ID G0RLE4_HYPJQ Unreviewed; 1860 AA.
AC G0RLE4;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 76.
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=TRIREDRAFT_48788 {ECO:0000313|EMBL:EGR48038.1};
OS Hypocrea jecorina (strain QM6a) (Trichoderma reesei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=431241 {ECO:0000313|Proteomes:UP000008984};
RN [1] {ECO:0000313|EMBL:EGR48038.1, ECO:0000313|Proteomes:UP000008984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QM6a {ECO:0000313|EMBL:EGR48038.1,
RC ECO:0000313|Proteomes:UP000008984};
RX PubMed=18454138; DOI=10.1038/nbt1403;
RA Martinez D., Berka R.M., Henrissat B., Saloheimo M., Arvas M., Baker S.E.,
RA Chapman J., Chertkov O., Coutinho P.M., Cullen D., Danchin E.G.,
RA Grigoriev I.V., Harris P., Jackson M., Kubicek C.P., Han C.S., Ho I.,
RA Larrondo L.F., de Leon A.L., Magnuson J.K., Merino S., Misra M., Nelson B.,
RA Putnam N., Robbertse B., Salamov A.A., Schmoll M., Terry A., Thayer N.,
RA Westerholm-Parvinen A., Schoch C.L., Yao J., Barabote R., Nelson M.A.,
RA Detter C., Bruce D., Kuske C.R., Xie G., Richardson P., Rokhsar D.S.,
RA Lucas S.M., Rubin E.M., Dunn-Coleman N., Ward M., Brettin T.S.;
RT "Genome sequencing and analysis of the biomass-degrading fungus Trichoderma
RT reesei (syn. Hypocrea jecorina).";
RL Nat. Biotechnol. 26:553-560(2008).
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; GL985066; EGR48038.1; -; Genomic_DNA.
DR RefSeq; XP_006966090.1; XM_006966028.1.
DR STRING; 431241.G0RLE4; -.
DR EnsemblFungi; EGR48038; EGR48038; TRIREDRAFT_48788.
DR GeneID; 18485218; -.
DR KEGG; tre:TRIREDRAFT_48788; -.
DR VEuPathDB; FungiDB:TRIREDRAFT_48788; -.
DR eggNOG; ENOG502QQJX; Eukaryota.
DR HOGENOM; CLU_000114_0_0_1; -.
DR OrthoDB; 2783039at2759; -.
DR Proteomes; UP000008984; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000008984};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000454}.
FT DOMAIN 143..218
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1092..1629
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT ACT_SITE 1275
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-1"
FT BINDING 1746
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-3"
FT BINDING 1747
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-3"
FT BINDING 1748
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-3"
FT BINDING 1846
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-3"
FT BINDING 1847
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-3"
FT MOD_RES 178
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-4"
SQ SEQUENCE 1860 AA; 204153 MW; 1B131F55CBD1096C CRC64;
MRPEVEQELA HTLLVELLAY QFASPVRWIE TQDVFLAERN AERIVEIGPA DTLGVMAKRT
LASKYEAYDA AKSVQRQILC YNKDAKEIYY DVDPVEEEPE PAASSSAAPA APAAAGAPAA
AAPVAAAPAP SAGPAAQVPD QPVQAVDIVH TLVAQKLKKS LAEVPLSKAI KDLVGGKSTL
QNEILGDLGK EFGTTPEKPE DTPLDELSAS MQATFDGNLG KHTQSLIARL ISSKMPGGFN
ITVARKYLET RWGLGPGRQD GVLLLALTME PPARLGNDGD AKAYLDGVTQ KYAATAGISL
TSAAASGGSE GGAGGMMMDP AAIDALTKDQ RALFKQQLEL FARYLKMDLR AGDKAHIESQ
KSEKVLQAQL DLWTAEHGDF YASGIEPVFS ALKARSYDSS WNWARQDALS MYYDIIFGRL
KTVDREIVSQ CIRIMNKSNP KLLEFMQYHI DNCPTERGET YQLAKELGQQ LIENCKEVLN
LPPAYKDVAV PTGPRTTVDA RGNLNYEEVP RASCRKLEHY VQQMAEGGKI SEYGNRTKVQ
NDLQRIYKLI KQQHKMSKTS QLEIKSLYGD VLRSLAMNES QIIPKENGKG RKPGFKGSSP
NKGRVETIPF LHLKRKSLHG WDYSKKLTAV YLNCLEEAAK DGVTFQDKYV LMTGAGAGSI
GAEVLQGLIS GGAKVVVTTS RFSRQVTEYY QSMYSRFGSR GSQIVVVPFN QGSKQDVEAL
VNYIYDTKNG LGWDLDYIVP FAAIPENGRQ IDNIDSKSEL AHRIMLTNLI RMLGCVKTQK
AERGFETRPA QVVLPLSPNH GTFGNDGLYS ESKLALETLF NRWHSEDWGH YLTICGAVIG
WTRGTGLMSG NNVVAEGVEA FGVRTFSQQE MAFNLLGLMS ATIVDLCQSE PVFADLNGGL
QFIPNLNESM TKLRKDIMET SEIRRAVSKE SAIENTIVNG ADSEVLYKKK TIEPRANIKC
DFPHLPDWKT EVAPLNEQLK GMVDLDKVVV VTGFAEVGPW GNSRTRWEME AYGEFSLEGC
IEMAWIMGLI KNHNGPLKGK PYAGWVDAKT GEPVDDKDVK QKYEKHILEH SGIRLIEPEL
FDGYDPNKKQ LLHEVVIQED LEPFEASKET AEEFRREHGD KVEIFEIPES GEYIIRVKKG
ASLWIPKALR FDRLVAGQIP TGWDPKRYGI PEDIISQVDP VTLFLLVSVA EALLSSGITD
PYEFYKYVHV SEVGNIVGSG MGGAKALRGM HKARYLDKPL QNDILQESFI NTMSAWVNML
LLSSSGPIKT PVGACATAIE SVDIGVETIL EGKARICLVG GFDDFGEEGS YEFANMKATS
NSLDEFAHGR TPAEMSRPTT TTRNGFMESQ GCGVQVIMTA QLALDMGVPI HGILAFTTTA
SDKIGRSVPA PGQGVLTSAR EHPGKFPSPL LDINYRRRQI ERRKKQIKQW EESELEFLHD
EIDAMKAQGG VFDEKEYAQE RILHIQKEAI RQEKELLRSM GNNFWKNDPS IAPLRGALAT
WGLTIDDLKV ASFHGTSTGA NDKNESSAIC QQLRHLGRSK GNAILGVFQK YLTGHPKGAA
GAWMMNGGLQ ILNTGLVPGN RNADNIDPIM ENYDLIVYPS RSIQTDGVKA FSLTSFGFGQ
KGAQAVAVHP KYLFATLDEK TYDAYRAKVE SRQKKAYRFF HNGMINNALF VSKANPPYTD
DQLSAVLMNP DARVVEDKKT AELKFPPNFM KASEKTVSPT VAKETQQVIE ALAHKVAGKN
SNVGVDVEDI ASFNIDNDTF IERNFTSQEV AYCKSAPSPQ SSFAGRWSAK EAVFKALGVA
SKGAGAALKD IEILKDDTGA PVVSLHGDAA AAAKQAGVKE VSVSISHADK QAVAVAVAHF
//
