ID C4Y7I2_CLAL4 Unreviewed; 1879 AA.
AC C4Y7I2;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE RecName: Full=Fatty acid synthase subunit alpha {ECO:0000256|PIRNR:PIRNR000454};
DE EC=2.3.1.86 {ECO:0000256|PIRNR:PIRNR000454};
DE Includes:
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase {ECO:0000256|PIRNR:PIRNR000454};
DE EC=1.1.1.100 {ECO:0000256|PIRNR:PIRNR000454};
DE Includes:
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase {ECO:0000256|PIRNR:PIRNR000454};
DE EC=2.3.1.41 {ECO:0000256|PIRNR:PIRNR000454};
GN ORFNames=CLUG_04160 {ECO:0000313|EMBL:EEQ40032.1};
OS Clavispora lusitaniae (strain ATCC 42720) (Yeast) (Candida lusitaniae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Clavispora.
OX NCBI_TaxID=306902 {ECO:0000313|EMBL:EEQ40032.1, ECO:0000313|Proteomes:UP000007703};
RN [1] {ECO:0000313|EMBL:EEQ40032.1, ECO:0000313|Proteomes:UP000007703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42720 {ECO:0000313|EMBL:EEQ40032.1,
RC ECO:0000313|Proteomes:UP000007703};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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 ECO:0000256|PIRNR:PIRNR000454};
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 ECO:0000256|PIRNR:PIRNR000454};
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 ECO:0000256|PIRNR:PIRNR000454};
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; CH408080; EEQ40032.1; -; Genomic_DNA.
DR RefSeq; XP_002615278.1; XM_002615232.1.
DR STRING; 306902.C4Y7I2; -.
DR GeneID; 8495993; -.
DR KEGG; clu:CLUG_04160; -.
DR VEuPathDB; FungiDB:CLUG_04160; -.
DR HOGENOM; CLU_000114_0_0_1; -.
DR InParanoid; C4Y7I2; -.
DR OMA; FPTLPDW; -.
DR OrthoDB; 2783039at2759; -.
DR Proteomes; UP000007703; 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 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:UP000007703};
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 1115..1655
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT REGION 585..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1298
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-1"
FT BINDING 1765..1767
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-2"
FT BINDING 1765
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-3"
FT BINDING 1766
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-3"
FT BINDING 1767
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-3"
FT BINDING 1791
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-2"
FT BINDING 1801
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-2"
FT BINDING 1810..1826
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-2"
FT BINDING 1834..1837
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-2"
FT BINDING 1864..1866
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-2"
FT BINDING 1865
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-3"
FT BINDING 1866
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 1879 AA; 205239 MW; 9A70D33B0058E287 CRC64;
MRPEIEQELS HVLLTELLAY QFASPVRWIE TQDVFLKEHN TERVVEIGPS PTLAGMASRT
IKAKYESYDA ALSLQRQVLC YAKDAKEIYY TPDPADLAPP AKEEPAAAAA PAAAAPAAAA
PVAAAPAAPA AAPAGPAASI SDEPVKASLL LHVLVAQKLK KPLEGVPMSK AIKDLVNGKS
TVQNEILGDL GKEFGSTPDK PEDTPLEELA EQFQDTFNGS LGKTSSSLIG RLMSSKMPGG
FSITVARKYL ETRFGLGSGR QDSVLLMALV NEPPSRLGSD AEAKEFLDSV AQKYASSAGI
SLSSASAGSG GAAAGGAVID SAALDALSAE SKTLARQQLE VLARYLQVDL NKGAKSFIKE
KEASVLLQKE LDLWEAEHGE FYAKGIKPIF SSLKARTYDS YWNWARQDVL SMYFDIIFGK
LTSVDRETIN QCIQIMNRAS PTLIKFMQYH IDHTPEYKGE TYQLARRLGQ QLIDNCKQVM
DVDPVYKDVS RITGPKTTVD SKGNIVYEEA NKESVRKFEQ YVYEMAQGGS MTKQVQPTIQ
EDLSRVYQAI SKQATVSKNT KVELDKLYSQ LVEFLEESKE IETAQATKTA LQHQTSSSST
DEEETSASSD DEIASLPDKT SILQPVSSTI PPQTIPFLNL QKKGKNGWEF DHKLSSMYLD
GLESGAVNGL TFKDKHVLVT GAGAGSIGAE ILQGLISGGA KVVVTTSRFS KKVTEYYQAM
YSRYGAAGST LIVVPFNQGS KQDVDALISY IYDTKEGLGW DLDAIIPFAA IPENGNGLDN
IDSKSELAHR IMLTNLLRML GAVKAKKTTD TRPAQVILPL SPNHGTFGFD GLYSESKISL
ETLFNRWYSE DWSTKLTICG AIIGWTRGTG LMSANNIIAE GIEKVGVRTF SQKEMAFNIL
GLLTPEVVNL CQEQPVMADL NGGLQFIDNL KEFTSKLRSD LVENADVRRA VSIENAIEQK
VVHGDNVDAN YSKVSVQPRA NMTFAFPDMK PYEEIKKISP DMENMLDLES VIVVTGFSEV
GPWGNARTRW EMEAYGEFSL EGCIEMAWIM GLIKYHNGNL KGKPYSGWVD AKTQQPVEDK
DIKAKYEEEI LEHSGIRLIE PELFDGYDPK KKQMIQEVVI QHDLEPFEAS KETAEQYKHQ
HGDKCEIFEI EESGEYTVKI LKGATLFVPK ALRFDRLVAG QIPTGWNAKN YGIPEDTISQ
VDPITLFVLV STVEALLAAG ITDPYEFYKY VHVSEVGNCS GSGMGGVSAL RGMFKDRYSD
RPVQNDILQE SFINTMSAWV NMLLLSSSGP IKTPVGACAT AVESVDTGIE TILSGKAKVC
IVGGYDDFQE EGSYEFANMN ATSNAVDEFA HGRTPSEMSR PATTTRNGFM EAQGSGIQVI
MTADLAIKMG VPIYAVLAMT ATATDKIGRS VPAPGKGILT TAREHHGDLK YPSAMMNVKY
RSRQLKKRLE QIGAWEASEI EYLSEEAELA KEEFGADFSV SEFMRERTEE IRREAKRQAA
DAKKQWGNFF YKNDPRIAPL RGSLAAFGLT IDDLGVASFH GTSTKANDKN ESATINSMMK
HLGRSEGNPV FGVFQKYLTG HPKGAAGAWM LNGAIQILNS GIVPGNRNAD NVDKVMEDFE
YVLYPSRSIQ TDGIKAVSVT SFGFGQKGAQ AVAVHPDYLF AVLDKNSYED YASRVSSRNK
RAYRYMHNAI TRNTMFVAKD KAPYADELEQ PVYLDPLARV EESKTGLVFS KKGVQSNKSY
VSSISDATSK ALSSLNKGSK GVGVDVELLS SLNLDNETFV ERNFTSAEVE YASKSPFPQA
SFTGTWSAKE AVFKALGVKS QGAGASLKDI EIVRDSNGAP KVVLNGSAKE AAAKAGVKNV
SVSISHDDFQ ATAVALSEF
//
