ID N1JIC5_BLUG1 Unreviewed; 1864 AA.
AC N1JIC5;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 61.
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=BGHDH14_bgh06789 {ECO:0000313|EMBL:CCU77621.1};
OS Blumeria graminis f. sp. hordei (strain DH14) (Barley powdery mildew)
OS (Oidium monilioides f. sp. hordei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Blumeria; Blumeria hordei.
OX NCBI_TaxID=546991 {ECO:0000313|EMBL:CCU77621.1, ECO:0000313|Proteomes:UP000015441};
RN [1] {ECO:0000313|EMBL:CCU77621.1, ECO:0000313|Proteomes:UP000015441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DH14 {ECO:0000313|EMBL:CCU77621.1};
RX PubMed=21148392; DOI=10.1126/science.1194573;
RA Spanu P.D., Abbott J.C., Amselem J., Burgis T.A., Soanes D.M., Stueber K.,
RA Ver Loren van Themaat E., Brown J.K.M., Butcher S.A., Gurr S.J.,
RA Lebrun M.-H., Ridout C.J., Schulze-Lefert P., Talbot N.J., Ahmadinejad N.,
RA Ametz C., Barton G.R., Benjdia M., Bidzinski P., Bindschedler L.V.,
RA Both M., Brewer M.T., Cadle-Davidson L., Cadle-Davidson M.M., Collemare J.,
RA Cramer R., Frenkel O., Godfrey D., Harriman J., Hoede C., King B.C.,
RA Klages S., Kleemann J., Knoll D., Koti P.S., Kreplak J., Lopez-Ruiz F.J.,
RA Lu X., Maekawa T., Mahanil S., Micali C., Milgroom M.G., Montana G.,
RA Noir S., O'Connell R.J., Oberhaensli S., Parlange F., Pedersen C.,
RA Quesneville H., Reinhardt R., Rott M., Sacristan S., Schmidt S.M.,
RA Schoen M., Skamnioti P., Sommer H., Stephens A., Takahara H.,
RA Thordal-Christensen H., Vigouroux M., Wessling R., Wicker T., Panstruga R.;
RT "Genome expansion and gene loss in powdery mildew fungi reveal tradeoffs in
RT extreme parasitism.";
RL Science 330:1543-1546(2010).
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 -!- 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:CCU77621.1}.
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DR EMBL; CAUH01003844; CCU77621.1; -; Genomic_DNA.
DR STRING; 546991.N1JIC5; -.
DR EnsemblFungi; BLGH_05333-mRNA-1; BLGH_05333-mRNA-1; BLGH_05333.
DR eggNOG; ENOG502QQJX; Eukaryota.
DR HOGENOM; CLU_000114_0_0_1; -.
DR InParanoid; N1JIC5; -.
DR OrthoDB; 2783039at2759; -.
DR Proteomes; UP000015441; Unassembled WGS sequence.
DR GO; GO:0005835; C:fatty acid synthase complex; IEA:EnsemblFungi.
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:EnsemblFungi.
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:0101026; P:mitotic nuclear membrane biogenesis; IEA:EnsemblFungi.
DR GO; GO:1900535; P:palmitic acid biosynthetic process; IEA:EnsemblFungi.
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; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000015441};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000454}.
FT DOMAIN 147..222
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1099..1635
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT REGION 115..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1281
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-1"
FT BINDING 1750..1752
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-2"
FT BINDING 1750
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-3"
FT BINDING 1751
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-3"
FT BINDING 1752
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-3"
FT BINDING 1776
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-2"
FT BINDING 1786
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-2"
FT BINDING 1795..1811
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-2"
FT BINDING 1819..1822
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-2"
FT BINDING 1849..1851
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-2"
FT BINDING 1850
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-3"
FT BINDING 1851
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-3"
FT MOD_RES 182
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-4"
SQ SEQUENCE 1864 AA; 205692 MW; D36A9BA9C655C1D1 CRC64;
MRPEIEQELA HTLLVELLAY QFASPVRWIE TQDVILAEKT TERIVEIGPA DTLGVMAKRT
LSSKYETYDA AKSVQRQILC YNKDAKEIYY DVDPVDNEEQ STDTALAPST IVQKTTSANP
VPPTVSNPSL SPASNAGPAA QVPDAPVGAL DIVRSLIAQK LKKPLLDIPL NKAIKDLVGG
KSTLQNEILG DLGKEFGSTP EKPEDTPLDE LSASMQATFD GQLGKQSSSL IARLISSKMP
GGFNLTSARK YLESRWGLSS GRQDGVLLLA ITMEPTARLS AESEAKSFLD DVALKYASNA
GIDITTPASG GDSGPGGAGM MIDPAALDAL TKDQRALFKQ QLELYARYLK IDLRAGEKAF
IGTQNSTAAL QAQLDLWNVE HGDIYASGIE PVFSPLKART YDSSWNWVRQ DALSMYYDII
FGRLKAVDRE IVSQCIRIMN RSNPILLEFM QYHIDNCPTE RGETYQLAKE LGQQLIDNCK
DVLETAPSYK DVSLPTGPHT TIDGRGKLSY TEIPRNSVRK LEHYVREMAD GGKISEYGNR
TKVQSDLTRI YKLIQQQHKL SKSSHLQIKQ LYGDVIRSLA MSEGQIIPKE NGSAYSNSTF
QKTSRNKLGK VETIPFLHLK RKNQHGWEYS KKLTGLYLDV LSQTAKLGVT FQGKNALMTG
AGAGSIGAEV LQGLISGGAK VIVTTSRFSR EVTEYYQSMY ARYGSKGSQL IVVPFNQGSK
QDVQALIDYI YDTKSGLGWD LDFVIPFAAI PENGREIDNI DSKSELAHRI MLTNLLRLLG
CVKAQKQSRG FETRPAQVVL PLSPNHGTFG NDGLYSESKL ALETLFNRWH SESWGNFLTI
CGAVIGWTRG TGLMSGNNIV AEGVEAYGVR TFSQQEMAFN LLGLMSPNIV DLCQSEPVFA
DLNGGLQFIP DLKDLMSKLR KDIMETSEVR QAVTKETSIE NKIVNGEDSE ALYKKVMIEP
RANIKFDFPH LPDWEKDIAP LNDNLKGMVD LEKVVVVTGF AELGPWGNSR TRWEMEAYGQ
FSLEGCVEMA WVMGLIKNFN GSIKGKQYSG WVDAKTGEPV EDKDVKSKYE KYILEHSGIR
LIEPELFRGY DPNKKQLLQE VVIQEDLEPF EASKETAEEF KREHGDQAEI FEIAETGEYI
VRMKKGATLL IPKALKFDRL VAGQIPTGWN AKQYGIPDDI ISQVDPVTLF VLVCTVESLL
ASGITDPYEF YKYVHLSEVG NCIGSGIGGT SALKGMYKDR YLDRPLQKDI LQESFINTMS
AWVNMLLISS TGPIKTPVGA CATAVESVDI GYETILEGKA RVCFVGGFDD FQEEGSYEFA
NMKATSNAVD EFAHGRTPKE MSRPTTTTRN GFMESQGCGI QVIMTAKLAL DMGVPIYGIL
GLTTTATDKI GRSVPAPGKG VLTTARENPG KFPSPLLDIK YRRRQIELRK KNIKHWQESE
LAYLHEEIEA MKSQGHSFNQ DEYAQERALH IEREANRQER EVLNSLGNNF WKNDPKIAPL
RGALATWGLT IDDLDVASFH GTSTVANDKN ESSVICSQLK HLGRKKGNAV LGIFQKYLTG
HPKGAAGAWM MNGCLQVLNS GLVPGNRNAD NVDSVMEQFD YIVYPSRSLQ TDGIKAFSVT
SFGFGQKGAQ AIGIHPRYLF ATLDEATYKS YSAKVQARQK KAYRYFHNGM INNCLFVAKD
KSPYTDDQEC AVFLNPDARV TPDPKSSLLT YASNFSKNTG PTASKKECTK QLVESLAKGA
ASPNNRVGVD VEEISSFNIE NETFLERNFS EKERTYCSRA PHPRSSYAGK WSAKEAVFKS
LGVRSKGAGA PLKDIEITND EKGAPIATLH GEAAKSAKIA GVREISISIS HSETQAIAIA
VATF
//
