ID A0A0G2GRL1_9PEZI Unreviewed; 1862 AA.
AC A0A0G2GRL1;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Fatty acid synthase subunit alpha {ECO:0000256|ARBA:ARBA00014008};
DE EC=1.1.1.100 {ECO:0000256|ARBA:ARBA00012948};
DE EC=2.3.1.41 {ECO:0000256|ARBA:ARBA00013191};
DE EC=2.3.1.86 {ECO:0000256|ARBA:ARBA00012878};
GN ORFNames=UCDDS831_g01817 {ECO:0000313|EMBL:KKY25968.1};
OS Diplodia seriata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Diplodia.
OX NCBI_TaxID=420778 {ECO:0000313|EMBL:KKY25968.1, ECO:0000313|Proteomes:UP000034182};
RN [1] {ECO:0000313|EMBL:KKY25968.1, ECO:0000313|Proteomes:UP000034182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS831 {ECO:0000313|EMBL:KKY25968.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY25968.1, ECO:0000313|Proteomes:UP000034182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS831 {ECO:0000313|EMBL:KKY25968.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-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=a fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP]
CC + CO2 + holo-[ACP]; Xref=Rhea:RHEA:22836, Rhea:RHEA-COMP:9623,
CC Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:14125,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78776, ChEBI:CHEBI:138651;
CC EC=2.3.1.41; Evidence={ECO:0000256|ARBA:ARBA00001402};
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 -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000256|ARBA:ARBA00004685}.
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:KKY25968.1}.
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DR EMBL; LAQI01000034; KKY25968.1; -; Genomic_DNA.
DR Proteomes; UP000034182; 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:UniProtKB-EC.
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:0004321; F:fatty-acyl-CoA synthase activity; IEA:UniProtKB-EC.
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:0042759; P:long-chain fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
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; 3.30.70.2490; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.90.25.70; -; 1.
DR Gene3D; 6.10.140.1390; -; 1.
DR Gene3D; 6.10.140.1410; -; 1.
DR Gene3D; 6.10.250.1930; -; 1.
DR Gene3D; 6.10.250.1940; -; 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 HAMAP; MF_00101; AcpS; 1.
DR InterPro; IPR008278; 4-PPantetheinyl_Trfase_dom.
DR InterPro; IPR037143; 4-PPantetheinyl_Trfase_dom_sf.
DR InterPro; IPR002582; ACPS.
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; 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; 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 Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
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 NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Phosphopantetheine {ECO:0000256|PIRNR:PIRNR000454,
KW ECO:0000256|PIRSR:PIRSR000454-4};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000454}.
FT DOMAIN 141..216
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1093..1633
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT REGION 580..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1279
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-1"
FT BINDING 1748..1750
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-2"
FT BINDING 1748
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-3"
FT BINDING 1749
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-3"
FT BINDING 1750
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-3"
FT BINDING 1774
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-2"
FT BINDING 1784
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-2"
FT BINDING 1793..1809
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-2"
FT BINDING 1817..1820
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-2"
FT BINDING 1847..1849
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-2"
FT BINDING 1848
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-3"
FT BINDING 1849
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-3"
FT MOD_RES 176
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-4"
SQ SEQUENCE 1862 AA; 204549 MW; 123EABEFE3144F94 CRC64;
MRPEIEQELS HTLLVELLAY QFASPVRWIE TQDVILGEKT TERIVEVGPA DTLGVMAKRT
LASKYEAHDA ARSVQRQILC YNKDAKDIYY DVDPVEDEPE APAAESSSAA ASAPAAAAAA
PVAAAPAPSA GPAAAVPDAP VTATDILRAL VAQKLKKPLG DIPLSKAIKD LVGGKSTLQN
EILGDLGKEF GSTPEKPEDS PLDELGASMQ ATFNGQLGKQ SSSLIARLIS SKMPGGFNNT
SARKYLETRW GLAAGRQDGV LLLGLTLEPA ARLGSETDAK AWLDDIAHKY AASAGISLSA
PVVGGDAGAG AGGMMMDPAA IDALTKDQRA LFKQQLELFA RYLKMDLRSG DKAFVGSQET
NKALQAQLDL WNTEHGEFYA AGIEPQFTSL KARVYDSSWN WARQDALTMY YDIIFGRLKA
VDREIVSQCI NIMNRSNPTL LEFMQYHIDH CPTERGETYE LAKELGQQLI ENCKDVLNAA
PVYKDVAMPT APSLNIDARG NMNYAEVPRS SVRKLEHYVK EMAEGGKLSE YGNRTKVQND
LQRIYKLIRQ QHKLSKSSQL QIKTLYGDVI RSLSMNEGQI IPSENGKSAN GRRKGRNGRI
NGTNKQGKVE TIPFLHLKRK DEHGWEYSKK LTGVYLDGLE RAARDGVTFQ GKNVLMTGAG
AGSIGAEVLQ GLISGGAKVV VTTSRFSRQV NEYYQSIYSR FGARGSQLIV VPFNQGSKQD
VEALVNYIYD AKNGLGWDLD YVVPFAAISE NGREIDGIDS KSELAHRIML TNLLRLLGCV
KQQKHANSYE TRPAQVILPL SPNHGTFGND GLYAESKIAL ETLFSRWHSE SWGNYLTICG
AVIGWTRGTG LMAGNNIVAE GIERYGVRTF SQQEMAFNLL GLMSPSIVNL CQVEPVWADL
NGGFQYLPNL KDLMTDLRKE HTETSEIRKA VTKETSTENK IVNGEKSEAL YQKVTVQPRA
NLKYDFPKVP DWETEVKPLN ENLKGMVDLE KAVVITGFAE VGPWGNARTR WEMEAYGEFS
LEGCVEMAWI MGLIKNHNGM IKGKSYSGWV DAKTGDPVDD KDIKKKYEKF VLEHSGIRLI
EPELFGGYDP NKKQLLQEVQ IDEDLEPFEA SKETAEEFKR EHGDKVEIFE LPDSGEYSVR
VKKGASLLIP KALRFDRLVA GQVPTGWDAR RYGVPEDIIE QVDTVTLFVL VSVSEALLSA
GITDPYEFYK YVHISEVGNC TGSGIGGSGA LRGMYKDRFL DKPLQKDILQ ESFINTMSAW
VNMLLLSSTG PIKSPSGACA TAVESVDIGY ETILEGKARI CLVGGFDDFQ EEGSYEFANM
KATSNAEDEF AHGRTPKEMS RPTTTTRNGF MESQGCGIQV IMDARLALDM GVPIYGILGF
TATATDKIGR SVPAPGQGVL TTAREEVSKF PSPLLDIKYR RRQLEHRRRQ IKQWQESELL
YLQDEVAAMK SQDASFSESE YMTDRLEHIE REAKRQEKAA LCSLGNQFWK QDPRIAPMRG
ALATWGLTID DLDVASCHGT STVANDKNES DVLCQQMKHL GRKKGNAILG IFQKYLTGHP
KGAAGAWMMN GALQVLNSGL VPGNRNADNV DKVLEKFDYM VYPSRSIQTD GVKAVSVTSF
GFGQKGAQAI AIHPKYLFAT LDHAEYANYK TRVESRQKKA YRYFHDGLLN NTMFRAKSKG
PYDEAQQSEV FLNPSARVSV DKKTSNWAYP AKIPAQIPVT KAKTEQTRQM VEHLAKATAG
ENSKVGVDVE NISSIPIDNE TFLERNFTEQ EQAYCKAAPN PAASFAGRWS AKEAVFKSLG
VAGKGAGAAL KEIEVLNDEN GAPVVTLHGD AEAAAKEAGV KSVNVSISHS DDQAIAIAVS
AL
//
