ID A0A1F8A6B9_9EURO Unreviewed; 2026 AA.
AC A0A1F8A6B9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Malonyl-CoA:ACP transacylase (MAT) domain-containing protein {ECO:0000259|SMART:SM00827};
GN ORFNames=ABOM_004000 {ECO:0000313|EMBL:OGM47233.1};
OS Aspergillus bombycis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=109264 {ECO:0000313|EMBL:OGM47233.1, ECO:0000313|Proteomes:UP000179179};
RN [1] {ECO:0000313|EMBL:OGM47233.1, 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 -!- 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:OGM47233.1}.
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DR EMBL; LYCR01000025; OGM47233.1; -; Genomic_DNA.
DR STRING; 109264.A0A1F8A6B9; -.
DR OrthoDB; 2158695at2759; -.
DR Proteomes; UP000179179; 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; 6.10.140.1400; -; 1.
DR Gene3D; 6.10.60.10; -; 1.
DR Gene3D; 6.20.240.10; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000179179};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR005562}.
FT DOMAIN 1644..2021
FT /note="Malonyl-CoA:ACP transacylase (MAT)"
FT /evidence="ECO:0000259|SMART:SM00827"
FT REGION 1086..1118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1087..1118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 273
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; 223254 MW; DB97B9D3A1A9B2A1 CRC64;
MIHSDRAVPS SSPAEMKGRL SLIFKGILVS LTIIDLDDWN FLQGQRDDFL WSLVQLPTDS
EGPRSPVEVV LSFIRYLLDQ EATPPSALRA VVRAFDDQFL RDSEVHAVIA QITKSPAERG
RWLETYYRAA CTTPGAYTGP QSALLQEALR GNFQLVGIFG GQGSRNTLCI QELRELYNTY
QPFLGDLFRV AGGRLRDLSR SPEASTQLNH PLDLESWMRD PQTTPTPTEM AEAPVSMPIT
GLLSLARYAV SCHLLGLTPG QLGSHFNSFT GHSQGILTAV VVALSDTWAS FYHYAEMALE
LLFWIGFQCY KSTPRASLPA NTEKSPSCML DISGMQLSQA ESTIAQINEG LDASERVHTS
VVNTRDRVVI GGPAGSLARL DSYLTSIAAS SNNQNRVPFS SRKPIFSHGF LPISIPFHTP
HLNHISTELK TRFTDKVVIG AQLRLSVRHT RTGHDIKQSR TANLIPMLID AILLEICDWP
AALALPESTT HILSFDPSMA PLAKLNVDGR GMRIISALQT DTQDEEIGNI LDLLSPSLLD
SSTKIRPWGQ RFRPRLSASA GGLGRLETRL TELLGTPPVM VAGMTPTTAH WDVVSAIVNA
GYHTELAGGG YYKEGDLSAA VKKVLQSIPQ GRGVTVNLIY ADPKAISWQI PLLQQLSRNQ
YHIQGLTIGA GVPSADVVAE YINSIGIQHI SLKPGSVPGI RDVIDIAKAH PNFPVIMQWT
GGRGGGHHSF EDFHAPILSM YAAIRRCTNI YLVAGSGFGS ADDIYPYLTG TWSVELGYPK
MPFDGVLLGS RMMVSKEAHT SQAVKELICN TPGVPDNEWE KTYTGSAGGI VTVKSEMGEP
IHKIANRGVM LWAEMDKTVF KLPREDRIAY LEKNKKYIIE RLNSDYAKPW FGRDSKANVV
DISQMTYIDV LRRLVELMYV DHQKRWINAS YTRFVQDIAF RTLERLAIGH GEAVSTSVLE
DDPHLFLESL VKVCPLARFQ LLSPEDASFF IARCKQGGQK PVNFIPTLDE DFEFYFKKDS
LWQSEDLDAV VGQDASRVCV LHGPVAAPYS TRSDESAQDI LDGIVYGLID RFQKGRRRIG
VGCQPESRCQ TPDSCSAASS GPESEVSEAE SETSVASSTL EQPVHAILGA VHGLLFDKYI
TQGHKRTENP FRSLLDSPQH IAKHFNYESS ELVVSAPSNS KSKEYIKIQC HDGQDIAVEV
HQPSAYSQNS VVLPLRYHFD GSSRAITEVM GGRNERIKSF YSKVWFGREI DPNLTVHSTF
HGPEVTFTRR LLTDLSLATG CAFENKDLPF SSSDTLPINV GILAAWESLT QPLVLKDISG
DLLALVHRSN KFEYVEGATP LSLGDTVTST ARVKAVTIEA AGKLVVVQAI IYRAAEEVMV
VTSEFLFRGE FHDYETTFRR TRHQRWAVKA SSDEDEAVLR DREWLHLDND SSSIIGQPLI
FELESFVTYQ SIAKFGSLQV QGSVFLNSGT GERQKIGSVR FQYGPCVGNP VLDFLERKGT
LVSGARVELE KPGWSGKSSI DVKMPKDGHQ YSDVSKDYNP IHTSPTFARL ANLPGTICHG
MYTSAVAAAA FDHLVLDGDR QRFRRFEVSF VDMVLPLESL AVHLQHIAMA QGRMCFKIEV
VRKSDSRKVM EADAEVEQPG TAYLFTGQGS ASPGMGMDLY NSSPLAKAIW DDVDKQFKDT
YGWSLLEIVK NNPKHLTVHF GGRKGRAIRD TYLSLSATVV LPDGSITQRP LLPNLTPKSA
SYTFSDPRGL LFVTMFTQPA ILVLENVAFA VLKAKGYIHE GAMYGGHSLG ELAALTSLLD
RVSIWSIAQI AFYRGLIMGY SSNTGATEGA EFSMVAANPK RVGKGFTPKD LSDIVRAISA
ESQQLLEIAN FNVEGEQYVC TGTTPNLYVL GKVLDHIAHG NHPLPSVSEK EPPEASNSLQ
SIIAGHVQES NRLPTPIKLE RGRATIPLHG INTPFHSSHL RTTVDDYRSL LLRSDVVNWR
GEIGKLAGRY VPNVIGKPFS LEVDYIQKVF DITGSPVLQK ILGSIQ
//
