN 1695..2047
FT /note="Malonyl-CoA:ACP transacylase (MAT)"
FT /evidence="ECO:0000259|SMART:SM00827"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2081..2103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1948..1975
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 286
FT /note="For acetyltransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR005562-1"
FT ACT_SITE 1839
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR005562-1"
SQ SEQUENCE 2103 AA; 232896 MW; 80A37CEBDD71A05C CRC64;
MYGAANGAQT GINTPRSSSS LRPLTLSHGI LETSFLIPTS LHFHASQLKE RFTANLPTPT
DELAQDDEPS SVAELVARYL GFVADQVETG EDDSQGSYEE VLKLVLNEFE RAFLHGNEVH
AVAATLPGIE LKKLEVIKSY YAARSVINRT IKPHESALLR AADDGAADLY TIFGGQGNIE
EYFEELRQIF TTYSGFVSEL ITSSAELLQT LSNDPSAEKS FPKGLDIMNW LQHPEATPDI
DYLISAPVSF PLIGLVQLAH YEVTCKVLGI NPGHLRERLR GSTGHSQGIV MAAATAAADS
WESWRDIATS TLTILFWIGT RSQQAFPVTS MTPTMLRESM DHGEGTPTPM LSIRDLSQQE
VQKHIDATNQ YLPANRHISI SLINSPRNLV VTGPPTSLYG LNSQLRKVKA PTGLDQTRVP
YTERKVRFAN RFLPITAPFH SQYLTEATAL IDEDLKNIVI DSSSLSIPVF DTNTGKDLRT
EVSGNIVPTL VRLITRDPVN WETATVFPNA SHVLDFGPGG ASGLGNLTSR NKEGTGVRVI
IAGAIEGALD AVGYKPELFD RDEENAITYA IDWVKEFGPK LVKNSKGEKY VDTKMSRLLG
LPPVMVAGMT PATVPWDFVA ATMNSGYHIE LAGGGYFNAK TMSQALDKIE KAIPAGRGIT
VNLIYVNPRA MAWQIPLLGR LRAEGVPIEG LTIGAGVPSI EVAQEYIETL GLKHIAFKPG
SVEAVQAVIN IAKANPTFPV LLQWTGGRGG GHHSFEDFHQ PILQMYGRIR RQENIILVAG
SGFGGADDTY PYVTGDWSKK YGYPPMPFDG CLFGSRMMVA KEAHTSKDAK QAIIDAPGLE
DAQWEQTYKG PAGGVITVRS EMGEPIHKLA TRGVRFWAEM DQKIFALPKE KRVAELKKNR
DYIIKKLNDD FQKVWFGCNK DGNAVDLEDM TYAEIVRRLV DLLYVKHQKR WIDASFARLT
GDFIHRVEER FTTTPGKPSH LQSYAELDEP YSAVKRILSF YPDAEKQIVN AQDVQHFLLL
CMRPGQKPVT FIPALDGNFE FFFKKDSLWQ SEDLDAVIDQ DVGRTCILQG PTAVKFSTIL
DEPVKSILDG IHNSHIEYLT RDYYGGKESA IPTIEYFGGE LVETEIPLDI EGLTVSYDEH
KNTYRLASGA GATMPPLDAW LSLLAGPNRN WRHALLMSDV IVQGQKFQTN PLRRIFAPYR
GLFVEINYPN DPSRTEIIVK EQPRYNQYVT VIEVKFAGKN EILVNMIKDT TALGRPLGLP
LRFTYHPEAG YAPIREVMDD RNDRIKEFYW KAWFGEDPMD LDALVTSKFD GGKTTITAEA
INDFVHAVGN TGEAFVDRPG KVVYAPMDFA IVVGWKAITK PIFPRKIDGD LLKLVHLSNG
FRMLPGAEPL KKGDEISTTA QINAVINQES GKMVEVCGTI TREGQPVMEV TSQFLYRGAY
TDFENTFQRK VETPVEVHLA TSKDVAVLRS KEWFSTDEMP NDFDLLGKTL TFRLQSLMRY
KNKDSFSSVE TRGEVLLELP TKEIIQVASV DYDAGDSQGN PVIDYLERHG TPLDQPINFE
NPIPLSGRTP LQLRAPASNE TYARVSGDYN PIHVSRVFSS YASLPGTITH GMYSSAAVRS
LVETWAAENN VGRVRSFHAS LVGMVLPNDD IQVQLQHVGM VAGRKIIKVE VSNKETEEKV
LLGEAEVEQP VTAYVFTGQG SQEQGMGMEL YDSSPVAKEV WDRADKYLLD NYGFSITNIV
RNNPKELTIH FGGPRGKAIR QNYMAMTFET VAADGSIKSE RIFKDVDEKT TSYTYRSPTG
LLSATQFTQP ALTLMEKASF EDMKSKGLVP RDSTFAGHSL GEYSALAALA DVMPIESLVS
VVFYRGLTMQ VAVERDAAGR SNYSMCAVNP SRISKTFNEE ALQFVVNNIS EETGWLLEIV
NYNIANMQYV CAGDLRALDT LAGVTNFLKM QKIDIEEMRS NIEEAKDALR EIIRGCAEAT
LKKPVPLELE RGFATIPLRG IDVPFHSTFL RSGVKPFRSF LLKKINKTTI DPPKLVGKYI
PNVTAKPFAL TKEYFEDVYK LTNSPKIGAV LANWDKITQD GGEAKSGSDS GVSAEHDGPG
AAA
//
