ID B0D9Q1_LACBS Unreviewed; 3935 AA.
AC B0D9Q1;
DT 26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2008, sequence version 1.
DT 24-JAN-2024, entry version 105.
DE RecName: Full=Fatty acid synthase subunit alpha {ECO:0000256|ARBA:ARBA00014008};
DE EC=1.1.1.100 {ECO:0000256|ARBA:ARBA00012948};
DE EC=2.3.1.86 {ECO:0000256|ARBA:ARBA00012878};
GN Name=FAS-2 {ECO:0000313|EMBL:EDR08619.1};
GN ORFNames=LACBIDRAFT_296983 {ECO:0000313|EMBL:EDR08619.1};
OS Laccaria bicolor (strain S238N-H82 / ATCC MYA-4686) (Bicoloured deceiver)
OS (Laccaria laccata var. bicolor).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Hydnangiaceae; Laccaria.
OX NCBI_TaxID=486041 {ECO:0000313|Proteomes:UP000001194};
RN [1] {ECO:0000313|EMBL:EDR08619.1, ECO:0000313|Proteomes:UP000001194}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 / ATCC MYA-4686 {ECO:0000313|Proteomes:UP000001194};
RX PubMed=18322534; DOI=10.1038/nature06556;
RA Martin F., Aerts A., Ahren D., Brun A., Danchin E.G.J., Duchaussoy F.,
RA Gibon J., Kohler A., Lindquist E., Pereda V., Salamov A., Shapiro H.J.,
RA Wuyts J., Blaudez D., Buee M., Brokstein P., Canbaeck B., Cohen D.,
RA Courty P.E., Coutinho P.M., Delaruelle C., Detter J.C., Deveau A.,
RA DiFazio S., Duplessis S., Fraissinet-Tachet L., Lucic E., Frey-Klett P.,
RA Fourrey C., Feussner I., Gay G., Grimwood J., Hoegger P.J., Jain P.,
RA Kilaru S., Labbe J., Lin Y.C., Legue V., Le Tacon F., Marmeisse R.,
RA Melayah D., Montanini B., Muratet M., Nehls U., Niculita-Hirzel H.,
RA Oudot-Le Secq M.P., Peter M., Quesneville H., Rajashekar B., Reich M.,
RA Rouhier N., Schmutz J., Yin T., Chalot M., Henrissat B., Kuees U.,
RA Lucas S., Van de Peer Y., Podila G.K., Polle A., Pukkila P.J.,
RA Richardson P.M., Rouze P., Sanders I.R., Stajich J.E., Tunlid A.,
RA Tuskan G., Grigoriev I.V.;
RT "The genome of Laccaria bicolor provides insights into mycorrhizal
RT symbiosis.";
RL Nature 452:88-92(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 -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000256|ARBA:ARBA00005005}.
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DR EMBL; DS547101; EDR08619.1; -; Genomic_DNA.
DR RefSeq; XP_001880844.1; XM_001880809.1.
DR STRING; 486041.B0D9Q1; -.
DR GeneID; 6076402; -.
DR KEGG; lbc:LACBIDRAFT_296983; -.
DR HOGENOM; CLU_000114_2_0_1; -.
DR InParanoid; B0D9Q1; -.
DR OrthoDB; 5488314at2759; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000001194; Unassembled WGS sequence.
DR GO; GO:0005835; C:fatty acid synthase complex; IEA:InterPro.
DR GO; GO:0008659; F:(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0004317; F:(3R)-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity; 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:0004313; F:[acyl-carrier-protein] S-acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016297; F:acyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) 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:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00828; elong_cond_enzymes; 1.
DR CDD; cd03447; FAS_MaoC; 1.
DR CDD; cd08950; KR_fFAS_SDR_c_like; 1.
DR Gene3D; 1.20.1050.120; -; 1.
DR Gene3D; 1.20.930.70; -; 1.
DR Gene3D; 3.30.1120.100; -; 1.
DR Gene3D; 3.30.70.2490; -; 1.
DR Gene3D; 3.30.70.3330; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.90.25.70; -; 1.
DR Gene3D; 6.10.140.1400; -; 1.
DR Gene3D; 6.10.140.1410; -; 1.
DR Gene3D; 6.10.250.1930; -; 1.
DR Gene3D; 6.10.60.10; -; 1.
DR Gene3D; 6.20.240.10; -; 1.
DR Gene3D; 3.90.470.20; 4'-phosphopantetheinyl transferase domain; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.10.129.10; Hotdog Thioesterase; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 3.
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; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR002582; ACPS.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR013565; Fas1/AflB-like_central.
DR InterPro; IPR041099; FAS1_N.
DR InterPro; IPR040899; Fas_alpha_ACP.
DR InterPro; IPR047224; FAS_alpha_su_C.
DR InterPro; IPR040883; FAS_meander.
DR InterPro; IPR041550; FASI_helical.
DR InterPro; IPR003965; Fatty_acid_synthase.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR039569; MaoC-like_dehydrat_N.
DR InterPro; IPR002539; MaoC-like_dom.
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; IPR032088; SAT.
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; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00106; adh_short; 1.
DR Pfam; PF08354; Fas1-AflB-like_hel; 1.
DR Pfam; PF18325; Fas_alpha_ACP; 1.
DR Pfam; PF18314; FAS_I_H; 1.
DR Pfam; PF17951; FAS_meander; 1.
DR Pfam; PF17828; FAS_N; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF13452; MaoC_dehydrat_N; 1.
DR Pfam; PF01575; MaoC_dehydratas; 1.
DR Pfam; PF16073; SAT; 1.
DR PRINTS; PR01483; FASYNTHASE.
DR SMART; SM00827; PKS_AT; 1.
DR SUPFAM; SSF56214; 4'-phosphopantetheinyl transferase; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 2.
DR SUPFAM; SSF51412; Inosine monophosphate dehydrogenase (IMPDH); 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 2.
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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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 Reference proteome {ECO:0000313|Proteomes:UP000001194};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 2222..2297
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 3174..3708
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT REGION 2656..2675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3935 AA; 431518 MW; 0BC20AD0B87CF857 CRC64;
MAVANGSAIH ANGIATRPLI LSLGQIRVSI PVSTQSNEWI AAEVLREEFI HKQSLLDAVD
TTAQLDNEQD AAVELSALFL GHVAASLHED PQSASARTAL LLNLLKHFTS SYLATKDIHS
LTASYDTETR KAVISAYVSA VAALQQRDIP FPRQPESALL NAASSNKASI FALFGGQGTN
EVYFDELQSL YDVYKPFVAS FFKTVTEDVL VPLATEHEAF SFYTFGLDVV SWLSGETSRP
SVAYLASVPV SLPLIGLTQL VQYLVVCRVS GLSPGEFRSR IAGATGHSQG IVAAVAVAAS
GTFEEFTNNS VKALKWLFFC GLRGQHAFPV TSVEPSIVQD ATEGGEGTPS PMLSVTGLGL
KELQPHITKT NKHLPENSQL FVSLHNGPKA FVVTGPPKAL FGLVTSLRKV KAPSGLDQSK
TPFSQRKPVF SIRFLVVGVP YHSDYLKGAT EKLLLEDLGG KELWEAKDLK ISVFNTEDGS
DLRNLSSSIT RSLCEQIFTS PIHWTKATNF PETATHAIDF GPGGTSGIGP LTARNFNGRG
VRVILAGVKG KGDAELFDAA DVKYEEWWSK KWSPSLVRTS DGTLHLDTPF SRLLGKPPIM
VAGMTPSTVK AGFVSAVLDA GYHIELAGGG HYNAAALRSK VAEIQKQIPA GVGITLNALY
INPRQFTFQF PLWQEMRKEG LPVEGFCVAA GIPTTEKAVE IIEGLRSAGI KHVAFKPGSV
DGIRQVVNIA AANPDFPIIL QWTGGRAGGH HSYEDFHQPV LSTYRSIRAH ANICLVGGSG
FGSADDVWEY LTGDWSVERF GLQPMPFDGF LFASRVMVAK EAHTSSSVKD LIVAASGVDD
GAWEGTYAKP TGGILTVRSE LGEPIHKVAT RGVKLWKEFD DTVFKLPKEK RVAWLKERRD
EVIGKLNKDF SKPWFGWKKD GNIATDLGDM TYEETVLRMV RLMFVAHQKR WVDVSLRNLT
GDWLRRVEER FAGVNGSGTK ASILQSYTLL DDPLPFADSF FKKYPLAAEQ LLSAEDTAFF
LAISQRPGQK PVPFIPVLDA SFEVWFKKDS LWAAEDIEAV FDQDPQRVCI LQGPVAAKWS
VVKDEPVKEL LGNINSSLIQ RLLERKYGGD ASKVPTIDYL AVKPTAVPSD LAGVQRTEVD
EEVTFQFGSI LPEASAWLEV LGGPELNWLR ALTTSTTIVQ GVSYIDNPLR RILAPRPGQK
VVVNYDGAVP YSVTVYGAAR SYGQHVVDFK ALEIEYDDES NQIDVTLYEE RKGVSVPLSL
HFEYKPSQGF APIHELSDGR NKRIKEFYWK LWYGDDATLP KIDIHEAFVG PEITIEAKDV
EQFCAVVGNQ GESFKTVRNE NVQAPMDFAI VTGWKAIMKS IFPAAIDGDL LKLVHLSNGF
RMVDGAKPLQ VGDVCKAEAR IVSVINANEG KIVKVKGHVY REGKKVIEVV SSFLYRGRFN
DYENTFDTTE EPDYMVPLET DAEVGVLQSK EWFEWENESS PLLAGTSLIF RIQSKVFFKD
RTAYRNVSVS GDIFVRNQLK VLVKVGSVDF QQDDSQGNPV LAYLQRHGSP QGLMVPLAND
GYTLTNADSS TTFSAPLTNE PYSKISGDFN PIHINPYFSD FASLPATITH GLWSSAATRR
YVENVVAKGH PDRVIAYNVN FVGMVLPGDE ITVKLRHTGM LAGNIVVSVE TSNSRGEKVL
QGTAEVAQPT TVYVFTGQGS QEPGMGMDLY NSSPAARAVW EGADAHLLAV YGFSIVEIVK
DNPKEKTIHF GGIKGQAIRQ RYMDMTYDTT DKDGHVKTLP LFADIDVRTP KYTFSHPNGL
LFATQFAQIA LVVTEKAAFE DMRMKGFVQK DCAFAGHSLG EYSALASIAD VLHISALVDV
VFYRGITMQR AVERDSENRS NYAMCAVNPS RISPSFSDAA LREVVESIAT LTGSLLEIVN
YNVEGQQYVC AGELIALQTM TNVLNFIKVQ KIDIAKLTET YTVEKVKEIL GDIVKSCYEK
AQEQQKAEGY IKLERGFATI PLPGIDVPFH SRYLWAGVLP FRAYLSKKIN ANQLNPDMLV
GKYIPNLIAK PFDVSREYAQ IIYDQTSSPR LDKVLRKWEQ DNWASPDNRQ KLAYIILVEL
LAYQFASPVR WIETQDLLFT KFAFERLVEL GPSPTLTGMA SRTLKAKYET ADGSISRSRA
ILCHAKNVKE IYYQFEDELE AETPAAEAPS SEASATPAAV SVAAPPPVAS SGPVASIEDV
PVKAIEILLV IVAQKLKKRV DEVPLTKSIK DLVGGKSTLQ NEILGDLQQE FSSAPEKGEE
LPLEELGSAL GTGFSGSLGK YTTGLVSRVI GGKMPGGFNS SAIKAYLAKS WGLGPSRSDS
VLLLATTLEP PKRLTSEPEA KAWLDGVVSV YAQRSGISLS APGAGGAAGG AAGGATINSE
EFLKFQADQE KFAAQHVELY MRYLNRDSRA GEIVFDQEKA NNVTLQAKLD SITREHGDTY
IDGIQPRFDP LKARHFDSSW NWVRQDALLM WFDMIFGRLT TVDREITARC ISLLNRADPA
MLQYMQYNVD RCDPSKGETY KLAKEFGQQL INNTREVIGK PPVYKDVTFP TAPHTEVTEK
GEIVYSEVVR ENVRKLEAYV EEMASGDTVS GAVNIQKVQD DVVKLWTVVK SLPEISVDQK
NRIKALYEGV VRSLHKGPES RPRSVTRSRR SSSQFLRPQV TGVPAVTSLA SDKIPLLHLK
RRVGSTWEYS SNLTGVYLDI LHEIATSGTT FKDKNALLTG VGKGSIGIEI VKGLLAGGAH
VVITTSSYNR KTVEYYQSIF QSVGSRGSAL TVVPFNQASK QDVEALVDYI YANLGMDLDY
ILPFAGIPEN GREIDGLDDR SELAHRMMLV NLLRILGAVK NKKASRHFVT RPTQVILPLS
PNHGLFGNDG LYSESKISLE TLFQRWASES WGEYLCLAGA VIGWTRGTGL MGPTNIVAHE
LESYGVRTFS SKEMAFNILG LMHPLLFSIT QVEPIWADLN GGMDRLPDLA DITSRIRTKL
NKKADLRRAV ARDNAADFKV INGTEAERLI QTIDVLPRAN FRFEFPSLES ASSLNELSHL
RGLIDLEKVV VITGFAEVGP WGSARTRWEM EARGEFTIEG CIEMAWMTGH IKHFDGRLKD
GSLYVGWVDT KTNEPIDDKD VKGRYEKDIL AHAGVRLIEP ELFRGYDPTK KVFNQEVELT
HDLEAIEVSD SEAQKFKLQH GDKCDVWAGE SGQWFAKFKK GACVFVPKAF KFSRTVAGQI
PTGWDAGRYG IPEDIIAQTD RATLWALVCT AEALASSGIT DPYELYKHMH PSDVGTSLGS
GMGGVSSMAK MFKDRRDERE VQNDILQETF INTTAGWINL LLLSSSGPVK IPVGACATAL
QSLEIASDCI LSGKAKVMIA GGFDDISEEG SYEFANMKAT SNAETEFAMG REPTEMSRPA
TTSRAGFMES QGTGVHIVMN AKTALELGAP IRGILAFTST STDKAGRSVP APGRGALTVA
RQVPSKHPSL ILDVAYRSRQ LSFRRSQISQ WLSHEHAQLQ EEIAYRKVEG ETIEDDFFSA
RVANIEAEAV RQEKDALAMY GMLEGSDPHI APLRRALAVW GLTADDIGVL SIHGTSTNAN
EENETRIWND IFTTISRTPG NAVPIVAQKS LLGHSKGGSA AWQMAGLLQS VITGIIPGNR
NSDNIDSHFQ DRQFLMFPSR SIRTDGIRAG VMSSFGFGQV GGTAMVLHPR YLFGALEPTY
YEGYKNRNRV RALQSYKAMS DMMIKNSLVK VKEHPPYIGE MEGKTLLNSM ARTTFDPKTG
EYSFKKLANE VPLDLGNLKA VSDIAAAGGL GVDTPVGVGV DQELISAVPS HNPTFVARNF
TDAEITYCQK QPSPPSSFAA RWAGKEAVFK SLGVKSKGAA AAMKDIEILN DASGVPTVHL
HGDAKAEAEK RGISKVLISL SHSETVAIAF AHASS
//
