ID Q5J3D3_ASPFL Unreviewed; 1671 AA.
AC Q5J3D3;
DT 15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE SubName: Full=HexA {ECO:0000313|EMBL:AAS90071.1};
OS Aspergillus flavus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5059 {ECO:0000313|EMBL:AAS90071.1};
RN [1] {ECO:0000313|EMBL:AAS90071.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AF36 {ECO:0000313|EMBL:AAS90071.1};
RA Ehrlich K.C., Cotty P.J.;
RT "Comparison of the aflatoxin biosynthesis gene cluster from five
RT Aspergillus species.";
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+)
CC + NADPH; Xref=Rhea:RHEA:17397, Rhea:RHEA-COMP:9916, Rhea:RHEA-
CC COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:78776, ChEBI:CHEBI:78827; EC=1.1.1.100;
CC Evidence={ECO:0000256|ARBA:ARBA00001572};
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 -!- SIMILARITY: Belongs to the thiolase-like superfamily. Fungal fatty acid
CC synthetase subunit alpha family. {ECO:0000256|ARBA:ARBA00007485,
CC ECO:0000256|PIRNR:PIRNR000454}.
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DR EMBL; AY510455; AAS90071.1; -; Genomic_DNA.
DR VEuPathDB; FungiDB:AFLA_006308; -.
DR VEuPathDB; FungiDB:F9C07_1482337; -.
DR GO; GO:0005835; C:fatty acid synthase complex; IEA:InterPro.
DR GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; IEA:InterPro.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0004312; F:fatty acid synthase activity; IEA:InterPro.
DR GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0018130; P:heterocycle biosynthetic process; IEA:UniProt.
DR GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd00828; elong_cond_enzymes; 1.
DR CDD; cd08950; KR_fFAS_SDR_c_like; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 6.10.250.1930; -; 1.
DR Gene3D; 3.90.470.20; 4'-phosphopantetheinyl transferase domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR008278; 4-PPantetheinyl_Trfase_dom.
DR InterPro; IPR037143; 4-PPantetheinyl_Trfase_dom_sf.
DR InterPro; IPR040899; Fas_alpha_ACP.
DR InterPro; IPR047224; FAS_alpha_su_C.
DR InterPro; IPR026025; FAS_alpha_yeast.
DR InterPro; IPR041550; FASI_helical.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR004568; Ppantetheine-prot_Trfase_dom.
DR InterPro; IPR016039; Thiolase-like.
DR NCBIfam; TIGR00556; pantethn_trn; 1.
DR PANTHER; PTHR10982:SF23; FATTY ACID SYNTHASE SUBUNIT ALPHA; 1.
DR PANTHER; PTHR10982; MALONYL COA-ACYL CARRIER PROTEIN TRANSACYLASE; 1.
DR Pfam; PF01648; ACPS; 1.
DR Pfam; PF18325; Fas_alpha_ACP; 1.
DR Pfam; PF18314; FAS_I_H; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR PIRSF; PIRSF000454; FAS_yeast_alpha; 3.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF56214; 4'-phosphopantetheinyl transferase; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR000454-3};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000454-3};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450,
KW ECO:0000256|PIRNR:PIRNR000454};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000454}.
FT DOMAIN 75..153
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 926..1428
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT REGION 1244..1285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1499..1520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1244..1282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1113
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-1"
FT BINDING 1552
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-3"
FT BINDING 1653
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-3"
FT MOD_RES 113
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-4"
SQ SEQUENCE 1671 AA; 181401 MW; C34B122D7B69500B CRC64;
MVIQGKRLAA SSIQLLASSL DAKKLCYEYD ERQAPGVTQI TEEAPTELPP LSSPPSLPQA
PNVSPISASK IVIEDVALSR VQIVQALVAR KLKTAIAQLP TSKSIKDLSG GRSSLQNELV
GDIHNEFSSI PDAPEQILLR DFGEANPTVQ LGKTSSAAVA KLISSKMPSD FNANAIRAHL
ANKWGLGPLR QTAVLLYAIA SEPPSRLTSS SAAEEYWDNV SSMYAESCGI TLRPRQDTMN
EDAMASSAVD PAAVAELSKA HRRLGVQQFQ ALAEYLQIDL SESQASQSDA MVAELQQKVD
LWTAEMTPKF LAGISPMLDV KKSRRYGSWW NMARQDVLAF YRRPSYSEFV DDALAFKVFL
NRLCNRADEA LLNMVRSLSC DAYFKQGSLP GYHAASRLLE QAITSTVADC PKARLILPAV
GPHTTITKDG KIEYAEAPRQ GVSGPTAYIQ SLRQGASFIG LKSADVDTQS NLTDALLDAM
CLALHDGISF VGKTFLVTGA GQGSIGAGVV RLLLEGGARV LVTTSREPAT TSRYFQQMYD
NHGAKFSELR VVPCNLASAQ DCEGLIRHVY DPRGLNWDLD AILPFAAASD YSTEMHDIRG
QSELGHRLML VNVFRLLGHI VHCKRDAGVD CHPTQVLLPL SPNHGIFGGD GMYPESKLAL
ESLFHRIRSE SWSDQLSICG VRIGWTRSTG LMTAHDIIAE TVEEHGIRTF SVAEMALNIA
MLLTPDFVAH CEDGPLDADF TGSLGTLGSI PGFLAQLHQK VQLAAEVIRA VQAEDEHERF
LSPGTKPTLQ APVTPVHPRS SLRVGYPRLP DYEQEIRPLS PRLERLQDPA NAVVVVGYSE
LGPWGSARLR WEIESQGQWT SAGYVELAWL MNLIRHVDDE SYVGWVDTQT GKPVRDGEIQ
ALYGDHIDNH TGIRPIQSTS YDPERMEVLQ EVAVEEDLPE FEVSQLTANA MRLRHGANVS
IRPSGNPDAC RVKLKRGAVI LVPKTIPFVW GSCAGELPKG WTPAKYGIPE NLIHQVDPVT
LYTICCVAEA FYSAGITHPL EVFRHIHLSE LGNFIGSSMG GPTKTRQLYR DVYFDHEIPS
DVLQDTYLNT PAAWVNMLLL GCTGPIKTPV GACATGVESI DSGYESIMAG KTKMCLVGGY
DDLQEEASYG FAQLKATVNV EEEIACGRQP SEMSRPMAES RAGFVEAHGC GVQLLCRGDI
ALQMGLPIYA VIASSAMAAD KIGSSVPAPG QGILSFSRER ARSSMISVTS RPSSRSSTSS
EVSDKSSLTS ITSISNPAPR AQRARSTIDI APLRAALATW GLTIDDLDVA SLHGTSTRGN
DLNEPEVIET QMRHLGRTPG RPLWAICQKS VTGHPKAPAA AWMLNGCLQV LDSGLVPGNR
NLDTLDEALR SASHLCFPTR TVQLREVKAF LLTSFGFGQK GGQVVGVAPK YFFATLPRSE
VEGYYRKVRV RTEAGDRAYA AAVMSQTVVK IQTQNPYDEP DAPRIFLDPL ARISQDPSTG
QYRFRPDATP ALDDDALPPP GEPTELVKGI SSAWIEEKVR PHMSPGGTVG VDLVPLASFD
AYKNAIFVER NYTVRERDWA EKSADVRAAY ASRWCAKEAV FKCLQTHSQG AGAAMKEIEI
EHGGNGAPKV KLWGAAQTAA RQRGLEGVQL SISYGDDAVI AVALGLMSGA S
//
