ID A0A0L1JI31_ASPNO Unreviewed; 1682 AA.
AC A0A0L1JI31;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=3-oxoacyl-synthase {ECO:0000313|EMBL:KNG91419.1};
GN ORFNames=ANOM_000464 {ECO:0000313|EMBL:KNG91419.1};
OS Aspergillus nomiae NRRL 13137.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG91419.1, ECO:0000313|Proteomes:UP000037505};
RN [1] {ECO:0000313|EMBL:KNG91419.1, ECO:0000313|Proteomes:UP000037505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG91419.1,
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=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}.
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:KNG91419.1}.
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DR EMBL; JNOM01000003; KNG91419.1; -; Genomic_DNA.
DR RefSeq; XP_015412342.1; XM_015545722.1.
DR STRING; 1509407.A0A0L1JI31; -.
DR GeneID; 26802268; -.
DR OrthoDB; 2725016at2759; -.
DR Proteomes; UP000037505; Unassembled WGS sequence.
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 CDD; cd00828; elong_cond_enzymes; 1.
DR CDD; cd08950; KR_fFAS_SDR_c_like; 1.
DR Gene3D; 3.30.70.2490; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.90.470.20; 4'-phosphopantetheinyl transferase domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
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; IPR004568; Ppantetheine-prot_Trfase_dom.
DR InterPro; IPR002347; SDR_fam.
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; PF00106; adh_short; 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 PIRSF; PIRSF000454; FAS_yeast_alpha; 2.
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; 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 Reference proteome {ECO:0000313|Proteomes:UP000037505};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000454}.
FT DOMAIN 913..1437
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT REGION 58..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1497..1519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1502..1519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1099
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-1"
FT BINDING 1568
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-3"
FT BINDING 1569
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-3"
FT BINDING 1570
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-3"
FT MOD_RES 127
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-4"
SQ SEQUENCE 1682 AA; 184559 MW; A83A2A268C1C602E CRC64;
MARKSATRYY KSYATSQWSH LQFLSYQDNK DEILYNYSTS NPWSDKKDRA GQLTSHDVSL
LPLSPGSQRE PQQCVPPKAP LSKSSPSLDV ALSSSHIVLA MTAQKLRRPF DKVSMGRTIR
ELSGGKSTLQ NELVGDFVAE FGKVPEEAED MTLVALGEAL EGAFVGKPAN QMTTLIARLI
SRKMPAGFNQ NSMQDYICSR WGFSKTHCLV PICLATTIEP PARLANADAA QAYLDELVSR
YALFQGISLA SADGLYSDRS EAMPPPGGFS NQEILYKEQH SYHRKHFDKL AKYLQIDLEA
SEQSPLDTTY QETLKRWNAE FDDQFCQGIE SIFNTSQSRN YDSWWNWARE GLIQWLHQIA
SGQVEAALPT KGNHLRRMLN RWDATCSNII EAIIKPPHPI LCPNQTIYPC SDVSLVLKEV
LRLGNLALAS DPIYIYSSPA LGPQTTVSSS GQLDYMEIAR KASSYPDVYA SKTVLVTGAG
PNSIGAQVVQ GLLCGGAQVV VTTSRTISES ASFYQNIYRQ YGARGASLTV LPMNQASKRD
CEYLIEHIYG VNSPIGGDLD YVIPFAAVPQ AGELDALGSH QELALRTMLV NLLRTIGFIR
QQKEKRRISC RPTTIVLPMS CNEGSFGGDG LYAESKAGLK TLLNRFHSEG WSSCITICAA
VMGWTRGTGL MRSSNFIAEE VEKLGVVTFT QAEMAFNILA LMTPEITILA EQAPVYADLT
GGLGKMWDIK DHISASRKRL AEEAQIQKAL HEEDAHHYSV LFGPQKQQPG NSGLNISRRR
AFLKLPFPSL QLYDDLAVSL PNLKGMIDLS RTVVVVGFSE LGPWGNSRTR WEMEHQGRFS
LEGYIEMAWI MGLINHIDGD WKGRSYVGWV DAETQEPIHD HDIPQRYHEY IMSNAGLRLI
EPGGVDTYIP SQKEFLQEVA VEEDLPPFEC SKTSAEAFKL RHGSNITLQP ITGSDNYRVF
LKKGAVLLIP KTVPFHQSVA GVVPTGWDAL RYGIPEEIVQ QVDKTTLYAL CCVSEAFLSA
GISDPYDIYQ HIHVSELANC LGTGGGPMKI IQNMYRDRFL DRQVRGDIIL EHFLNTMGAW
VNMLLLSASG PLKTPVGACA TALESLDIGC DAIISGKCKV AIVGGCDDYR EELSFEFDSI
KATANCAEEL SRGRLPSEIS RPTASSRSGF AESAGCGVQL LMNAELALKL GLPIHGVVAY
CQMASDQVGR SIPAPGKGIL TAARESHEAK VSPMLDFGFR RVGFDEEVAD VEQRFVSGQL
RKAQGSGTPE EAAEQFRRLR VRDAQYRWAH DIRLQDPSIS PLRAALATWG LGIDDIGVVS
THGTSTKAND INEGEVINAQ MEHLGRRKGN PLLCVCQKSL TGHPKAAAGA WQLNGCMQIL
QGGIVPGNRN ADNIDQQLRQ FEHLVYPMES IQTTGVKATM ITSFGFGQKG AIAIIVAPSY
LFASISASMY EKYSMRVTQR QRAANPMFVS RILNNRIVQV KSLPPWENRD ATEKVFLDPG
SCRQDDQTQL TNEAHASPSS SINVIADHTS RTVENQDEGN ALSCLVEGML VEAVGRSKGT
SPPSVGVDVE EIASISIENE AFLKRNFTMA EREYCSKATN PQASFAGRWS AKEAVFKSLQ
TSSSGPGAAM HEIEVLNHCG IPKITLHGQV KDIAQAKGID SVEISISHST NAAVAIAVAV
KG
//
