ID G0S866_CHATD Unreviewed; 1865 AA.
AC G0S866;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 74.
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=CTHT_0037740 {ECO:0000313|EMBL:EGS21900.1};
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
OS (Thermochaetoides thermophila).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides.
OX NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN [1] {ECO:0000313|EMBL:EGS21900.1, ECO:0000313|Proteomes:UP000008066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC {ECO:0000313|Proteomes:UP000008066};
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
RN [2] {ECO:0007829|PDB:7Q5S}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.47 ANGSTROMS).
RX PubMed=35093201; DOI=10.1016/j.str.2022.01.001;
RA Skalidis I., Kyrilis F.L., Tuting C., Hamdi F., Chojnowski G.,
RA Kastritis P.L.;
RT "Cryo-EM and artificial intelligence visualize endogenous protein community
RT members.";
RL Structure 30:575-589.e6(2022).
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}.
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DR EMBL; GL988041; EGS21900.1; -; Genomic_DNA.
DR RefSeq; XP_006694196.1; XM_006694133.1.
DR PDB; 7Q5S; EM; 4.47 A; A/D/F/H/J/L=1-1865.
DR SMR; G0S866; -.
DR STRING; 759272.G0S866; -.
DR GeneID; 18257812; -.
DR KEGG; cthr:CTHT_0037740; -.
DR eggNOG; ENOG502QQJX; Eukaryota.
DR HOGENOM; CLU_000114_0_0_1; -.
DR OMA; FPTLPDW; -.
DR OrthoDB; 2783039at2759; -.
DR Proteomes; UP000008066; 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; 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 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:7Q5S};
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:UP000008066};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000454}.
FT DOMAIN 145..220
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1092..1630
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT REGION 99..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..138
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1275
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-1"
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 1851
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-3"
FT MOD_RES 180
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-4"
SQ SEQUENCE 1865 AA; 204830 MW; 86A1C4E7BD8F36ED CRC64;
MRPEVEQELA HTLLVELLAY QFASPVRWIE TQDVFLAEQM AERIVEIGPA DTLSVMAKRT
LASKYEAYDA AKSAQRQILC YSKDAKEIYY DVDPIEEEPE PAPAQAATPT APAAPAATPA
AAPAPVAAPP PPGVGPAAQV PDAPVTALEI VRALIAQKLK KPYQEVPLSK AIKDLVGGKS
TLQNEILGDL GKEFGSTPEK PEDTPLDELG AAMQATFDGN LGKTSQGLIA RLISSKMPGG
FNITTARKYL ETRWGLGPGR QDGVLLLAIT MEPPSRLGSE ADAKAFLDDV SQKYAANAGI
SLSTAAAAGP AAGAGGGMLM DPAALEALTS DQKALFKQQL ELIARYLKLD IRAGDKAYQA
SQESAKVLQS QLDLWLAEHG DFYASGIEPV FSPLKARVYD SSWNWARQDA LSMYYDIIFG
RLKTVDREIV SQCIRIMNRA NPTLLEFMQY HIDNCPTDRG ETYQLAKELG AQLIENCKEV
LNANPVYKDV AIPTGPKTTI DARGNLKYEE VPRPSCRKLE HYVQQMAAGG KISEYGNRIK
VQNDLAKIYK LIKQQHKLPK TSQLEIKALY SDIIRALQMN ENQILGQTNG KSLGLPKKGK
PKAKTETIPF LHLRKKSVMG WEYNKKLTSL YLDCLEKAAR DGLTFAGKYA LMTGAGAGSI
GAEVLQGLIS GGAHVIVTTS RYSREVTEYY QSMYSRYGAR GSQLVVVPFN QGSVQDVNAL
VEYIYDTKNG LGWDLDYIVP FAAISEQGRQ IDGIDSKSEL AHRIMLTNLI RLLGAVKTQK
ASRGYETRPA QVILPLSPNH GTFGSDGLYS ESKLGLETLF NRWESENWSN YLTICGAIIG
WTRGTGLMSG NNIVAEAVEK FGVRTFSQQE MAFNLLGLMA PTIVDLCQNE PVCADLNGGL
QFIPNLNELM TRERKNLTET SEIRQAVTKE TAAENKVVNG EASEALYKKK IIERRANIKF
DFPPLPDWKK DIQPLNDKLK GMVDLEKVIV VTGFAEVGPW GNSRTRWEME AYGEFSLEGC
IEMAWIMGLI KNYNGLIKGK PYSGWVDAKT GEPVDDKDVK PKYEKYILEH SGIRLIEPEL
FGGYDPNKKQ LLHEVVIQED LDPFQCSAET AEQFKREHGD KVEIFEIPES GEYTVRFKKG
ATLWIPKALR FDRLVAGQIP TGWDAKRYGI PDDIIQQVDP VCLFVLVSTV EALLSSGITD
PYEFYKYVHV SELGNCIGSG MGGATALRGM HRDRFLDKPL QNDILQESFI NTMSAWVNML
LLSSSGPIKT PVAACATAVE SVDVGVETIL EGKARICLVG GFDDFGEEGS YEFANMKATS
NAVDEFAHGR TPQEMSRPTT TTRNGFMESQ GSGVQVIMTA KLALEMGVPI YGILALTTTA
SDKIGRSVPA PGQGVLTTAR EHRGKFPSPL LDINYRRRQI ERRTKQVMEE KEAEFEYLAA
EIEALKAEGR PQSEIEEYAA HRAAHIEKTA EKQAKEILRS FGNFFWKNDP TIAPLRGALA
VWGLTIDDLD VASFHGTSTK ANDKNESSVI CQQLAHLGRK KGNAVLGIFQ KYLTGHPKGA
AGAWMLNGCL QVLNTGLVPG NRNADNVDKV MEQFDYIVYP NRSIQTDGIK AFSVTSFGFG
QKGAQCIGVH PKYLYATLDE QTYNEYCTKV QARQKKAYRY FHNGLINNTL FQAKEKAPYT
DEQLSAVLLN PDARVVEDKK TGQLIFPPNF MKLSEKTQAA AQPKVSLESV LSREARRLES
VNTRVGVDVE DISAINTDND TFLDRNFTEA EQKYCLASKS GRSPQKAFAG RWTAKEAVFK
ALGVSSKGAG AALKDIEILV DENGAPTVSL HGAAAEAAKK AGIKSVSVSI SYTDSQAAAI
ATAQL
//
