ID A0A0H2RDM4_9AGAM Unreviewed; 3934 AA.
AC A0A0H2RDM4;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
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=SCHPADRAFT_909290 {ECO:0000313|EMBL:KLO07628.1};
OS Schizopora paradoxa.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Hymenochaetales; Schizoporaceae; Schizopora.
OX NCBI_TaxID=27342 {ECO:0000313|EMBL:KLO07628.1, ECO:0000313|Proteomes:UP000053477};
RN [1] {ECO:0000313|EMBL:KLO07628.1, ECO:0000313|Proteomes:UP000053477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KUC8140 {ECO:0000313|EMBL:KLO07628.1,
RC ECO:0000313|Proteomes:UP000053477};
RG DOE Joint Genome Institute;
RA Min B., Park H., Jang Y., Kim J.-J., Kim K.H., Pangilinan J., Lipzen A.,
RA Riley R., Grigoriev I.V., Spatafora J.W., Choi I.-G.;
RT "Complete genome sequence of Schizopora paradoxa KUC8140, a cosmopolitan
RT wood degrader in East Asia.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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};
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DR EMBL; KQ086128; KLO07628.1; -; Genomic_DNA.
DR STRING; 27342.A0A0H2RDM4; -.
DR InParanoid; A0A0H2RDM4; -.
DR OrthoDB; 5488314at2759; -.
DR Proteomes; UP000053477; 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: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; 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; 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:UP000053477};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 2225..2300
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 3149..3710
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT REGION 2660..2684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3934 AA; 429893 MW; FB0850508D2261CE CRC64;
MASAISNAAT CSNDGLQARP LVIELGKLRI SIPVSTATNE WVAAEILRDD FIHKEKNDGV
VENTAELEDT AEATIELFAR FLAFIADNIK PGTPCATSRT AVLLNAYKAF TTSHLTEKDI
HNFAVSFDVD VRKSVLASYY KAQAALQAQK VSAIPTAPTS ALLTAAKDGS ASVFALFGGQ
GTNEVYFDEL QSLYDIYKPF VAPFLTSLTV NVLQPLAAGS SSTFFAYGLD VISWLAGAPR
PPTEYLASIP VSFPLIGLTQ LTQYLVSCRV AGITPGEMRT RLQGATGHSQ GIVSAVAVAA
SDSFDSFTSN SAKALKWLFF SGVRGQEAFP VLALEPSMVA DSVEGGEGAP TPMLSVAGLS
LSDLEPHIKK TNKHLPSNSQ LSVSLYNGPK TFVVTGPAKA LYGLVTSLRK VRAQPGLDQS
KIPHSQRKPV FSARFLAVGV PYHSEYLSGA TEKVLQDLGE ELWKAKELSI PVYHTEDGSD
LRALSSSLTQ SLCDQIFTKP IHWTVATAFP DSATHAVDFG PGGLSGIGPL TQRNMEGRGV
RVVVVGEKGK GGAELYDSSE IKREVWWAKK WAPKLVKTAD GKIHIDTPFS RLLGKPPIMV
AGMTPTTVKA GFVSAVLRAG YHVELAGGGH YNVKALRSKV NEIQAQIPAG VGLTLNALYI
NPRQFSFQFP LWQEMRKEGI PVEGFCVAAG IPSTEKAVEI IEGLTSAGIK HVSFKPGSVD
GIRQVVNIAA ANPNFPIIMQ WTGGRAGGHH SCEDFHQPIL QTYASIRQHS NIALVGGSGF
GGADDVWPYL TGEWSSKMFG VQPMPFDGFL FASRVMVAKE AHTSSSVKDL IVAASGVDDK
AWEGTYAKET GGILTVRSEL GEPIHKVANR AVKLWKQFDD TVFNMPKEKR GAWLTENREM
VISKLNSDFS KPWFGWKKGD VVVNDLGDMT YEETVLRMVR LMYVAHENRW IDQTLRNLTG
DWLRRIEERF AGVDGTKTKP SLLQTFTAMD EPTDFIKKFF AAYPEATTQL IAAEDKAYFL
AISQRQAQKP VPFIPVLDAN FEVWFKKDSL WAAEDIEAVF DRDPQRVCIL QGPVAVKYCT
KKDEPIADLL GGITSQLTDK LLQSVYGGDK SKVPAADYLG DIPSSSVSVP SGVSFSSKGT
ETTYSIGATV PDTSAWLETL SGPALTWLRA LLASRIIIQG TSFVDNPLRR ICAPRAGQKV
VVDRASDLTP KSLTFYGSAR SHGVHNPDFK TLEISYNSSS KQITVVVHEE RGGVSVPLTL
LFSYRPDMGS APIHEISQGR NSRIKEFYWK LWFGDNSTLP AIGLRDALTG PEVTIDARQV
ERFCAVVGND GEEFKTVRAE DVQAPMDFAI VTGWKAIMQA IFPKSIDGDV LKLVHLSNGF
RMVEGQKPLQ VGDKCKAEAR VIAVINNDSG KVVKVKGSVI RKGQTVIEVV SSFLYRGRFV
DFENTFESEK APVYTVEMKD ESAVGVLQSK EWFQWDDDSK PLKPGVALVF EVRSEVTFRD
KAQYATVVVE GEVFTRDTLN NLIKVATVEF DSDNCQGNPV VAYLKRHGSA EGTVAPLSNE
GYSMTTPGVS TSFTSPLTNE PYSKVSGDFN PIHINPYFAD FAALPGTITH GLWSSAATRR
YLETVVAKGH PERVLSYDVS FVGMVLPGDE LTVDLKHIGM KQGNVVVNVS TTNSRGERVI
EGTAEVAQPT TAYVFTGQGS QEQGMGMDLF NNSTAALAVW EGADAHLLEV YGFSIIDIVK
NNPKMKTIHF GGFKGQVIRQ RYMDMSYDTT DKDGHVKTLP LFADINDRTP QYTFSHPNGL
LFATQFAQIA LVVTEKAAFE DMRSKGLVQK NCPFAGHSLG EYSALASIAD VLPISSLVDI
VFYRGITMQR AVERDEHNRS NYAMCAVNPS RISKTFDDSA LREVVDSISR ETNLLLEIVN
YNVEGQQYVC AGELVALQTL TNVLNYLKVE KVDVAKLAEK FSVEKVKEML ADIIKSCFEK
AKELKKAEGF IKLERGFATI PLPGIDVPFH SRYLWAGVMP FRAYLLKKIN VELINPDTLV
GKYVPNLVAK PFEVNKAYVQ RVYDQTSSPR LDKILKAWDQ EGWGDAEHRQ RLAYTILVEL
LAYQFASPVR WIETQDMLFK HYDFERFIEI GPSPTLTGMA TRTLKAKYEV QDDSIGRKRE
ILCHSKNTKE IYYQFEDEAA AEPEPAAATE VAPAPVAQAA APVAASVAAP SASAGPAASI
PDEPLKAGDT LRIIIAQKLK KSVDEVPLGK SIKDLVGGKS TLQNEILGDL QLEFGSAPEK
SEELPLDELA SGLGSGYSGS LGKYTSGLIS RLVGSKMPGG FNMSAVKAHL SKAWGLGSSR
SDAIMMLGLT MEPPKRLGSE PEAKAWLDSI VPIYAQRAGI SLSQGGSAAA GGGASGGAVI
NSEEFTKFQS QQGQFVGQQV EVLMRYLGKD SRAGEAAFAK EKENANELQQ KLDSIAKEHG
DAYIEGIQPS FDALKARHFD SSWNWVRQDA LLMFYDILFG KLKTVDREIT ARCISIMNRA
DPTLLAYMQY HIDKVDPERG STYKLAKEFG QQLIDNCREV IGEAPLYKDV TFPTAPHTLV
TERGDIVYSE VVRENVRKLE AYVEEMASGD TIPGTFNMQK VQDDVLKLWN VVKSQSEISQ
DQKNKIKALY DGVVRSLKKT PEVRQRSAPT TRHRRSSSQF LRPQVPSLAS VPSDKVPLLH
LKRKVGTSWE YSSNLTGVYL DVLSEIATSG TTFKDKNALL TGVGKGSIGC EILKGLLSGG
AHAVVTTSRY SRATVEYYQD IYQRYGSRGS ALTVVPFNQA SKQDVEALID YIYGTLGLDL
DYVLPFAAVP ENGRQIDGLD DKSELAHRIM LVNVLRLLGA VKTKKASRHF VTRPTQVILP
LSPNHGLFGN DGLYSESKIS LETLFARWNS ESWGEYLCLA GAVIGWTRGT GLMDQTNMVA
QQIESYGIRT FSAKEMAFNI LGLMHPLLFS ITQVEPIWAD MSGGMDRLPD LAEITNKIRS
TLNQQAELRK AITRDTSLDF AVINGGEAER VLQTVSVSPR ANFKFEFPAL ESKEALADVS
KLEGLLDLDK VVVVTGFGEV GPWGSSRTRW EMEARGEFTI EGCIEMAWIM GYIKHFDGRL
PDGNLYVGWV DAKSGDPVDD KDVRAKYEKE ILAHAGVRLI EPEIFNGYDP KKKIFNQEIE
LIHDLEPMEV SEEEAEKFKY EHGDKCDIWA SEGGEWYVKL KKGARVFVPK AVRFSRLVAG
QIPSGWHAGR YGIPQDIIDQ VDRATLWALV SAAEALNASG ITDPYELYKY MHPSEVGTAI
GSGMGGVESM RQMFRERRDC VEVQNDVLQE TFINTTAGWI NLLLLSSSGP IKIPVGACAT
ALQSIEIACD TLLSGKAKVM LAGGHDDTSE EGSFEFAQMK ATSNAETEFA MGREPTEMSR
PTTTTRAGFM ESMGSGVHVL MTAKTALQIG APIRAVVAFT STSTDKAGRS VPAPGRGALT
IAREIPSKHL PPILDIGYRT RQLSFRRKQI SQWLSNEHDM LRDEIEVRKS QGEKVDDEYV
SNRVAQIEGE ASRQEKDALS IYGMLDGSDP HISPLRRALA VFGLTVDDIG ILSIHGTSTQ
ANEANETHIW NDILEKLGRS KGNAVPIMAQ KYLCGHAKGG SAAWQLAGLV QTVASGTVPG
NRNADNVDSE FRQYEHLLFP SKTIQTDGIR AGVMTSFGFG QVGGSVLILH PRYVFGAVGA
NDYESYKIRN RERALSCYKA MTSMMTTNSL VRVKDAPPYT KDLELPVLMN SMARATLDQK
SGNYVFSKKL STKPDYNLAN VDAAMKSLSS APGTVGVGVD HELISAVPSS NPTFVSRNFT
DAEVRYCRSQ PSPAASFAAR WAGKEAVFKS LGVSSKGAGA GMKDIEILPD ASGVPTVALH
GEAKSAAGAK GVKSVLVSLS HSESVAIAFA QASA
//
