ID A0A0F8UQE1_9EURO Unreviewed; 1605 AA.
AC A0A0F8UQE1;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KKK21819.1};
GN ORFNames=ARAM_004342 {ECO:0000313|EMBL:KKK21819.1};
OS Aspergillus rambellii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=308745 {ECO:0000313|EMBL:KKK21819.1, ECO:0000313|Proteomes:UP000034291};
RN [1] {ECO:0000313|EMBL:KKK21819.1, ECO:0000313|Proteomes:UP000034291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRRC1468 {ECO:0000313|EMBL:KKK21819.1,
RC ECO:0000313|Proteomes:UP000034291};
RA Moore G.G., Beltz S.B., Mack B.M.;
RT "Draft Genome Sequences of Two Closely-Related Aflatoxigenic Aspergillus
RT Species Obtained from the Cote d'Ivoire.";
RL Submitted (FEB-2015) 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:KKK21819.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JZBS01001662; KKK21819.1; -; Genomic_DNA.
DR STRING; 308745.A0A0F8UQE1; -.
DR OrthoDB; 2289340at2759; -.
DR Proteomes; UP000034291; 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:UniProtKB-EC.
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 Gene3D; 3.30.70.2490; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.90.25.70; -; 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; IPR016035; Acyl_Trfase/lysoPLipase.
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; 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 PIRSF; PIRSF000454; FAS_yeast_alpha; 4.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF56214; 4'-phosphopantetheinyl transferase; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 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 Reference proteome {ECO:0000313|Proteomes:UP000034291};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000454}.
FT DOMAIN 125..212
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 915..1374
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT REGION 1452..1472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1452..1467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1104
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-1"
FT BINDING 1490
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-3"
FT BINDING 1590
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-3"
FT MOD_RES 163
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-4"
SQ SEQUENCE 1605 AA; 173314 MW; A2A9EC13161031C2 CRC64;
MAIHSIERAI AHELVIELLA HQFAFPVQWI ETQETLLRHI RRLVELGPSK TLLGMSQKTI
APNPRQPIQL LACTQDLQQL CYVYDDPEES TVDDPVIGTP VSSTLAEVTA PEPEAEPVPA
VQVQEAPLTA IVIIRALIAR KFRKSAAEID TTQSIKDLCG GKSTLQNELV GELGNEFPTL
PDRPEDVPLG DLDTALGEVS LGQVSSALLQ RVFSAKMPAR MTVATVRARL ATMWGLPTHR
QTAVLVGALA AEPQVRLPSL EAATQYWDGL TEAYAQSVGL SLQRQTVQRS RRPQLTPGDD
DDILALKDSL GAKSLARKQY EALRQYLGIS NSNTETDGLT VELQQRLDSW TAEFSDEFLS
RITPCFDAHR ARQYRDWWNA ARQELLAVCE LGAEAVFTEQ LRDVLCRRSD RSLVRVAQAN
PAARILAPAL VAALDSPPRV RLGESLTMAP QTVVSRTGVI EYHEHPRDPS RFAEFFTHWI
QKNRNPGAAQ SNGTDLTTQM LESLAHASQT GVTFVNKTYL ITGAGPGSIG GHIARLLLAG
GACVIVTTSR EPSVAAPHFK KLYDELDLDA ILPFAATGQV GAEIDGLDAG NEVALRLMLV
NVLRLLGFIV TQKRQRAIHC RPTQVVLPLS PNHGILGGDG LYAESKRGLE TVMRRFHSES
WEEELSICGV NIGWTRSTSL MTTNDMVAET AEQQGKVLTF SGPEMAELIT LLLSPAWATH
CEDAPVMADF SGALGDWQNA AAGLAAARAS IQQRAEIARA IAQEDERESS GRLGTTKAQD
LVPIRASLRL GFPRLPEYMS EVEPLQHQLM PDLVPEDAVV VVGFAELGPW GSARVRWEME
SRGQLSLAGH VEMAWLMNLI RHADGPGPNG HYIGWVDAQS GQPVADAEIP QQYGDTIRTH
AGIRPLPSDN REIFQEIVLD EDLAAFETTR ANAEALLQRH GSNLVTILSS GDGDDDDPSS
TCQVQLRHGA TIRVPKSSMA GPGVAGQLPM GWSPDKYGIP AEIVQQVDPV TLVLLCCVAE
TFYSAGITDP MEIFEHIHLS ELGNFIGSSM GGVVNTRALY HDVSLDQDVP SDALQETYLN
TAPAWVNMLL LGAAGPIKTP VGACATALES IDSALESIQA GHTKICLVGG YDDLQPEESV
GFARMKATAS VPNEQARGRL PTEMSRPTAA SRAGFVESQG CGVQLLCRGD VALAMGLPIY
GIVAGSGMAA DGVSRSVPAP GHGILTFARE NSKSSPAPLR AALARWGLGI DDLTVASLHA
TSTPANDKNE PAVIQSEMAH LGRTPGRPLW AICQKSVTGH PKAPAAAWML NGCLQVLDSG
LVPGNRNADD IEPELRAFDH LCFPTRPVQT AGVRAFLLNS CGFGQKEAQV VGVHPRYFFA
LQSGPEFHAY QIRVQRRTRH AERAYIRALM GNHIVQVQSR PPYEGTDMDS ILLNPSARLH
REQATGSYHV SVPAASSAPT RASPNAASGS VPPLRPVSAP DAHPSTVGVD TVTLSTFTAH
ENLIFLRRNY TDREYQSLQT HRDMRAAVAS GWCAKEAVFK CLKTVSKGAG SAMKEIEILR
SQGAPYVVLH GDALQAAQEA GLQNIQLSLS YADDSVIAIA LGVPQ
//
