ID F0X8I8_GROCL Unreviewed; 1863 AA.
AC F0X8I8;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 75.
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=CMQ_4162 {ECO:0000313|EMBL:EFX06093.1};
OS Grosmannia clavigera (strain kw1407 / UAMH 11150) (Blue stain fungus)
OS (Graphiocladiella clavigera).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Leptographium.
OX NCBI_TaxID=655863 {ECO:0000313|Proteomes:UP000007796};
RN [1] {ECO:0000313|EMBL:EFX06093.1, ECO:0000313|Proteomes:UP000007796}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=kw1407 / UAMH 11150 {ECO:0000313|Proteomes:UP000007796};
RX PubMed=21262841; DOI=10.1073/pnas.1011289108;
RA DiGuistini S., Wang Y., Liao N.Y., Taylor G., Tanguay P., Feau N.,
RA Henrissat B., Chan S.K., Hesse-Orce U., Alamouti S.M., Tsui C.K.M.,
RA Docking R.T., Levasseur A., Haridas S., Robertson G., Birol I., Holt R.A.,
RA Marra M.A., Hamelin R.C., Hirst M., Jones S.J.M., Bohlmann J., Breuil C.;
RT "Genome and transcriptome analyses of the mountain pine beetle-fungal
RT symbiont Grosmannia clavigera, a lodgepole pine pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:2504-2509(2011).
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; GL629735; EFX06093.1; -; Genomic_DNA.
DR RefSeq; XP_014175575.1; XM_014320100.1.
DR STRING; 655863.F0X8I8; -.
DR GeneID; 25977343; -.
DR eggNOG; ENOG502QQJX; Eukaryota.
DR HOGENOM; CLU_000114_0_0_1; -.
DR InParanoid; F0X8I8; -.
DR OrthoDB; 2783039at2759; -.
DR Proteomes; UP000007796; 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 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:UP000007796};
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 1087..1627
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT ACT_SITE 1273
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 1750
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-3"
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 178
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-4"
SQ SEQUENCE 1863 AA; 203715 MW; 36C3E8FEAB993022 CRC64;
MRPEVEQELA HTLLVELLAY QFASPVRWIE TQDVFLAEKT AERIVEIGPA DTLGVMAKRT
LASKYEAYDA AKSVQRQILC YNKDAKEIYY DVDPVEDEPE PTPEASSSAA APASAASTAA
AAVAVAAPPA GAGPAAQVPD APVQALDIVR SLIAQKLKKP LSEIPLSKAI KDLVGGKSTL
QNEILGDLGK EFGSTPEKPE DTPLDELGAA MQATFNGSLG KHSQSLIARL ISSKMPGGFN
ITAARKYLET RWGLASGRQD GVLLLAITME PPARLGSEAD GKAYLDDVSQ KYASNAGISL
STAASAGPAA GGGGGMMMDP AAIDALTKDQ RALFKQQLEL LARYLKMDLR AGDKAFQTSQ
ESSKVLQSQI DLWAAEHGDF YAAGIEPVFS PLKARVYDSS WNWARQDALS MFYDIIFGRL
QTVDREIVSQ CIRIMNRSNP TLLEFMQYHI DNCPTERGET YKLAKELGAM LIDNCKDVLN
VAPVYKDVAI PTGPRTIIDA RGNLKYEEVP RASCRKLEHY VQQMAAGGKI TEYGTRAKVQ
TGLSRLYKLM KQQHKISKTS QLEFKNLYGE LLRSLEMNES QIISANGAAK KPLTSKGTPK
AKVETIPFLH IRSQASSGWE YNKKFTGLYL DCLREAAASG VSFQGRYALM TGAGAGSIGA
DVLQGLISGG AHVVVTTSRY SREVTEYYQA MYARYGSRES QLVVVPFNQG SKQDVEALVQ
YIYDPKNGLG WDLDFIVPFA AISENGRQID SIDSKSELAH RIMLTNLIRL LGAVKTEKAN
RGFITRPAQV ILPLSPNHGT FGSDGLYSES KLGLETLFNR WHAEDWADYL SVCGAVIGWT
RGTGLMSANN IVAEGVERFG VHTFSQQEMA FNLLSLLSPT IVDLCQNEPV MADLNGGLQF
IPNLNNVMTR LRKEITETSE IRKEVTKETA IESKVVNGEN YETLYKKKTI EPRANMQFEF
PNLPDWKEEI APLNENLKGM VDLDKVVVVT GFAEVGPWGN SRTRWEMEAH GEFSLEGCIE
MAWIMGLIHN HNGPIKGKPY SGWVDAKSGD PVDDKDVKAK YEKHILEHSG IRLIEPELFD
GYDPNQKQLL HEVVIDEDLE PFESSKETAE EFKREHGDKV EIFEIPESGQ YTVRMKKGAA
LWIPKALRFD RLVAGQIPTG WDAKRYGVPE DIISQVDPVA LFVLVSVAEA LLSSGVTDPY
EFYKYVHVSE VGNCMGSGMG GATALRGMHK ARFLDKPLQN DILQESFINT MSAWVNMLLL
SSSGPIKTPV GACATAVESV DIGYETIMEG KARICLVGGF DDFGEEGSYE FANMKATSNA
VDEFAHGRTP KEMSRPATTT RNGFMESQGS GVQVIMTARL ALEMGVPIYG VLALTTTASD
KIGRSVPAPG MGVLTTAREN AGRFTSPLLD IKYRRRQMEL RKRQVRQWHE AELEYLADEV
AAIKAQGEPF NEKEYVADRA SHIEKEAVRQ EKEVLRSLGN NFWKSDPSIA PLRGALATWG
LTIDDLDVAS FHGTSTKAND KNESSVICKQ LAHLGRTKGN AVLGIFQKYL TGHPKGAAGA
WMMNGCLQVL NTGLVPGNRN ADNVDQVMEQ FDYIVYPSRS LQTDGIKAFS VTSFGFGQKG
AQAIGIHPRY LYATLDEATF DGYRAKVAAR QKKAYRFFHN GMINNSLFVA KTHAPYSDEQ
LPSVLLNPDA RVTVDKKTAE LTFAANFMQQ AAKATLPTAG GAAAKTTLEA LEALAAQVQT
RKNKVGVDLE DVAAIHINND TFVERNFTAA EIAYCNSTPN VQAAFAGRWS AKEAVFKSLG
VASRGGGAPL KEIEILRDDK GAPTVHLHGQ AATAAKAANL KEVNVSISHS DSQAVAIAVS
TFE
//
