ID D8Q3X0_SCHCM Unreviewed; 3927 AA.
AC D8Q3X0;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 80.
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 ORFNames=SCHCODRAFT_82184 {ECO:0000313|EMBL:EFI96697.1};
OS Schizophyllum commune (strain H4-8 / FGSC 9210) (Split gill fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Schizophyllaceae; Schizophyllum.
OX NCBI_TaxID=578458 {ECO:0000313|Proteomes:UP000007431};
RN [1] {ECO:0000313|EMBL:EFI96697.1, ECO:0000313|Proteomes:UP000007431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H4-8 / FGSC 9210 {ECO:0000313|Proteomes:UP000007431};
RX PubMed=20622885; DOI=10.1038/nbt.1643;
RA Ohm R.A., de Jong J.F., Lugones L.G., Aerts A., Kothe E., Stajich J.E.,
RA de Vries R.P., Record E., Levasseur A., Baker S.E., Bartholomew K.A.,
RA Coutinho P.M., Erdmann S., Fowler T.J., Gathman A.C., Lombard V.,
RA Henrissat B., Knabe N., Kuees U., Lilly W.W., Lindquist E., Lucas S.,
RA Magnuson J.K., Piumi F., Raudaskoski M., Salamov A., Schmutz J.,
RA Schwarze F.W.M.R., vanKuyk P.A., Horton J.S., Grigoriev I.V.,
RA Woesten H.A.B.;
RT "Genome sequence of the model mushroom Schizophyllum commune.";
RL Nat. Biotechnol. 28:957-963(2010).
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; GL377306; EFI96697.1; -; Genomic_DNA.
DR RefSeq; XP_003031600.1; XM_003031554.1.
DR STRING; 578458.D8Q3X0; -.
DR GeneID; 9592687; -.
DR KEGG; scm:SCHCO_02627311; -.
DR VEuPathDB; FungiDB:SCHCODRAFT_02627311; -.
DR eggNOG; ENOG502QQJX; Eukaryota.
DR HOGENOM; CLU_000114_2_0_1; -.
DR InParanoid; D8Q3X0; -.
DR OMA; WQVTRKA; -.
DR OrthoDB; 5488314at2759; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000007431; 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; 2.
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:SF21; FATTY ACID SYNTHASE SUBUNIT BETA; 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; 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:UP000007431};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 2217..2299
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 3164..3698
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT REGION 2170..2192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2647..2666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3927 AA; 430111 MW; C9073BC0C83E3A40 CRC64;
MAGSDVSSSA AAISKRPIVV ALGSARLSIP VSTDKDAWIA AEVLRDEFTH DQAAEDAIET
TIELENPHEA AVELAAKFLA YITANLDADQ ESGPARTSVL LHVFKYFTSA YLASKDVHSL
AASFDTDVRK TVLKAYFGAY AALEARAVPD IPKQPQSALL TAAAEGSASV YAIFGGQGTN
EVYFDELQAL YDIYTPFVAA FIRTITEQVL VPLADKEAAS SFYAYGLNVI SWLLDPSSRP
GVPYFASIPL SLPLIGLTQL VQYLVVCRVA GLTPGELRTR IAGATGHSQG IVSAVVIAAS
DSFESYTENA LKAVRWLFYS GLRAQQAFPV VAVEPSIVAD SVEGGEGVPS TMLLVTGLLL
KDVETHLAKT NKHLPSNSKL HISLYNGPKA FVITGPARAL YGLVQNLRKV KAPSGLDQSK
VPFSQRKPVF SVRFLVVNAP YHSEYLTGVT DKVAGEDLAG EELWQAADLK VPVYHTENGS
DLRESKSSIT RELCDQIFTL ALHWDRATNF PETATHAVDF GPGGLSGIGP LTARNLDGRG
VRVIVAGDKG KGDAELFDPT QIKTEQCWSK KWAPKLVKTS DGTIHLDTPF SRLLGKPPIM
VPGMTPSTVQ AGFVSAVLNA GYHIELAGGG HFAPGMLRAK VAEIQKRVAP GVGVTLNALY
INPAQFTFQL PLWQEMRREG LPIEGFCVAA GIPTVEKAAE IISSLQASGI KHVSFKPGSV
EGIRQVVAIA AANPDFPVIM QWTGGRAGGH HSYEDFHAPI LATYRSIRAH DNLILVGGSG
FGSGEDVWPY LTGDWSKEMF GLQPMPFDGF LFGSRVMVAK EAHTSAGVKD LIVAASGVDD
KNWEDTYVKP AGGILTVRSE LGEPIHKVAT RAVKLWKEFD DTVFKLPREK REAWLTERKD
EIIGKLNRDF NKPWFPWKKD DSAAADLSDM TYEEVVLRML RLMYVAHQSR WVDISLRNLT
GDWIRRVEER FAGVNGTGDK PSLLQSYTRL DDPMPFVEEF FAAYPLAKEQ LLATDDAAYF
LAICRRPTQK PVPFIPVLDN QFEFWFKKDS LWAAEDVDAV FDQDPQRVCI LQGPVAVKWS
KVKDEPIKEL LGGINSTLVT RLLERSYNND ESKVPVVDYL AARPKSVPSL HSAKADGKLV
FQTGATVPST TSWLESLAGP ELSWLRALIT SKTIVQGGSY IDNPLRRILI PRPHQKVVVD
YSGDVPSHLS AFGAMRSHGA HDPDFKAVDI AYDAASKNIS LTLFEERRGV SVPLNLEFVY
KPEQGFAPIH EVAEGRNDRI KAFYWKLWYG DDEALPNIDV RDVLKGAEVT IKAEDVEQFC
AVVGNQGEAF KSAREETPMA PMDFAIVTGW QAIIKSIFPS TIDGDLLKLV HLSNGFRMVE
GASPLRVGDV CTAEARILSV VNSDAGKIVK VKGHVLRAGK PVIEVVSAFL YRGKFTDFGN
TFETTEEPDY EVALENDAQV GVLQSKEWFE WDDDTHPLLA GTNLIFRVRT QVSYKDKNSF
SDMEVSGEIF VRNQLKALVK VGTVSFESDE CKGNPVVAYL QRHGKVLNAQ TPLATEYTMS
KEVTPFSAPL TNEPYSKISG DFNPIHINPY FACFASLPCT ITHGLWSSAA TRRYVENVVA
QGHPERVLSY DVSFVGMVLP GDSLKVNIRH VAMRDGNLVV KIVTTNDRDE KVLEGSAEVA
QPPTAYVFTG QGSQEPGMGM DLYNSSPAAR AVWEGADAHL LAVYGFSIVD IVKNNPKEKT
IHFGGIKGQA IRQRYMDMTY DTTDKDGNVK TLPLFADIDI RTAKYTFSHP NGLLFATQFA
QIALVVTEKA AFEDMRVKGF VQKDCPFAGH SLGEYSALAS IADVLHISAL VDVVFYRGIT
MQRAVERDEH NRSNYAMCAV NPSRISKTFT DAALREVVDG IASSTNRLLE IVNFNVEGQQ
YVCAGELVAL QTLTNVLNYL KVKKVDIVQL TQQFSVEKVK EMLGEIIKSS HDSAVEKQKS
DGYIILERGF ATIPLPGIDV PFHSRYLWAG VMPFRTYLSK KINPAHLNPD TLIGKYIPNL
IAQPFDISRE YAQIIYDRTS SPRLDKVLKN WEEEKWGSTE NRQKLAYVIL VELLAYQFAS
PVRWIETQDL LFTDFAFERL VELGPGPTLI GMATRTLKAK YEASDDSVGR KRAILCHAKH
PKEIYYQFED EPEDAPAEEP ASADAPAAPS AAPAAAAAPA PVAAPSGPVA SVEDVPIKPV
DVLAVIVAQK LKKTVNEIPL SKSIKDLVGG KSTLQNEILG DLQLEFTSAP EKGEELPLEE
LGSSLQSGGG LGKHTSGLVS RLIGGKMPGG FNASAIKSYL SKTWGLGPLR ADAVLLLGTT
MEPPKRLASE AEGRAWVDSV VSAYAQRAGI SLAAPGGASG GGGGGAGPTI NSEEFIKFQA
DQQKFAAQHV ELYMRYLGRD SRAGELAFDQ EKANSQALQA KLDSILREHG DTYIDGIQPA
FDPLKARHFN SSWNWARQDA LLMFYDIIFG RLTTVDREIT ARCIRLLNRA DPELITYMQY
YIDKCDPERG ETFKLAKHFG QQLIDNTREV VGKEPLYKDV TFPTAPHTEV TAKGDIVYTE
VVREGVRKLE AYVEEMASTD PVSGSVNIEK VQDDVAKLWT LVKSQPGITE EQKKRIKALY
EGVVRSLRKG PDSPRPRVTP RTRRSSSQFL RPQVSAANVS ADHVPLLHLK RKAGSTWEYS
SNLTGVYLDV LHEIATSGTT FKDKNALLTG VGKGSIGVEV VKGLLSGGAH VVITTSRYSR
STVEYYQDIY QTYGARGSAL TVVPFNQGSK QDVEALVDYI YANLGLDLDY ILPFAGIPEN
GREIDSIDDK SELAHRIMLV NLLRILGAVK SKKASRQFVT RPTQVILPLS PNHGLFGNDG
LYSESKISLE TLFQRWASES WGEYLCLAGA VIGWTRGTGL MGPTNIVAHE LESYGVRTFS
AKEMAFNILG LMHPLLFSIT QVEPIWADLN GGMDRLPDLA EITTKIRTSL MKKAELRRAI
TLDTSADFKI TKGPDAERLL QTVNVLPRAN HRYEFPALES TASLADVSYM QGLLDLDKVI
VVTGFGEVGP WGSSRTRWEM EARGELTIEG CIEMAWIMGF IKHFDGRLKD GTLYVGWVDS
KSSEPVDDKD VKGRYEKEIL AHAGVRLIEP ELFRGYDPKK KVFNQEIELT HDLEPIEVAE
SEAQKFKLQH GDKCDIWAGE EGQWFAKLKK GACVYVPKAF KFSRTVAGQI PTGWSAGRYG
IPDDIVAQTD RVTLWALVCA AEALNQSGIT DPYELYQHIH PSEIGTSLGS GMGGVVSMAK
MFKDRRDEKD VQNDILQETF INTTAGWVNL LLLSSSGPVK IPVGACATAL QSVEIACDTI
LSGKAKVMLA GGFDDLSEEG SYEFANMKAT SNAETEFAMG REPTEMSRPA TSTRSGFMES
QGSGVHVLMS ARTALELGAP IRGIVAFTST STDKAGRSIP APGRGALSIA REVPSTQPLP
ILDIKYRTRQ LEFRRKQISQ WLTHEHYQLQ EEIEFRKQEG AEVTEEELAA RVDSIEKEAA
RQEKDALAVF GMLEGSDPRV APLRRALAVW GLTTDDVGVL SIHGTSTGAN EKNETQIWND
IFKGLSRTPG NAVPIMAQKS LLGHSKGGSA AWQMSGLLQS VYHGIIPGNR NSDNIDPMFQ
DRHFLMFPSK TIYTAGIKAG LMSSFGFGQV GGTVLILHPR FVFGALDPAY YEAYKARNRV
RALQSYKAMS DMMVKHSLVK VKDAPPYTPD LEGKVLMNSL ARTIRNPKTG KFEFGKINST
VKQDTANVKA VSELLSSGGL SESAIGVGVD EELISAVPSH NPTFVERNFT DNEVSYCQAQ
PSPASSFAAR WAGKEAVFKA LGVKSKGAGA AMKDIEILND PETGAPTVVL HGDAKAKAEE
KGVSKVLISL SHSETVAIAF AQASKAA
//
