ID A0A0W8D0P6_PHYNI Unreviewed; 3829 AA.
AC A0A0W8D0P6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=AM587_10006936 {ECO:0000313|EMBL:KUF89968.1};
OS Phytophthora nicotianae (Buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4790 {ECO:0000313|EMBL:KUF89968.1, ECO:0000313|Proteomes:UP000052943};
RN [1] {ECO:0000313|EMBL:KUF89968.1, ECO:0000313|Proteomes:UP000052943}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 0 {ECO:0000313|Proteomes:UP000052943};
RA Liu H., Ma X., Yu H., Fang D., Li Y., Wang X., Wang W., Dong Y., Xiao B.;
RT "Genomes and virulence difference between two physiological races of
RT Phytophthora nicotianae.";
RL Submitted (NOV-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};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000256|ARBA:ARBA00005005}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUF89968.1}.
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DR EMBL; LNFO01001599; KUF89968.1; -; Genomic_DNA.
DR STRING; 4790.A0A0W8D0P6; -.
DR EnsemblProtists; KUF89968; KUF89968; AM587_10006936.
DR OMA; APLVHGM; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000052943; Unassembled WGS sequence.
DR GO; GO:0005835; C:fatty acid synthase complex; IEA:InterPro.
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:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IEA:InterPro.
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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; cd08950; KR_fFAS_SDR_c_like; 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; 6.10.60.10; -; 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; 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; IPR002539; MaoC-like_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
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; 2.
DR Pfam; PF18314; FAS_I_H; 1.
DR Pfam; PF17951; FAS_meander; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 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; 1.
DR SUPFAM; SSF53901; Thiolase-like; 2.
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 NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000052943};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 3054..3568
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
SQ SEQUENCE 3829 AA; 421549 MW; A2157EC53493A782 CRC64;
MSDTNTLLDV DKYKFIPEFG GQGISYWSEL QRLYVSSKGT TRSFLDTAVQ ALLEESGTDE
AQRSVAFEAV IDLKDWLQRD SLEGLELNRV FFSMPMLMLT QCANYLNFLE ATGVTHGGMV
TNSTTAIGHS QGVVSAVVFS AAKTIEEFQE LGVAMLRYMF WQGLRTQEAY LELLEQHNQK
NGSSSPMLAV RGLKQEQVLE TIESQAEMPD LHLALINASD LINVTGFPAS LRTLKQTLEG
IMAGSDVDQT RVPYSQRKPT GSLSFLPLSA PFHTPLLSAA VPKVLQDVQR LRFTLKGSHL
QVPVYATDMD ANNLQTVDDV IEEIIKLQLL QPVDWTSTWS KIAELHPDAT HVLEFGPDLG
VAKLSNKPAE GLGIEVIIAT AKHPIMDLSM QVVGLQQFID AAPTFTSKKK TWAEKFGLQV
TKSGDLYNNF TRVLNKPPVM VAGMMPTTSL EGIDLVAAIQ NAGFHAELAA GGLSRSNIFE
NAVTDLVSKL KPGHGISINM LYLNAKQWGF QFPMVLRMRR SEVPIESVTI GAGVPTKERG
LEILTQLQAV GIHLVSFKPG SVDGIHSVLE IATAVPTMTV MIQWTGGRAG GHHSFEDFHQ
PMEEMYAAIR RVSNVLLVVG SGFGNWEDSV QYLTGEWSLT RGYPYRMPVD GILLGSRVMV
AKEAATAPEV KQLLVNTPGI EESEWETSYS GVVGGLITVS SELGEPIHVV ASRWALLWKE
FDDKYFSLPR EQLELALRLN KKDIITRLNA DYQKPYFGCK IDAETVEIVP ADLEQMTYGE
VLSRMIDLMS VEIPVKPQRW LDESYFSRFS DFLVRTEQRF HRQGSDDIFA TTELKMNPRG
ALEAFVAKYP QVASTLMSVL DCEFFLELCR SGGKPVNFMP VIDAEFKTWF KKDSLWYSED
LDAVPERDEQ RVLILQGPVA VRHSTIMDEP VADILTGIVD GFASTVSEDV AVGGTIKQAI
NIASVQVTES QASMEYSISA LVSANEWLTA LAASVMDKDW LNAVISSNHV VENKKWVPNP
IRQLLMPQIG QKYVVNAAGI RVFDSSINMS GPVIEITKKH ANISVIVSEV RPAVADLKAD
VVTLEMTFTY HSEMSCSIHA EGSDYIDKVK AFYARFWVAI EDKEEESCKA ACTASVKDSF
MTNFAVTKED IIAYRTALGL KCDEVGAPVD FSTVVSWRAL IQSVLANEVK GNLLNLVHLK
HSYKLLSSRK YSAMFLPGDD IVSTAKVASL RIIDSGKIVH SMATISRRAL NDDMEVFEPL
VELHSEFLIR GCFTDFESTF SVEETKHEFV LKDAEELKTK TWLKLAAETS VNVGDRLALQ
LTTKRQYASI SSLSSLEVSG VLFRGEAGTT VEIGAVEFKS DEVNESPITA FLRQVQLETS
GVFVNNGSYM LETPLEINVP TNALAYAVAS RDLNPIHRSN YAAILAGLKG KPIMHGMWTA
TKVRDLVTQS FSQGLDSNVV EYEVSFDGMV YPGDKLFMQA RHVGQKNGNK ILSIEVVNSS
SERVITARAV VKQRPTAFVF TGQGSAEVGM GMNRYQESPI AREIWDRGDR HLLNMFGFSI
LDIVHNNPKS ITVYFGGKKG RRIREKYMSL TCEDPTTGET VPLLPEINTR TQSFTFSLPE
GLLFATQFNQ PAIVLLEKAM FSEIEDAQLI PSDAFFAGHS LGEYAGLSSF AGVLALEDVV
EVVFLRGLIM QRAVKRDAEG RSDYGMVAAN PMRVGSHMTE ELLYTIVQGI EAASGKLLQV
VNFNVQQYQY VVAGDSVNLE TLSLGLAAFK TLKSTESEDV DKIIMYSLEQ ARARKEECEQ
RGRPFMLTRG LATIPLPGID VPFHSRELLS GVPSFRELLR TKFDPHVLER QLPLLEGRYI
PNLVATPFSL ERSYFQKVYA ATRSRYLAEI LDSKKWESAS KAQLAHLLMV ELLAYQFASP
VQWIKTQQLL FSQGGVHRFV EIGPAPALTN MALRTLEIGD YPNVPREIFW YQRDREAVHF
EEETSNISAF EHVRGLAGEV IATEPVPKVE EVLAPAPVAA VPVQQIQAAL APAPDAPVAA
LHVLRVFLAV RLNKDLAEIR EDTDVKTLCA GKSAVQNEIL GDLEKEFGSV TEDAGEMPLK
ELESKFSGYK TLGKTRVKSD ADARKWLDET MKDYASCAGI SLDCPTVAAT SDAVGMSFNP
VPVSIPTVSG KPVEAKHSLL VMLAAKFGKA FNEILETATI KELAAGKSAM QNEIVGDVEK
EFGSVPDDAA EMKLVELAGT FVDYASPGRA TSALIAKMLA SKMPGGFGLS AIKEYLSSER
CLPSGRVDSV LLHGLTQNPK LRLTDDAAAK TWLDGVADDY ALYSGIEIPY LSKLGGMMAA
PALGQQVIQS SSLSRDFEKR LKTMIADQVD ALNSFLGEDK LDWHRQLEAE VGVRQYAESS
MSQWLTEHDE SYTAGITGKF DAKKERQYDS YWNWAVQDMM ELYYGSMLED RSGDPALERA
KLYVHNRATP ELLQCIQFFS SRAEKEGRSE LAETFRLLAG QVQDGVNTDP VNIQLFTPTQ
PQLRVREDGE LEYSEVPRIG VGDSSSYVDE VARGLEYDNV ETETLAGSGI TSESLKNIVL
PHVHVRKPSD VDPTFRLYDV ESTCVLLSCM REMASTGISF AGKVALLTGC GKNSIGVEIV
KALLEGGATV FVATSSFSMM TTGVFREMYQ QHGSRGSRLI VLPFNQASKT DVQGLVTHIY
SVHKLDLDCV IPFAALSEVG RTITDIDSRS ELAHRIMLTN IVRLLGEVVT AKKTRGITTR
PALVILPMSP NHGDFGGDGL YAESKLGMES LMSKWRSEDW SEQLSIIGAV IGWTRGTGLM
SSNNVVAADV EKMGVRTFSM TEMGFNLSAL LHPTMVDRAA DAPIYVDFSG GMAQVSGLKD
QVDAIRMKIM KTAKLKTAIH ADKRKTKHLK VLPRANLSSY YCNTFPNLAN VAGLSASSKQ
ELMRGMLDLR QVVVVTGFGE VSPWGNSRTR WEMESYGEFS LEGCIELAWL TGRIVLKGGN
WVDAKTEEIV SDHQVKARYE EDILNHAGIR IVXPELFDGY DPKNKMVLXX XAIDKKMSPI
XVAXREXALQ FRKELGKDNV DVFQSASGAW MICLRKGSVL NIPRALNFDR FVAGQIPTGW
SAERLGLPKD IAESVDPITL YALASTMDAF VAAGMTDPYE FYQYVHVSEV GNTSGGGMGG
FRAYSQIYKG RLLGKPAPSD XXQXCFINTP PAWVNMLXLS SSGPIKTPVG ACATAAESVD
IAVETIKNGK ARVCIVGGYD DFGEESAFEF AQMKATSDSV KEMSMGREPK EMCRPCSSTL
DGFMESHGAG IQLLMDAQLA LDMGLPIYGI IALANTATDK IGRSIPAPGQ GILTTARETV
AKLSPLLDVE YRHRQFDDEL ESIEKWFARE KMLVDVDDTR LKLLDEIKER KVKAAQAMYG
ESFYVGRTDI APLRGALSVW NLDVDDLGAA SFHGTGTKAN DKNESEVTHK QMTHLGRSPG
NPLSVICQKS ITGHPKGAAA AWQLNGLLQV LNTGLIPGNR QLDNTWEMLR KYNHLVYPNR
SLQTNGIKAV LLKSFGFGQA SGELLVVHPD YLLSTLSVVD FQQYSARREK RLVKMNTHAQ
SVITGKKPHI QVKNEAPYSS AMESSVYLDP TARAQYDAVS QTWRFGGTAA SQRRHRVKRG
KKTNTIKLVH SKKTSKLDSS SSLLAAIGNT AIELGLSKNM SVGVDVQPVA TFESLNDRED
FIRRNFSDQE SAYCYSAPHP AASFAARWAV KEAVIKAISS VAPTESYLWQ GAEASRRDIE
VVMTASGAPT VQLSGYPLHI FDRLELAKLS VSISHSGAFA VAQVVASFE
//
